A group of leading international scientists is calling for a global conversation about the potential creation of "mirror bacteria"—a hypothetical form of life built with biological molecules that are the opposite of those found in nature.

In a new report published today in the journal , the researchers, including Professor Patrick Cai, a world leader in synthetic genomics and biosecurity, from The University of Manchester, explain that these mirrored organisms would differ fundamentally from all known life and could pose risks to ecosystems and human health if not carefully managed.

Driven by scientific curiosity, some researchers around the world are beginning to explore the possibility of creating mirror bacteria, and although the capability to engineer such life forms is likely decades away and would require major technological breakthroughs, the researchers are calling for a broad discussion among the global research community, policymakers, research funders, industry, civil society, and the public now to ensure a safe path forward.

Professor Cai said: “While mirror bacteria are still a theoretical concept and something that we likely won’t see for a few decades, we have an opportunity here to consider and pre-empt risks before they arise.

“These bacteria could potentially evade immune defences, resist natural predators, and disrupt ecosystems. By raising awareness now, we hope to guide research in a way that prioritises safety for people, animals, and the environment."

The analysis is conducted by 38 scientists from nine countries including leading experts in immunology, plant pathology, ecology, evolutionary biology, biosecurity, and planetary sciences. The publication in is accompanied by a detailed 300-page .

The analysis concluded that mirror bacteria could broadly evade many immune defences of humans, animals, and potentially plants.

It also suggests that mirror bacteria could evade natural predators like viruses and microbes, which typically control bacterial populations. If they were to spread, these bacteria could move between different ecosystems and put humans, animals, and plants at continuous risk of infection.

The scientists emphasise that while speculative, these possibilities merit careful consideration to ensure scientific progress aligns with public safety.

Professor Cai added: “At this stage, it’s also important to clarify that some related technologies, such as mirror-image DNA and proteins, hold immense potential for advancing science and medicine. Similarly, synthetic cell research, which does not directly lead to mirror bacteria, is critical to advancing basic science. We do not recommend restricting any of these areas of research. I hope this is the starter of many discussions engaging broader communities and stakeholders soon. We look forward to hosting a forum here in 91ֱ�� in autumn 2025.”

Going forward, the researchers plan to host a series of events to scrutinise their findings and encourage open discussion about the report. For now, they recommend halting any efforts toward the creation of mirror bacteria and urge funding bodies not to support such work. They also propose examining the governance of enabling technologies to ensure they are managed responsibly.

, which aims to improve the way prosthetics for people who have suffered traumatic limb loss work, wowed the judges at the (iGEM) 2024 Grand Jamboree.

The non-profit iGEM Foundation hosts an international student competition each year to promote education and collaboration among new generations of synthetic biologists.

Human-machine interfaces are becoming more advanced, with new technologies harnessing the body’s electric signals to control devices.

Artificial limbs, known as myoelectric prosthetics, are directed by electrical signals generated by muscle contractions in the residual limb, which can be translated to motion.

However, heavy batteries and motors in myoelectric prosthetics can cause excessive sweating and make the electrodes slip from their contact points, resulting in discomfort and imprecise limb movement.

To solve the problem, the team proposed using synthetic biology to create tiny specially designed wires that work with skin cells.

They engineered a type of bacteria – Escherichia coli – to express tiny, hair-like structures known as pili (e-pili) found on electricity conducting bacteria called Geobacter sulfurreducens.

By combining the Escherichia coli with a protein-binding peptide, the team created nanowires that specifically target and bind to proteins at the skin’s surface, potentially enhancing the precision of an artificial limb.

The 91ֱ�� iGEM team were Damian Ungureanu, Devika Shenoy, Francisco Correia, Janet Xu, Jia Run Dong, Usrat Nubah, Yuliia Anisimova, and Zainab Atique-Ur-Rehman.

, said: “I’m delighted our team won gold at the iGEM 2024 Grand Jamboree for an innovation which could make a difference for people who need artificial limbs.

She added: “I have supervised the 91ֱ�� iGEM teams together with Professor Rainer Breitling since 2013.

“Our teams, based in the (MIB), have been very successful and have achieved a gold medal all but one of the years that we participated - which is quite an achievement.

“In 2016, the team also scooped the special award for ‘Best Computational Model’ and were shortlisted for the ‘Best Education and Public Engagement’ award.”

This year’s 91ֱ�� iGEM team worked in the MIB labs throughout the summer, with financial and logistical support from the MIB, School of Biological Sciences, School of Social Sciences/Department of Social Anthropology, School of Arts Languages and Cultures, and the Future Biomanufacturing Research Hub.

The team also worked with the (AMBS) to comprehensively explore the social and economic implications of their ideas using a (RRI) approach.

The competition provides an interdisciplinary learning opportunity for students outside biology, by encouraging participants to think beyond their lab work.

Damian Ungureanu, second year Biochemistry student, said: “Working with people from different cultural and academic backgrounds has allowed me to substantially develop my communication skills. Even though this was a synthetic biology project, the human practices aspect was just as important as the science. Winning the gold medal felt like the culmination of one year of hard work.”

Devika Shenoy, second year Biomedical Sciences student, said: “I am grateful to have gotten the opportunity to work with so many like-minded individuals and under the guidance of skilled advisors and PIs. iGEM has truly broadened my horizons and understanding of how science and synthetic biology can be used to solve world issues.”

Biocatalysis is a process that uses enzymes as natural catalysts to carry out chemical reactions. Scientists at The University of Manchester and AstraZeneca have developed a new biocatalytic pathway that uses enzymes to produce nucleoside analogues, which are vital components in many pharmaceuticals used to treat conditions like cancer and viral infections.

Typically, producing these analogues is complicated, time consuming and generates significant waste. However, in a new breakthrough, published in the journal , the researchers have demonstrated how a "biocatalytic cascade" — a sequence of enzyme-driven reactions — can simplify the process, potentially cutting down production time and reducing environmental impact.

The researchers engineered an enzyme called deoxyribose-5-phosphate aldolase, enhancing its range of functions to efficiently produce different sugar-based compounds, which serve as building blocks for nucleoside-based medicines, such as oligonucleotide therapeutics. These building blocks were combined using additional enzymes to develop a condensed protocol for the synthesis of nucleoside analogues which simplifies the traditional multi-step process to just two or three stages, significantly improving efficiency.

With further refinement, this method could help streamline the production of a wide range of medicines, while significantly reducing their environmental footprint. The team are now continuing this work with the MRC funded , which looks to develop sustainable biocatalytic routes towards functionalised nucleosides, nucleotides and oligonucleotides.

The Centre for Innovative Recycling and Circular Economy (CIRCLE) UK team will be led by Dr , Reader is Sustainable Biotechnology at the 91ֱ�� Institute of Biotechnology, alongside a team of international academics. Also part of the project are Professors and , and Drs , and Micaela Chacon.

CIRCLE aims to address the global challenge of anthropogenic waste by closing the loop and using it as a feedstock for the chemicals industry. Much of the waste produced by society is a rich source of carbon, a building block for many important chemicals and materials found in everyday products such as plastics, personal care products, and pharmaceuticals. CIRCLE will identify and employ novel biotechnological processes to break down this waste into its chemical components and avoid the need for virgin petrochemical feedstocks.

This project will bring together academic expertise from across the globe, including the US, Canada and South Korea.

The 2024 Global Centres awards focus on advancing bioeconomy research to solve global challenges, whether by increasing crop resilience, converting plant matter or other biomass into fuel, or paving the way for biofoundries to scale-up applications of biotechnology for societal benefit.  The programme supports holistic, multidisciplinary projects that bring together international teams and scientific disciplines, including education and social sciences, necessary to achieve use-inspired outcomes. All Global Centres will integrate public engagement and workforce development, paying close attention to impacts on communities.

“Alongside replacing fossil fuels, there is an urgent need to replace petrochemical industrial feedstocks across a wide range of sectors. This is a global challenge that requires global solutions and UKRI is delighted to be partnering in the NSF Global Centres 2024 programme to meet this need”, said UKRI CEO, Professor Dame Ottoline Leyser. “The announcement today will be at the forefront of real-world solutions, from improved recycling to new bioplastics, building a sustainable circular economy. The centres will create the global networks and skills needed to drive a thriving bioeconomy benefitting all.”

These findings have the potential to accelerate the discovery of novel, more efficient cryoprotectants - and may also allow for the repurposing of molecules already known to slow or stop ice growth.

Professor Matthew Gibson, from 91ֱ�� Institute of Biotechnology at The University of Manchester, added: “My team has spent more than a decade studying how ice-binding proteins, found in polar fish, can interact with ice crystals, and we’ve been developing new molecules and materials that mimic their activity. This has been a slow process, but collaborating with Professor Sosso has revolutionized our approach. The results of the computer model were astonishing, identifying active molecules I never would have chosen, even with my years of expertise. This truly demonstrates the power of machine learning.”

The full paper can be read .

Sugars play a crucial role in human health and disease, far beyond being just an energy source. Complex sugars called glycans coat all our cells and are essential for healthy function. However, these sugars are often hijacked by pathogens such as influenza, Covid-19, and cholera to infect us.

One big problem in treating and diagnosing diseases and infections is that the same glycan can bind to many different proteins, making it hard to understand exactly what’s happening in the body and has made it difficult to develop precise medical tests and treatments.

In a breakthrough, published in the journal , a collaboration of academic and industry experts in Europe, including from The University of Manchester and the University of Leeds, have found a way to create unnatural sugars that could block the pathogens.

The finding offers a promising avenue to new drugs and could also open doors in diagnostics by ‘capturing’ the pathogens or their toxins.

, a researcher from at The University of Manchester, said “During the Covid-19 pandemic, our team introduced the first lateral flow tests which used sugars instead of antibodies as the ‘recognition unit’. But the limit is always how specific and selective these are due to the promiscuity of natural sugars. We can now integrate these fluoro-sugars into our biosensing platforms with the aim of having cheap, rapid, and thermally stable diagnostics suitable for low resource environments.”

Professor Bruce Turnbull, a lead author of the paper from the School of Chemistry and Astbury Centre for Structural Molecular Biology at The University of Leeds, said “Glycans that are really important for our immune systems, and other biological processes that keep us healthy, are also exploited by viruses and toxins to get into our cells. Our work is allowing us to understand how proteins from humans and pathogens have different ways of interacting with the same glycan. This will help us make diagnostics and drugs that can distinguish between human and pathogen proteins.”

The researchers used a combination of enzymes and chemical synthesis to edit the structure of 150 sugars by adding fluorine atoms. Fluorine is very small meaning that the sugars keep their same 3D shape, but the fluorines interfere with how proteins bind them.

, a researcher from 91ֱ�� Institute of Biotechnology at The University of Manchester, said “One of the key technologies used in this work is biocatalysis, which uses enzymes to produce the very complex and diverse sugars needed for the library. Biocatalysis dramatically speeds up the synthetic effort required and is a much more green and sustainable method for producing the fluorinated probes that are required.”

They found that some of the sugars they prepared could be used to detect the cholera toxin – a harmful protein produced by bacteria – meaning they could be used in simple, low-cost tests, similar to lateral flow tests, widely used for pregnancy testing and during the COVID-19 pandemic.

Dr Kristian Hollie, who led production of the fluoro-sugar library at the University of Leeds, said: “We used enzymes to rapidly assemble fluoro-sugar building blocks to make 150 different versions of a biologically important glycan. We were surprised to find how well natural enzymes work with these chemically modified sugars, which makes it a really effective strategy for discovering molecules that can bind selectively.”

The study provides evidence that the artificial “fluoro-sugars” can be used to fine-tune pathogen or biomarker recognition or even to discover new drugs. They also offer an alternative to antibodies in low-cost diagnostics, which do not require animal tests to discover and are heat stable.

The research team included researchers from eight different universities, including 91ֱ��, Imperial College London, Leeds, Warwick, Southampton, York, Bristol, and Ghent University in Belgium.

The breakthrough, published in the journal , could significantly improve accessibility of essential protein-based drugs in developing countries where cold storage infrastructure may be lacking, helping efforts to diagnose and treat more people with serious health conditions.

The researchers, from the Universities of Manchester, Glasgow and Warwick, have designed a hydrogel – a material mostly made of water – that stabilises proteins, protecting its properties and functionality at temperatures as high as 50°C.

The technology keeps proteins so stable that they can even be sent through the post with no loss of effectiveness, opening up new possibilities for more affordable, less energy-intensive methods of keeping patients and clinics supplied with vital treatments.

Protein therapeutics are used to treat a range of conditions, from cancer to diabetes and most recently to treat obesity and play a vital role in modern medicine and biotechnology. However, keeping them stable and safe for storage and transportation is a challenge. They must be kept cold to prevent any deterioration, using significant amounts of energy and limiting equitable distribution in developing countries.

The medicines also often include additives – called excipients – which must be safe for the drug and its recipients limiting material options.

The findings could have major implications for the diagnostics and pharmaceutical industries.

, is one of the paper’s corresponding authors. He said: “In the early days of the Covid vaccine rollout, there was a lot of attention given in the news media to the challenges of transporting and storing the vaccines, and how medical staff had to race to put them in people’s arms quickly after thawing.  

“The technology we’ve developed marks a significant advance in overcoming the challenges of the existing ‘cold chain’ which delivers therapeutic proteins to patients. The results of our tests have very encouraging results, going far beyond current hydrogel storage techniques’ abilities to withstand heat and vibration. That could help create much more robust delivery systems in the future, which require much less careful handling and temperature management.”

The hydrogel is built from a material called a low molecular weight gelator (LMWG), which forms a three-dimensional network of long, stiff fibres. When proteins are added to the hydrogel, they become trapped in the spaces between the fibres, where they are unable to mix and aggregate – the process which limits or prevents their effectiveness as medicines.

The unique mechanical properties of the gel’s network of fibres, which are stiff but also brittle, ensures the easy release of a pure protein. When the protein-storing gel is stored in an ordinary syringe fitted with a special filter, pushing down on the plunger provides enough pressure to break the network of fibres, releasing the protein. The protein then passes cleanly through the filter and out the tip of the syringe alongside a buffer material, leaving the gel behind.

In the paper, the researchers show how the hydrogel works to store two valuable proteins: insulin, used to treat diabetes, and beta-galactosidase, an enzyme with numerous applications in biotechnology and life sciences.

Ordinarily, insulin must be kept cold and still, as heating or shaking can prevent it from being an effective treatment. The team tested the effectiveness of their hydrogel suspension for insulin by warming samples to 25°C and rotating them at 600 revolutions per minute, a strain test far beyond any real-world scenario. Once the tests were complete, the team were able to recover the entire volume of insulin from the hydrogel, showing that it had been protected from its rough treatment.

The team then tested samples of beta-galactosidase in the hydrogel, which was stored at a temperature of 50°C for seven days, a level of heat exceeding any realistic temperature for real-world transport. Once the enzyme was extracted from the hydrogel, the team found it retained 97% of its function compared against a fresh sample stored at normal temperature.

A third test saw the team put samples of proteins suspended in hydrogel into the post, where they spent two days in transit between locations. Once the sample arrived at its destination, the team’s analysis showed that the gels’ structures remained intact and the proteins had been entirely prevented from aggregating.

is the paper’s other corresponding author. He said: “Delivering and storing proteins intact is crucial for many areas of biotechnology, diagnostics and therapies. Recently, it has emerged that hydrogels can be used to prevent protein aggregation, which allows them to be kept at room temperature, or warmer. However, separating the hydrogel components from the protein or proving that they are safe to consume is not always easy. Our breakthrough eliminates this barrier and allows us to store and distribute proteins at room temperature, free from any additives, which is a really exciting prospect.”

The team are now exploring commercial opportunities for this patent-pending technology as well as further demonstrating its applicability. 

Researchers from the University of East Anglia and Diamond Light Source Ltd also contributed to the research. The team’s paper, titled ‘Mechanical release of homogenous proteins from supramolecular gels’, is published in Nature.

The research was supported by funding from the European Union’s Horizon 2020 programme, the European Research Council, the Royal Society, the Engineering and Physical Sciences Research Council (EPSRC), the University of Glasgow and UK Research and Innovation (UKRI).

Peptides are comprised of small chains of amino acids, which are also the building blocks of proteins. Peptides play a crucial role in our bodies and are used in many medicines to fight diseases such as cancer, diabetes, and infections. They are also used as vaccines, nanomaterials and in many other applications. However, making peptides in the lab is currently a complicated process involving chemical synthesis, which produces a lot of harmful waste that is damaging to the environment.

In a new breakthrough, published in the journal , 91ֱ�� scientists have discovered a new family of ligase enzymes – a type of molecular glue that can help assemble short peptide sequences more simply and robustly, yielding significantly higher quantities of peptides compared to conventional methods.

The breakthrough could revolutionise the production of treatments for cancer and other serious illnesses, offering a more effective and environmentally friendly method of production.

For many years, scientists have been working on new ways to produce peptides. Most existing techniques rely on complex and heavily protected amino acid precursors, toxic chemical reagents, and harmful volatile organic solvents, generating large amounts of hazardous waste. The current methods also incur high costs, and are difficult to scale up, resulting in limited and expensive supplies of important peptide medicines.

The team in 91ֱ�� searched for new ligase enzymes involved in the biological processes that assemble natural peptides in simple bacteria. They successfully isolated and characterised these ligases and tested them in reactions with a wide range of amino acid precursors. By analysing the sequences of the bacterial ligase enzymes, the team identified many other clusters of ligases likely involved in other peptide pathways.

The study provides a blueprint for how peptides, including important medicines, can be made in the future.

, who also worked on the project said, “The ligases we discovered provide a very clean and efficient way to produce peptides. By searching through available genome sequence data, we have found many types of related ligase enzymes. We are confident that using these ligases we will be able to assemble longer peptides for a range of other therapeutic applications.”

Following the discovery, the team will now optimise the new ligase enzymes, to improve their output for larger scale peptide synthesis. They have also established collaborations with a number of the top pharmaceutical companies to help with rolling out the new ligase enzyme technologies for manufacturing future peptide therapeutics.

Dr Selena Lockyer, Professor Matthew Gibson, Professor Sarah Lovelock and the Functional Framework Materials: Design and Characterisation Team, led by and Professor Sihai Yang have all been recognised with a prize this year.

Dr Selena Lockyer has been named winner of the Royal Society of Chemistry’s Dalton Emerging Researcher Prize for her synthetic and spectroscopic studies of molecular magnets, particularly supramolecular assemblies that could be used in quantum information processing. Dr Lockyer will also receive £3000 and a medal.

Dr Lockyer investigates the properties of individual electrons at the molecular level and how they can interact with one another and relay or store information. This is done at the National Service for Electron Paramagnetic Resonance Spectroscopy at The University of Manchester.

Apart from making devices smaller, quantum devices possess other advantages. One such phenomenon is known as a superposition state that can be used in quantum bits (qubits), which a standard classical bit – the ones in our laptops – is unable to achieve.

A quantum computer will help us address society's challenges by modelling and developing solutions for climate change, sustainability and energy sources, medical conditions, and how to make a more efficient and better quantum computer.

After receiving the prize, Dr Lockyer said: “It’s such an honour and privilege to receive this award. Unexpected, as there are so many up-and-coming scientists working on numerous research areas, which makes this all the more special. When you look back at the list of previous winners, it is overwhelming to now be part of this.”

has been named winner of the Royal Society of Chemistry’s Corday-Morgan Prize.

Professor Gibson won the prize for transformative contributions in polymer and biomaterials science, particularly for the development of materials to stabilise biologics. Professor Gibson will also receive £5000 and a medal.

Storing and transporting biological materials is crucial to modern life, from frozen food to the safe delivery of blood transfusions, stem cells, or even organs. Professor Gibson and his team have learned from some of nature’s toughest organisms, which can survive sub-zero temperatures, to develop new materials which can protect biopharmaceuticals against cold stress.

After receiving the prize, Professor Gibson said: “I’m honoured to be recognised for the work we have done in my team to develop new tools to help us stabilize biologics against cold stress and to join a such a distinguished list of former awardees.”

has been named winner of the Royal Society of Chemistry’s Harrison-Meldola Prize.

Dr Lovelock won the prize for the development of innovative biocatalytic approaches to produce therapeutic oligonucleotides. She also receives £5000 and a medal.

Therapeutic oligonucleotides are a new class of RNA-based molecules that have the potential to treat a wide range of diseases. However, the rapidly growing number of therapies approved and in advanced clinical trials is placing unprecedented demands on our capacity to manufacture oligonucleotides at scale.

Biocatalysis is an exciting technology that is widely used across the chemical industry: this is where enzymes are used to convert starting materials into high-value products. Dr Lovelock’s group is developing biocatalytic approaches to produce therapeutic oligonucleotides in a more sustainable and scalable way.

One strategy they have developed produces complex oligonucleotide sequences in a single operation using polymerases and endonucleases (nature’s enzymes). These enzymes work together to amplify complementary sequences embedded within a catalytic template. The group is working in partnership with industry to translate their approaches into manufacturing processes.

After receiving the prize, Dr Lovelock said: “I am delighted to have been awarded the 2024 Harrison-Meldola Memorial Prize. I am very grateful to my talented research group. It is their hard work, great ideas, and dedication that has made this award possible.”

The Functional Framework Materials: Design and Characterisation Team have been named winners of the Royal Society of Chemistry’s Horizon Prize, which celebrates discoveries and innovations that push the boundaries of science.

The team is a collaboration between The University of Manchester, Oak Ridge National Laboratory, Diamond Light Source, ISIS Neutron and Muon Source STFC, Berkeley Advanced Light Source, Peking University, Xiamen University and the University of Chicago.

They were awarded the prize for seminal contributions to in situ and operando characterisation of porous materials and catalysts for the binding, capture and separation of fuels, hydrocarbons, and pollutants. The team receive a trophy and a video showcasing their work, and each team member receives a certificate.

Metal-organic frameworks (MOFs) are porous materials that can capture and store important fuels like hydrogen, methane, and ammonia, hydrocarbons (ethane, propane, and xylenes), and harmful pollutants (carbon dioxide, sulfur dioxide, and nitrogen dioxide).

Using state-of-the-art X-ray and neutron techniques, the team have been able to see the MOFs at the atomic level and how the captured molecules interact with the MOF’s internal structure during reactions. They also used computational modelling to give a deep understanding of how these advanced functional materials operate at a molecular level. This extensive collaboration has been crucial for producing improved materials that can be integrated into our daily lives and makes a vital contribution towards solving the pressing climate and energy challenges that the world faces.

Professor Martin Schröder, Vice President and Dean, Faculty of Science and Engineering, who leads the group at The University of Manchester, said: “I am delighted and honoured that the Royal Society of Chemistry has recognised our interdisciplinary team with the Dalton Horizon Prize. This has been a truly international collaborative effort spanning multiple individuals and groups each bringing their own unique expertise to address challenge research areas.”

The Royal Society of Chemistry’s prizes have recognised excellence in the chemical sciences for more than 150 years. This year’s winners join a prestigious list of past winners in the RSC’s prize portfolio, 60 of whom have gone on to win Nobel Prizes for their work, including 2022 Nobel laureate Carolyn Bertozzi and 2019 Nobel laureate John B Goodenough.

The Research and Innovation Prizes celebrate brilliant individuals across industry and academia. They include prizes for those at different career stages in general chemistry and for those working in specific fields, as well as interdisciplinary prizes and prizes for those in specific roles. The Horizon Prizes highlight exciting, contemporary chemical science at the cutting edge of research and innovation. These prizes are for groups, teams and collaborations of any form or size who are opening up new directions and possibilities in their field, through groundbreaking scientific developments. Other prize categories include those for Education (announced in November), the Inclusion & Diversity Prize, and Volunteer Recognition Prizes.

Dr Helen Pain, Chief Executive of the Royal Society of Chemistry, said: “The chemical sciences cover a rich and diverse collection of disciplines, from fundamental understanding of materials and the living world to applications in medicine, sustainability, technology and more. By working together across borders and disciplines, chemists are finding solutions to some of the world’s most pressing challenges.

“Our prize winners come from a vast array of backgrounds, all contributing in different ways to our knowledge-base and bringing fresh ideas and innovations. We recognise chemical scientists from every career stage and every role type, including those who contribute to the RSC’s work as volunteers. We celebrate winners from both industry and academia, as well as individuals, teams, and the science itself.

“Their passion, dedication and brilliance are an inspiration. I extend my warmest congratulations to them all.”

For more information about the RSC’s prizes portfolio, visit .

The centre has been awarded £1.2m through an International Centre to Centre grant from the Engineering and Physical Sciences Research Council, part of UK Research and Innovation. Led by Professor , Interim Director of the MIB, along with Professor and Dr , and in partnership with Professor David Baker from the Institute of Protein Design (IPD) at the University of Washington, ICED will employ the latest deep-learning protein design tools to accelerate the development of new biocatalysts for use across the chemical industry. The centre will deliver customised biocatalysts for sustainable production of a wide range of chemicals and biologics, including pharmaceuticals, agrochemicals, materials, commodity chemicals and advanced synthetic fuels.

Biocatalysis uses natural or engineered enzymes to speed up valuable chemical processes. This technology is now widely recognised as a key enabling technology for developing a greener and more efficient chemical industry. Although powerful, existing experimental methods for developing industrial biocatalysts are costly and time-consuming, and this restricts the potential impact of biocatalysis on many industrial processes. Furthermore, for many desirable chemical transformations there are no known enzymes that can serve as starting templates for experimental engineering. In ICED we will bring together leading computational and experimental teams from across academia and industry to bring about a step-change in the speed of biocatalyst development. The approaches developed will also allow the development of new families of enzymes with catalytic functions that are unknown in nature.

Professor David Baker, lead researcher from the Institute of Protein Design says; “Accurately designing efficient enzymes with new catalytic functions is one of the grand challenges for the protein design field. We are thrilled to be working with Professor Green and his team in the MIB to address this crucial biotechnological challenge.’’

The design tools developed throughout the project will be readily available to specialists and non-specialists to support their own enzyme engineering and biocatalysis needs. As the centre develops, we expect to grow our partnerships with the wider academic and industrial sector to ensure that we can best serve the needs and ambitions of the global biocatalysis community.

With the chemical and pharmaceutical industries contributing £30.7bn to the UK economy alone, technologies like biocatalysis are poised to revolutionise how every day, essential products are made while also benefitting our health and our environment.

The project leverages a £5 million investment from the ’s Place-Based Impact Acceleration Account to stimulate innovation and commercial growth. The IBIC will give businesses and start-ups a platform to engage with higher education institutions, governmental organisations and researchers in the north-west, and support translating fundamental biotechnology research from the lab to the real world.   

The IBIC launches at a significant time for the UK’s biotechnology market. The UK Government’s on biotechnology and signal increasing interest in the sector, which was valued at £21.8billion in 2023, according to IBISWorld.

Professor Aline Miller, Professor of Biomolecular Engineering and Associate Dean for Business Engagement and Innovation at The University of Manchester, said: "Combine academic research with industrial application, and together we can yield transformative outcomes for both our economy and environment.

“With the launch of the IBIC, we are inviting businesses and startups to join us as we take on global challenges like climate change and sustainability. To do that, we need to create a vibrant ecosystem of interconnected disciplines to help scale businesses, bring research to life and ultimately deliver huge economic benefits to the north-west and beyond.”

This invitation extends particularly to SMEs, high-growth biotech companies, and other businesses interested in contributing to and benefiting from a thriving biotechnology industry in the north-west.

Companies interested in participating or learning more about the Industrial Biotechnology Innovation Catalyst can contact the IBIC team at ibic@manchester.ac.uk for more information and to discuss potential collaboration and partnership opportunities.

‘Tales From The Past’, created in partnership with 91ֱ��’s leading independent brewery Cloudwater Brew Co, celebrates the University’s 200th anniversary and will be launched at its bicentenary festival, where it will be available to buy from the festival bar.

Supported by a Knowledge Transfer Partnership (KTP) grant, The University of Manchester team crossed Saccharomyces jurei, a new species of yeast discovered by Delneri in 2017, with a common ale yeast, Saccharomyces cerevisae, to produce a new starter hybrid strain that enhances the aroma and flavour of the beer.

This new hybrid has several advantages over similar brewing yeasts; it has the ability to thrive at lower temperatures, adds a different flavour profile, and is able to ferment maltose and maltotriose, two abundant sugars present in the wort. These capabilities provide a range of new opportunities for brewers, with the potential for a multitude of hybrids with different fermentation characteristics.

Paul Jones, CEO of Cloudwater Brew Co, said; “It is exciting to be able to brew a beer with a brand new species of yeast and to explore the range of flavours we can create. This beer represents the possibilities of joining academia with industry and we are lucky to have access to this fount of knowledge right on our doorstep.”

The University team has also been developing new hybridisation techniques. Typically, yeast hybrids grow by budding, where a new cell grows from an original ‘parent’, but they are sterile. Now, using a genetic method which doubles the content of the hybrid genome, researchers have overcome infertility allowing the creation of future hybrid generations with diverse traits. These offspring can then be screened for desirable biotechnological characteristics, allowing the team to select and combine beneficial traits from different yeast species using multigenerational breeding.

As yeasts play a major role in many industrial biotechnology applications, different hybrids bred in this way pave the way for creating bespoke microbial factories that can be used to create sustainable products.

As well as their familiar roles in brewing and baking, scientists use yeasts as model organisms to study how cells work. This role has placed them at the forefront of engineering biology, an emerging area of science that seeks to use nature’s own biological mechanisms to replace current, unsustainable industrial processes. As a result, the team’s novel yeast could lead to future breakthroughs in new, green pharmaceuticals and more sustainable fuels.

To launch the beer and share more about her pioneering work, Professor Delneri will give a talk at the Universally 91ֱ�� festival on Friday 7 June at 5.45pm. Tickets can be

The bid was delivered by a coordination team, which includes and from the University and has secured £49.35m from the UKRI Infrastructure Fund to establish C-MASS - a national hub-and-spoke infrastructure designed to integrate and advance the country’s capability in mass spectrometry.

Mass spectrometry is a central analytical technique that quantifies and identifies molecules by measuring their mass and charge. It is used across science and medicine, for drug discovery, to screen all newborn babies for the presence of metabolic disorders, to monitor pollution and to tell us what compounds are in the tails of comets.

Researchers at The University of Manchester develop and apply mass spectrometry in many of its research centres and institutes, including the , the , , , the , and the

C-MASS will enable rapid methodological advances, by developing consensus protocols to allow population level screening of health markers and accelerated data access and sharing. It will bring together cutting-edge instrumentation at a range of laboratories connected by a coordinating central hub that will manage a central metadata catalogue. Together, this will provide unparalleled signposting of data and will be a critical measurement science resource for the UK.

The bid for the funding has been developed over the last 10 years and has included input and support from more than 40 higher education institutes, 35 industrial partners and numerous research institutes.

91ֱ�� is renowned for its expertise in mass spectrometry. J.J. Thomson, who was an alumnus of The University of Manchester, built the first mass spectrometer - originally called a parabola spectrograph - in 1912. Later, another alumnus, James Chadwick, commissioned the first commercial mass spectrometer, built by the 91ֱ�� firm Metropolitan Vickers, for use in the second world war to separate radioactive isotopes.

Now, many decades later, the University receives more funding in mass spectrometry than any other higher education institution in the UK and more mass spectrometers are made in the 91ֱ�� region than any other in Europe.

At the University, researchers across a range of disciplines including , , use mass spectrometry for wide range of world-leading research. Just some of those projects include: , improving the testing and diagnosis of womb cancer, improving our understanding of Huntington’s disease and rheumatic heart disease, diagnosing Parkinson’s disease and finding treatments for blindness.

The mass spectrometry laboratories at the University boast a range of industry-leading instrumentations, not just for staff and students, but also collaborating with many external companies. 

The awards celebrate outstanding women post-doctoral scientists, and forms part of the L’Oréal-UNESCO for Women in Science UK & Ireland Rising Talent Programme, which offers awards to promote, enhance and encourage the contribution of women pursuing their scientific research careers in the UK or Ireland.

Dr Swidah, a postdoctoral researcher at the 91ֱ�� Institute of Biotechnology, was one of five winners at the award at a ceremony at the House of Commons in London on Monday, 18 March.

Other winners were awarded in the categories of engineering, life sciences, mathematics and computing and physical science.

Reem said: “I am honoured to announce that I have been awarded the prestigious L'Oréal UNESCO Award for Women in Science in the category of Sustainable Development.  

“These awards are vital for supporting and celebrating women in science, offering recognition and inspiration. It provides financial research support, fosters networking and collaboration among recipients, and contributes to reducing gender disparities in STEM fields. By highlighting the achievements of women scientists, the award inspires future generations and advocates for gender equality in science.

“Programs like L'Oréal UNESCO  for women in science are critically important, providing vital recognition and support for women scientists while challenging prevailing stereotypes and biases.  Believe in yourself, defy stereotypes, continuously enhance your professional skills, and persist in pursuing your dreams. If opportunities don't come your way, create your own path. Seek mentors, embrace learning, take risks, step out of your comfort zone, and surround yourself with supportive peers. Remember, diversity in STEM drives progress and innovation.

“This award will enable me to balance motherhood and research while gaining the necessary support to make a meaningful impact in my field.”

Reem received a £25,000 grant that is fully flexible and tenable at any UK or Irish university or research institute to support 12 months of research. Her work currently focuses on the genome minimization project (part of the Sc3.0 project initiative), focusing on genome minimization within the synthetic yeast strain (Sc2.0).

Reem was selected for the award for her drive and ambition to leverage her skills in synthetic biology to address global challenges and her work to harness the exceptional evolutionary abilities of synthetic yeast strains to develop innovative and cost-effective technologies to produce biofuels.

She believes that these advancements hold the potential to combat climate change and play a pivotal role in achieving the ambitious goal of Net Zero emissions by 2050, a key strategic objective of The University of Manchester.

She added: “This award will enhance childcare support for my baby and will afford me the time and financial resources to develop my professional skills. I intend to engage in one-to-one career coaching programs and leadership training, which will help me unlock my full potential and excel in my role, which I currently cannot do.

“The grant will also enable me to attend international conferences, where I can engage with scientists and stay updated on global challenges and solutions and it will help me to enhance my research independence by using the grant to purchase small equipment and to conduct essential experiments to boost my research objectives.”

The Women in Science National Rising Talents  is run in partnership between L’Oréal UK and Ireland, the UK National Commission for UNESCO and the Irish National Commission for UNESCO, with the support of the Royal Society.

Thierry Cheval, L'Oréal UK and Ireland, Managing Director said: “As a company founded by a scientist over 100 years ago, L’Oréal, together with UNESCO, is committed to driving gender equality in STEM and recognising the exceptional work of female scientists who are vitally contributing to solving the challenges of tomorrow.

“Congratulations to this year’s Fellows who are a true inspiration for generations to come.”

Professor Anne Anderson, Chair of the UK National Commission for UNESCO's Board of Directors, added: “Congratulations to the 2024 Rising Talents. As we stand at a pivotal moment in time for scientific advancement, UNESCO continues to highlight the importance of true gender equality in science, technology, engineering and mathematics (STEM) and the vital role women play in a more equitable scientific society.

“The United Kingdom National Commission for UNESCO is proud to support these young women in STEM from the UK & Ireland and celebrate their achievements as researchers paving the way for a brighter global future.”

91ֱ�� is the recipient of five awards, including:

• , Senior Lecturer in Chemical Biology and Biological Chemistry of the , and , Professor of Polymer Science at the Henry Royce Institute, who are a Co-Investigators on a Mission Hub led by the University of Portsmouth. The mission Hub is looking into how engineering biology can tackle plastic waste.
• , Professor of Geomicrobiology, from the Department of Earth and Environmental Sciences, is involved in a Mission Hub led by the University of Kent, and also leads a Mission Award, both of which will be looking at ways to use engineering biology to process metals, including for bioremediation and for metal recovery from industrial waste streams.
• , , and of the 91ֱ�� Institute of Biotechnology, received a Mission Award for a project that will engineer biological systems to enable economical production of functionalised proteins including biopharmaceuticals and industrial biocatalysts.
• , Chair in Evolutionary Biology, from the Division of Evolution, Infection and Genomics, and Professor Patrick Cai of the 91ֱ�� Institute of Biotechnology, are looking into engineering phages with intrinsic biocontainment to develop new treatments against drug-resistant bacterial infections.

The hubs are funded for five years through UKRI and the Biotechnology and Biological Sciences Research Council (BBSRC) and are a collaboration between academic institutions and industrial partners. The Mission Award Projects are funded for two years. These projects will expand upon our current knowledge of engineering biology and capitalise on emerging opportunities.

Announcing the funding the Science, Research and Innovation Minister, Andrew Griffith, said: “Engineering biology has the power to transform our health and environment, from developing life-saving medicines to protecting our environment and food supply and beyond.

“Our latest £100m investment through the UKRI Technology Missions Fund will unlock projects as diverse as developing vaccines…preventing food waste through disease resistant crops, reducing plastic pollution, and even driving efforts to treat snakebites.

“With new Hubs and Mission Awards spread across the country, from Edinburgh to Portsmouth, we are supporting ambitious researchers and innovators around the UK in pioneering groundbreaking new solutions which can transform how we live our lives, while growing our economy.”

Engineering biology has the potential to tackle a diverse range of global challenges, driving economic growth in the UK and around the world, as well as increase national security, resilience and preparedness.  The University of Manchester has a broad range of expertise in engineering biology across its three Faculties and is also home to the international centre of excellence, the 91ֱ�� Institute of Biotechnology.

In Dr Stefan Hoffmann, lead author on the paper, and have found that by adding an estradiol-controlled destabilising domain degron (ERdd) to the genetic makeup of baker's yeast (Saccharomyces cerevisiae), they can control survival of the organism.

Destabilising domain (DD) degrons are an element of a protein that allow for degradation, unless a particular ligand – a small molecule that binds with the DD degron – is present to stabilise it. The researchers engineered the yeast to degrade proteins essential for life unless estradiol, a type of oestrogen, was present. Without estradiol, the yeast would die.

This new genetic containment technique differs from previous techniques in that it directly targets essential proteins. It has no detrimental effects on organism function, even when compared with the wild-type organism and it remains an active part of the genome, even after 100 generations.

To achieve this, the researchers tagged 775 essential genes with the ERdd tag and screened the resulting organisms for estradiol-dependent growth. Through this screening, they identified three genes, SPC110, DIS3, and RRP46 as suitable targets. The modified yeast grew well in the presence of estradiol and failed to thrive in its absence.

Professor Patrick Cai, Chair in Synthetic Genomics, said: “Safety mechanisms are instrumental for the deployment of emerging technologies such as engineering biology. The development of biocontainment systems will effectively minimize the risk associated with the emerging technologies, and to protect both the researchers and the wider community. It also provides a novel solution to combat intellectual espionage to safeguard our ever-growing bio-economy. This work is a great example of the responsible innovation of MIB research.”

Engineering biology is a relatively new, but expanding field of science that allows industry to use microorganisms, such as yeasts and bacteria, to produce value-added chemicals cheaply and efficiently. However, as microorganisms are often genetically engineered to increase efficacy, it becomes a problem if the organisms escape into the natural environment.

To ensure modified organisms do not find their way out of an laboratory setting, the NIH sets strict escape rate thresholds. Currently, most genetic safeguards rely on one of two methodologies to keep within the guidelines: either by engineering in an auxotrophy, whereby the organism relies on a specific metabolite to be present in its environment to survive, or a “suicide” gene, where the organism itself produces a toxin that kills it if certain conditions are not met.  

While these methods are generally genetically stable and effective enough to meet the NIH guidelines, they do have caveats to their efficacy. In the case of relying on a metabolite to sustain the organism, this metabolite may also be found in the wild and could not ensure the organism does not survive if it escapes. For “suicide” genes, as this is a direct threat to the organism, over generations the gene can selectively mutate and become inactive rendering it an ineffective control.

The new biocontainment method described by Hoffmann and Cai could be used in conjunction with the existing methods to bolster their effectiveness and deliver an even more robust escape frequency. Even if used as the sole biocontainment method, it provides an escape frequency of <2x10^-10 which far exceeds the NIH guideline of an escape rate of less than 10^-8.  

Today, the and The announced the nine recipients of the 2024 Blavatnik Awards for Young Scientists in the UK, including three Laureates and six finalists.

and are named among the three Laureates, who will each receive £100,000 in recognition of their work in Chemical Sciences and Physical Sciences & Engineering, respectively.

Now in its seventh year, the awards are the largest unrestricted prizes available to UK scientists aged 42 or younger. The awards recognise research that is transforming medicine, technology and our understanding of the world.

This year’s Laureates were selected by an independent jury of expert scientists from across the UK.

Professor Anthony Green, a Lecturer in Organic Chemistry from The University of Manchester, has been named the Chemical Sciences Laureate for his discoveries in designing and engineering new enzymes, with valuable catalytic functions previously unknown in nature that address societal needs. Recent examples include the development of biocatalysts to produce COVID-19 therapies to break down plastics, and to use visible light to drive chemical reactions. 

Rahul Nair, Professor of Materials Physics at The University of Manchester, was named Laureate in Physical Sciences & Engineering for developing novel membranes based on two-dimensional (2D) materials that will enable energy-efficient separation and filtration technologies. Using graphene and other 2D materials, his research aims to study the transport of water, organic molecules, and ions at the nanoscale, exploring its potential applications to address societal challenges, including water filtration and other separation technologies.

Internationally recognised by the scientific community, the Blavatnik Awards for Young Scientists are instrumental in expanding the engagement and recognition of young scientists and provide the support and encouragement needed to drive scientific innovation for the next generation.

, Founder and Chairman of Access Industries and Head of the Blavatnik Family Foundation, said: “Providing recognition and funding early in a scientist’s career can make the difference between discoveries that remain in the lab and those that make transformative scientific breakthroughs.

“We are proud that the Awards have promoted both UK science and the careers of many brilliant young scientists and we look forward to their additional discoveries in the years ahead.”

, President and CEO of The New York Academy of Sciences and Chair of the Awards’ Scientific Advisory Council, added: “From studying cancer to identifying water in far-off planets, to laying the groundwork for futuristic quantum communications systems, to making enzymes never seen before in a lab or in nature, this year’s Laureates and Finalists are pushing the boundaries of science and working to make the world a better place. Thank you to this year’s jury for sharing their time and expertise in selecting these daring and bold scientists as the winning Laureates and Finalists of the 2024 Blavatnik Awards for Young Scientists in the UK.”

The 2024 Blavatnik Awards in the UK Laureates and Finalists will be honoured at a black-tie gala dinner and award ceremony at Banqueting House in Whitehall, London, on 27 February 2024.

The Sustainable Commodity Chemicals through Enzyme Engineering and Design (SuCCEED) project will look to find new ways of manufacturing the chemicals needed for many every-day products through industrial biotechnology routes. By doing this, it will help the chemical manufacturing industry move away from fossil-based feedstocks and reduce their carbon footprint. 

Bio-based manufacturing routes are not currently widespread as they are difficult to scale up and don’t operate at the profit margins required for commodity chemicals. This poses a barrier to moving the chemicals industry away from petrochemicals and creating a greener industry. 

To help address this, the Prosperity Partnerships bring together industry and academia to find workable solutions to industry-based problems. The 91ֱ�� Institute of Biotechnology (MIB) and Shell have assembled an interdisciplinary team, led by , of biochemists, protein engineers, synthetic biologists, chemists, and chemical engineers to create a proof-of-principle, scalable, biorefinery. 

If successful, this 5-year project could help reshape the chemicals industry and support the UK delivering on its clean growth strategy.

Jeremy Shears, Chief Scientist for Biosciences at Shell said: “Shell aims to transition to a net-zero emissions energy business by 2050 and our work with the 91ֱ�� Institute of Biotechnology is important to unlock a more commercial route to sustainably produced chemicals. If we can demonstrate an effective route to bio-production, we hope this will be the catalyst for industrial change across the sector.”

Science, Research and Innovation Minister, Andrew Griffith, said:

“Our new bioscience prosperity partnerships are a valuable opportunity for government, business and academia to come together and help unleash world-class, pioneering discoveries across the UK while growing our local economies.

“More than £17m of Government funding is backing vital projects including work in Belfast to unearth life-saving drugs, in 91ֱ�� to improve skin health research and in Cambridge to tackle a major source of global pollution – enhancing the health and wellbeing of people across our country and beyond.”

Dr Lee Beniston FRSB, Associate Director for Industry Partnerships and Collaborative R&D at BBSRC, said:

“The inaugural round of the BBSRC prosperity partnerships programme has been a huge success. Led by BBSRC, with investment from our colleagues at MRC and EPSRC, we will invest more than £17 million in ten projects.

“This investment will support outstanding, long-term collaborative partnerships between businesses and academic researchers across the UK. Through the BBSRC prosperity partnerships programme, the businesses involved are investing over £21 million into research and development.

“The projects supported will deliver on UK ambitions for private sector investment in research and innovation as outlined in the Science and Technology Framework, helping to drive economic growth and societal impact through key bioscience and biotechnology sectors and industries.”

Industrial biotechnology uses nature’s own processes to produce value-added products, it is currently used to produce high-value chemicals such as pharmaceuticals. Enzymes and bacteria are the staple workhorses of biocatalysis – a process that speeds up chemical reactions – and can produce target chemicals by using anything from biomass to anthropogenic waste as a feedstock. Industrial biotechnology holds huge potential for creating a sustainable manufacturing environment and supporting the world’s transition to net zero.

The University was also successful in securing a second Prosperity Partnership with Boots, and co-leading a third with University College London.

MOOCs were set up in the mid-2000s to offer learning opportunities to distance learners. Since their inception they have brought education to thousands around the world, usually for free or at a low cost compared with traditional degrees. They have been credited with helping democratise higher education (HE) especially for those in developing nations by offering them a way to receive education from universities around the world, in a way and at a time that suits them.

The industrial biotechnology MOOC was designed and coordinated by Lesley-Ann Miller and Dr. Nicholas Weise from the 91ֱ�� Institute of Biotechnology, drawing together expertise from the University, and beyond, through a selection of contributors. The modules, which are all freely available worldwide to anyone with an internet connection, covers topics such as enzyme catalysis, synthetic biology, biochemical engineering, pharmaceutical synthesis, biomaterials, bioenergy and glycobiotechnology.  

The course exemplifies how industrial biotechnology can be used by society to meet global net zero goals and create more sustainable routes to manufacture of everyday products, as well as specialist chemicals used by industry. Since the Industrial Revolution, society has relied upon fossil fuels to provide the raw materials for many everyday products including pharmaceuticals, food and drink, materials, plastics, and personal care products.

With government targets drawing closer, industry must find new ways to manufacture these products without relying on finite resources. Industrial biotechnology offers a way for industry to adapt and change to meet these targets while still being able to produce high-quality and high-yielding products with a smaller impact on the environment.

Course instructors, Prof. Nicholas Turner, Dr. Nicholas Weise and Prof. Nigel Scruton, are delighted that the course has been used by hundreds of thousands as a way to access knowledge of sustainable bio-inspired technologies. The course is designed to help those looking to enter the field of biotechnology, upskill or even retrain to help solve technological challenges in their own areas. The course has received an average rating of 4.7/5.0 with learner stories such as:

Open dissemination of expertise from the University that can be used to solve global challenges is an important part of the research impact and social responsibility agenda for the university. The course has already received a recognition for its innovative practices in teaching and learning from the LearnSci Teaching Innovation Awards, a Teaching Excellence Award from the Institute of Teaching & Learning as well as being highly commended at the Making A Difference Awards for outstanding teaching innovation in social responsibility. 

Researchers in the 91ֱ�� Institute of Biotechnology (MIB) at The University of Manchester have created the tRNA Neochromosome – a chromosome that is new to nature.

It forms part of a wider project (Sc2.0) that has now successfully synthesised all 16 native chromosomes in Saccharomyces cerevisiae, common baker’s yeast, and aims to combine them to form a fully synthetic cell.

The international team has already combined six and a half synthetic chromosomes in a functional cell. It is the first time scientists have written a eukaryotic genome from scratch.

Yeasts are a common workhorse of industrial biotechnological processes as they allow valuable chemicals to be produced more efficiently, economically, and sustainably. They are often used in the production of biofuels, pharmaceuticals, flavours and fragrances, as well as in the more well-known fermentation processes of bread-making and beer-brewing.

Being able to re-write a yeast genome from scratch could create a strain that is stronger, works faster, is more tolerant to harsh conditions and has a higher yield.

The process also sheds light on the traditionally problematic genome fundamentals, such as how genomes are organised and evolved.

The findings of both projects, published as two research articles of the prestigious journals Cell and Cell Genomics respectively, are a culmination of 10 years of research from an international consortium of scientists led by Professor Patrick Cai and The University of Manchester, and mark a new chapter in engineering biology.

The University of Manchester’s research also features on the front covers of both journals.

Prof Cai, Chair in Synthetic Genomics at The University of Manchester who is the international coordinator of Sc2.0 project, said: “This is an exciting milestone when it comes to engineering biology. While we have been able to edit genes for some time, we have never before been able to write a eukaryote genome from scratch. This work is fundamental to our understanding of the building blocks of life and has the potential to revolutionise synthetic biology which is fitting as 91ֱ�� is the home of the Industrial Revolution. Now, we’re at the forefront of the biotechnological revolution too.

“What’s remarkable about this project is the sheer scale of collaboration and the interdisciplinarity involved in bringing it to fruition. We’ve brought together not only our experts here in the MIB, but also experts from across the world in fields ranging from biology and genomics to computer science and bioengineering.

Dr Daniel Schindler, one of the two lead authors and group leader at the Max Planck Institute for Terrestrial Microbiology and the Center for Synthetic Microbiology (SYNMIKRO) in Marburg, added: "The international Sc2.0 is a fascinating, highly interdisciplinary project. It combines basic research to expand our understanding of genome fundamentals, but also paves the way for future applications in biotechnology and drives technology developments.

“The international and inclusive nature of the project has unleashed the science and seeded future collaborations and friendships. The 91ֱ�� Institute of Biotechnology, with its excellent research environment and open space, has always facilitated this."

The tRNA neochromosome is used to house and organise all 275 nuclear tRNA genes from the yeast and will eventually be added to the fully synthetic yeast where the tRNA genes have been removed from the other synthesised chromosomes. 

Unlike the other synthetic chromosomes of the Sc2.0 project, the tRNA neochromosome has no native counterpart in the yeast genome.

It was designed using AI assisted, computer-assisted design (CAD), manufactured with state-of-the-art roboticized foundries, and completed by comprehensive genome-wide metrology to ensure the high fitness of the synthetic cells.

Next, the researchers will work together to bring all the individual synthetic chromosomes together into a fully synthetic genome. The final Sc2.0 strain will not only be the world’s first synthetic eukaryote, but also the first one to be built by the international community.

“The potential benefits of this research are universal – the limiting factor isn’t the technology, it’s our imagination”, says Prof Cai.

The centre, led Dr Mauricio A Álvarez, will train the next generation of AI researchers to develop AI methods designed to accelerate new scientific discoveries – specifically in the fields of astronomy, engineering biology and material science.

The University will be working in partnership with The University of Cambridge, and is one of 12 Centres for Doctoral Training (CDTs) in Artificial Intelligence (AI) based at 16 universities, announced by UK Research and Innovation (UKRI) today (31 October).

The investment by UKRI aims to ensure that the UK continues to have the skills needed to seize the potential of the AI era, and to nurture the British tech talent that will push the AI revolution forwards. 

£117 million in total has been awarded to the 12 CDTs and builds on the previous UKRI investment of £100 million in 2018.

Doctoral students at The University of Manchester will be provided with a foundation in Machine Learning and AI and an in-depth understanding of the implications of its application to solve real-world problems.

The programme will also cover the areas of responsible AI and equality, diversity and inclusion.

Dr Mauricio A Álvarez, Senior Lecturer in Machine Learning at The University of Manchester, said: "We are delighted to be awarded funding for this new AI CDT. 91ֱ�� is investing heavily in AI research and translation, and the CDT will complement other significant efforts in research through our AI Fundamentals Centre at the University and innovation via the Turing Innovation Catalyst. Our partnership with Cambridge will also enable us to educate experts capable of generalising and translating nationally to stimulate the development and adoption of AI technology in high-potential, lower AI-maturity sectors.

“Modern science depends on a variety of complex systems, both in terms of the facilities that we use and the processes that we model. AI has the potential to help us understand these systems better, as well as to make them more efficient.

“The AI methods we will develop will apply to a wide range of challenges in complex systems, from transport systems to sports teams. We are partnering with a diverse pool of industry collaborators to address these challenges jointly."

Dr Julia Handl, Professor in Decision Sciences at The University of Manchester, said: “This CDT is a fantastic opportunity to bring together researchers from a wide spectrum of disciplines, from across all three of Manchester’s Faculties, to ensure we can develop innovative solutions that are appropriate to the complexity and uncertainty of real-world systems. The involvement of the Faculty of Humanities is crucial in ensuring such systems are effective and inclusive in supporting human decision makers, and in delivering the centre’s cross-cutting theme of increasing business productivity, supported by collaboration with the Productivity Institute, the Masood Enterprise Centre and a range of industry partners.”

UKRI Chief Executive, Professor Dame Ottoline Leyser, said: “The UK is in a strong position to harness the power of AI to transform many aspects of our lives for the better. Crucial to this endeavour is nurturing the talented people and teams we need to apply AI to a broad spectrum of challenges, from healthy aging to sustainable agriculture, ensuring its responsible and trustworthy adoption. UKRI is investing £117 million in Centres for Doctoral Training to develop the talented researchers and innovators we need for success.”

Dr Kedar Pandya, Executive Director, Cross-Council Programmes at UKRI, said: “This £117 million investment, will involve multiple business and institutional partners for the Centres of Doctoral Training. These include well-known brands such as IBM, Astra Zeneca, and Google, as well as small to medium sized enterprises that are innovating in the AI field. A further £110 million has been leveraged from all partners in the form of cash or in-kind contributions such as use of facilities, resources or expertise.”

The first cohort of UKRI AI CDT students will start in the 2024/2025 academic year, recruitment for which will begin shortly.

IBIC is a collaborative initiative, led by The University of Manchester, aimed at harnessing the region's scientific and research expertise to accelerate knowledge exchange, impact, and innovation, while fostering a more productive, research-intensive economy and promoting sustainability.

Industrial Biotechnology is a multi-disciplinary field that utilises biological resources for everyday product development, including food, fuels, and medicines. It is poised for significant growth with a market potential exceeding £34 billion in the UK alone. The confluence of consumer demand, carbon emission targets, and technological advancements requires new approaches to manufacturing, especially using methods that are divested of petrochemical feedstocks, and industrial biotechnology offers the solutions.

Together with the Universities of Liverpool, 91ֱ�� Metropolitan, Bolton and Salford, The University of Manchester will lead a consortium of academia and industry and create a cohesive ecosystem for IB innovation. The new £5million EPSRC Place-Based Impact Acceleration Account (PBIAA) builds on an existing critical mass of IB expertise in the Northwest including the 91ֱ�� Institute of Biotechnology’s pioneering work (recognised by a Queen’s Anniversary Prize in 2019), major healthcare and biomanufacturing companies like AstraZeneca, Teva, Croda, and Unilever. As well as thriving SME innovation zones, including Daresbury, Liverpool Knowledge Quarter, and Alderley Park, the UK's largest life science campus. 

Professor Miles Padgett, Interim Executive Chair at EPSRC, said:

“I’m pleased to announce our first ten Place Based Impact Acceleration Accounts which will play a unique role in enhancing the capabilities of innovation clusters across the UK. A key priority for UKRI is to strengthen clusters and partnerships in collaboration with civic bodies and businesses, thereby driving regional economic growth.”

Science Minister, George Freeman, said: “Biotechnology delivers for our health, planet, prosperity and beyond and by targeting the North-West through our £41m place-based investment, we can build on the region’s thriving innovation cluster and better integrate the UK’s renowned research activity.

“Our investment will also create hundreds of new jobs, projects and businesses that will in turn drive investment to the region to grow the local and wider UK economy.”

Professor Claire Eyers, Associate Pro Vice Chancellor for Research and Impact in the Faculty of Health and Life Sciences at the University of Liverpool, said: “The University of Liverpool is one of the UK’s leading research-intensive higher education institutions. We pride ourselves in having a long history of working with a variety of organisations and this collaboration allows for the further application of our world-class research to solve real-world challenges.

We very much look forward to working with our regional partners to combine knowledge and expertise and create meaningful and lasting impact for a thriving north-west innovation ecosystem.”

Dr Damian Kelly, Vice President – Innovation & Technology Development at Croda is fully supportive of the initiative: “At Croda we are committed to be climate, land and people positive by 2030. We work to identify functional materials that can be manufactured from widely available, non-fossil materials while also developing low emission processing.  We are looking forward to being an active member of the IBIC ecosystem and engaging with the collaborative mechanisms.”

The launch of IBIC is expected to stimulate significant investments, create numerous job opportunities, foster collaborative projects, and drive economic growth across the region. Building upon the region’s current credentials of a workforce of 25,000 people and a more than £6 billion turnover each year, the cluster is predicted to directly stimulate £2.5M cash and £4M in-kind co-investment, establish 150 collaborative projects, train 200+ students, create up to 100 green jobs, and establish 20+ new commercial ventures which could attract a further £10M in investment. This would see the cluster delivering a minimum 3:1 economic return on public investment over the medium term, with long-term plans to become an independent, business-led cluster of excellence.

For more information about IBIC and its initiatives, contact Professor Miller via email: aline.miller@manchester.ac.uk.

The research, funded by the Biotechnology and Biological Sciences Research Council’s (BBSRC) strategic Longer and Larger (sLoLa) grants programme, takes the first major step towards understanding complex microbial communities and will support the move towards a more sustainable and Net Zero future.

The University is one of four institutions to receive a share of £18 million from the BBSRC to support adventurous research aimed at tackling fundamental questions in bioscience.

The project, worth £5.4 million, builds on the work of the 91ֱ�� Microbiome Network - a network that brings together the leading microbiome science expertise from across the University to deliver a step-change in understanding microbial communities, regardless of habitat.

Lead researcher, Professor Sophie Nixon, BBSRC David Phillips and Dame Kathleen Ollerenshaw Fellow at The University of Manchester, said: “Microbial communities, often called microbiomes, are found in almost every habitable environment on the planet. They exert a significant influence on each of these environments, whether that be the soil we grow our food, in the guts of animals, or even in extreme environments like geothermal springs – our target environment for this project. However, microbiomes are inherently complex and challenging to study, and their ‘rules of life’ remain obscure.

“Recent technological advances have allowed researchers to study the interactions between members of microbiomes for the first time. Yet, we have barely scratched the surface of resolving how these interactions affect the structure, function, and stability of the community as a whole.   

Over five years, the researchers from The University of Manchester and the Earlham Institute will concentrate on low-diversity communities inhabiting geothermal springs, using a powerful combination of biochemical, ‘omics, and synthetic biology approaches to uncover the rules that govern microbial life in communities.

Using a tractable model system, the team aim to engineer the microbial community both as a learning tool to test emerging hypotheses, such as the ways in which microbes depend on or hinder one another, and as a testbed for future biotechnological development.

Ultimately, the findings will facilitate the engineering of bespoke microbial communities to be used for a plethora of important applications, including new ways to bio-convert CO2 emissions into socio-economically beneficial compounds, contributing toward a more sustainable and Net Zero future. 

Professor Guy Poppy, Interim Executive Chair at BBSRC, said: “The latest investment by BBSRC’s sLoLa award programme represents a pivotal step in advancing frontier bioscience research.

“These four world-class teams are poised to unravel the fundamental rules of life, employing interdisciplinary approaches to tackle bold challenges at the forefront of bioscience.

“By fostering collaboration and innovation, we aim to catalyse ground-breaking discoveries with far-reaching implications for agriculture, health, biotechnology, the green economy and beyond.”

The University of Manchester’s research team includes seven researchers from the Faculty of Science and Engineering (five of which are based in the flagship 91ֱ�� Institute of Biotechnology), two from the Faculty of Biology, Medicine and Health, and one from the Earlham Institute - a life science research institute based in Norwich.

Therapeutic oligonucleotides are an emerging class of drug molecules that have the potential to treat a wide range of diseases.

The finding, by The University of Manchester, will facilitate large-scale production of oligonucleotides to ensure the widest possible access of these drugs for patients.

Oligonucleotides are short sequences of DNA that can modulate or control gene expression. In this way, they have the potential to address the underlying causes of various diseases such as heart disease, cancer, and muscular dystrophy.

Over recent years, there has been an increasing number of approved oligonucleotide-based therapies, but widespread use of the drug has been limited in part because of difficulties in its manufacturing process.

Current methods rely on chemical synthesis that requires large amounts of solvent, generates substantial waste, and delivers final products with low yield and modest purity. Reactions are performed on solid supports or columns, which limits scalability, making them suitable only for producing oligonucleotides in small batches.

The new research, published in the journal , presents a sustainable and scalable approach to oligonucleotide production, addressing the challenges associated with current methods.

The findings could have major implications for the pharmaceutical industry.

Sarah Lovelock, Senior Lecturer at the 91ֱ�� Institute of Biotechnology at The University of Manchester, said: “Therapeutic oligonucleotides are an exciting new drug modality with huge potential to treat a wide range of diseases, including genetic disorders and viral infections.

“Many pharmaceutical companies have therapeutic oligonucleotide candidates in their pipelines, including those for common diseases. The development of more scalable and sustainable approaches to oligonucleotide production will be key to ensuring the widest possible access to this powerful class of therapeutics.”

In nature, DNA can be copied or amplified using enzymes called polymerases. The new approach uses these polymerases to amplify a catalytic DNA template to make a high volume of therapeutic oligonucleotides in a single step. This contrasts the iterative rounds of chain extension, capping, oxidation and deprotection associated with established methods.

Researchers at the University of Manchester are now working in a collaborative partnership with technology innovation catalyst CPI, AstraZeneca, and Novartis to scale up the approach presented within this research. 

The Enzyme Discovery team won the Chemistry Biology Interface Horizon Prize: Rita and John Cornforth Award, while the Molecular Ratcheteers team won the Organic Chemistry Horizon Prize: Perkin Prize in Physical Organic Chemistry. 

The Enzyme Discovery team was recognised for its work investigating enzymes to combat antimicrobial resistance in the developing world. 

The team, based at the and the at The University of Manchester, with collaborators from GlaxoSmithKline, won the accolade for successfully discovering new enzymes for sustainable synthesis.

Their findings could lead to more affordable medicines, antibiotics that are more resistant to antimicrobial resistance, and even treat previously untreated diseases.  

Professor Jason Micklefield from the 91ֱ�� Institute of Biotechnology and the Department of Chemistry at The University of Manchester, said: “Our team is acutely aware of the importance of finding more sustainable and efficient routes to new and improved antimicrobials and other important therapeutic agents that are urgently required to combat antimicrobial resistance, treat diseases and tackle future pandemics.  

“Our research has allowed us to discover and engineer enzymes and pathways for sustainable synthesis, and we look forward to the future applications of our work in providing more parts of the world with increased access to essential medicines and more sustainable routes to commonly used products.”  

If adopted in industry, the Enzyme Discovery team’s work could lead to more affordable products, including medicines, which could be made more widely available to help combat antimicrobial resistance and other neglected diseases in the developing world. Their work also has the potential to help reduce other problems such as chemical waste. 

The Molecular Ratcheteers team was recognised for its work in nanotechnology, advancing the building blocks for everything from medicine delivery to information processing.

Based at the University of Manchester, with support from the University of Maine, the University of Luxembourg and East China Normal University, the Molecular Ratcheteers won the accolade for inventing engineering concepts that will help unlock the potential of the nanoworld.

The work leads to a variety of real-life applications like the creation of new nanomachines such as molecular motors, pumps and switches, that could make improvements in everything from the delivery of medicines to information processing. 

The group – which brought together minds with specialities in areas such as the physics of information and molecular biology – join a prestigious list of past winners in the RSC’s prize portfolio, 60 of whom have gone on to win Nobel Prizes for their work, including 2022 laureate Carolyn Bertozzi and 2019 laureate, John B Goodenough. 

Professor Dave Leigh from the Molecular Ratcheteers team at The University of Manchester, said: “It’s been fantastic to be part of such a talented team on the Molecular Ratcheteers project, and we’re proud to have developed concepts that could truly drive forward engineering in the nanoworld.” 

Miniaturisation has driven advances in technology through the ages. Early computers filled entire rooms and consumed vast amounts of energy yet had far less computing power than the tiny energy-frugal chips in today’s smartphones.

Making machinery smaller reduces power requirements, curtails the amounts of materials needed, cuts waste, facilitates recycling and produces faster operating systems. In doing so it advances technological progress while addressing the environmental and sustainability needs of society. 

Both research teams will also receive a trophy and a professionally produced video to celebrate the work. 

Dr Helen Pain, Chief Executive of the Royal Society of Chemistry, said: “The Horizon Prizes recognise brilliant teams and collaborations who are opening new directions and possibilities in their field, by combining their diversity of thought, experience and skills, to deliver scientific developments for the benefit of all of us.  

“The work of the Enzyme Discovery team is a fantastic example of why we celebrate great science; not only because of how they have expanded our understanding of the world around us, but also because of the incredible contribution they make to society as a whole. We are very proud to recognise their work.” 

The Royal Society of Chemistry’s prizes have recognised excellence in the chemical sciences for more than 150 years. In 2019, the organisation announced the biggest overhaul of this portfolio in its history, designed to better reflect modern scientific work and culture. 

The Horizon Prizes celebrate the most exciting, contemporary chemical science at the cutting edge of research and innovation.  

For more information about the Royal Society of Chemistry’s prizes portfolio, visit .

Dr Sophie Nixon, a BBSRC David Phillips and Dame Kathleen Ollerenshaw Research Fellow in the Department of Earth and Environmental Sciences, won the award for Sustainable Development, while Dr Kara Lynch, who was recently awarded an Ernest Rutherford Fellowship and Dame Kathleen Ollerenshaw Research Fellowship in the Department of Physics, won the award for Physical Sciences.

The national award works to support post-doctoral women scientists and overcome gender-driven inequalities. It offers a number of opportunities designed to help further establish women’s research careers. 

Dr Nixon and Dr Lynch are two of only five post-doctoral women scientists to win the 2023 award, which includes a grant of £15,000 each to spend on whatever they need to continue their research.

Dr Nixon's  research broadly looks how microbial communities in the environment cycle carbon, and how we can harness community-scale metabolism to help remedy global environmental issues, such as climate change and plastic pollution.

The project she will pursue with her award looks to microbial communities in hot springs for novel approaches to converting waste CO₂ emissions into value-added products in order to achieve a Net Zero future as soon as possible - an ambitious but potentially powerful nature-based solution to the CO₂ emissions crisis.

She said: “It was a big milestone to even be shortlisted for this notoriously competitive award, but to win was just wonderful.

“Awards and programmes like this one are really important for putting a spotlight on women in STEM – we need more talent in STEM but also need to showcase and celebrate the talent we already have. One problem we have is lack a of role models, but another is peer support. This programme champions this talent and creates a really strong alumni network that will be invaluable going forward.

“For me, the most powerful part of this award is the flexibility the grant allows. A significant part of my grant will go towards the cost of childcare - I’ve been working condensed hours since the cost of childcare for our daughter has risen. The extra time and money this will buy me allows me to pursue some extra personal development training, some career and leadership coaching, and also attend events or conferences.

“I wouldn’t be able to achieve any of this if I couldn’t find a way to subsidise the cost of childcare. It has opened many doors and I’m extremely grateful.”

Dr Lynch's research revolves around nuclear physics and using laser spectroscopy and decay spectroscopy to understand the properties of exotic nuclei. Her upcoming research project will measure the shape of proton-emitting nuclei, which is a new and exciting opportunity to test and improve understanding of the nucleus.

She said: “The L’Oréal-UNESCO For Women in Science Rising Talent Programme is a really innovative and refreshing way of supporting women in science, as it allows you to use the grant in whichever way is most beneficial to your research and your career.

“Programmes highlighting and supporting women in science are very important, so we can encourage more women to pursue scientific careers as well as support those already in science. The postdoc years can be particularly challenging as we try to forge our own independent research career, so having a network of support is invaluable.

“I feel very lucky and proud to be alongside the wonderful and inspiring women who were shortlisted for this award, and to win was just a wonderful surprise.”

Dr Lynch will use the grant to buy research equipment that will allow her to perform the first laser spectroscopy studies of proton-emitting nuclei, which she hopes will kick-start her research programme in an unexplored area of nuclear physics. 

She will also use the grant for childcare to allow her to travel to CERN-ISOLDE – a radioactive ion beam facility - to perform her experiments outside of her normal working pattern.

Dr Lynch added: “Having just returned to physics research after a career break to start a family, the grant will uniquely support my desire to blend primary caregiving with my re-started academic career.

“I'm very grateful to L’Oréal and UNESCO for the opportunity to be part of this amazing network.”

All shortlisted candidates were invited to 10 Downing Street to discuss support for women in STEM. They met with George Freeman MP, Minister of State in the new Department for Science, Innovation and Technology, along with Angela McClean, Chief Scientific Advisor. They also received media training and had professional photographs taken at the Royal Society before attending the award at a ceremony at the House of Commons on Monday, 24 April 2023.

Building infrastructure in space is currently prohibitively expensive and difficult to achieve. Future space construction will need to rely on simple materials that are easily available to astronauts, StarCrete offers one possible solution. 

The scientists behind the invention used simulated Martian soil mixed with potato starch and a pinch of salt to create the material that is twice as strong as ordinary concrete and is perfectly suited for construction work in extra-terrestrial environments.

In an article published in the journal , the research team demonstrated that ordinary potato starch can act as a binder when mixed with simulated Mars dust to produce a concrete-like material. When tested, StarCrete had a compressive strength of 72 Megapascals (MPa), which is over twice as strong as the 32 MPa seen in ordinary concrete. Starcrete made from moon dust was even stronger at over 91 MPa.

This work improves on previous work from the same team where they used astronauts’ blood and urine as a binding agent. While the resulting material had a compressive strength of around 40 MPa, which is better than normal concrete, the process had the drawback of requiring blood on a regular basis. When operating in an environment as hostile as space, this option was seen as less feasible than using potato starch.

“Since we will be producing starch as food for astronauts, it made sense to look at that as a binding agent rather than human blood. Also, current building technologies still need many years of development and require considerable energy and additional heavy processing equipment which all adds cost and complexity to a mission. StarCrete doesn’t need any of this and so it simplifies the mission and makes it cheaper and more feasible.

“And anyway, astronauts probably don’t want to be living in houses made from scabs and urine!” Dr Aled Roberts, Research Fellow at the Future Biomanufacturing Research Hub, The University of Manchester and lead researcher for this project.

The team calculate that a sack (25 Kg) of dehydrated potatoes (crisps) contain enough starch to produce almost half a tonne of StarCrete, which is equivalent to over 213 brick’s worth of material. For comparison, a 3-bedroom house takes roughly 7,500 bricks to build. Additionally, they discovered that a common salt, magnesium chloride, obtainable from the Martian surface or from the tears of astronauts, significantly improved the strength of StarCrete.

The next stages of this project are to translate StarCrete from the lab to application. Dr Roberts and his team have recently launched a start-up company, , which is exploring ways to improve StarCrete so that it could also be used in a terrestrial setting.

If used on earth, StarCrete could offer a greener alternative to traditional concrete. Cement and concrete account for about 8% of global CO₂ emissions as the process by which they are made requires very high firing temperatures and amounts of energy. StarCrete, on the other hand, can be made in an ordinary oven or microwave at normal ‘home baking’ temperatures, therefore offering reduced energy costs for production.

Oligonucleotides are a revolutionary new therapeutic in the pharma industry. These short, chemically synthesised fragments of DNA or RNA modulate protein expression through several different mechanisms to treat the underlying drivers of disease. This means almost limitless potential for treating conditions like heart disease, cancer, and muscular dystrophy.

There is, however, a risk that inefficiencies in the high cost, unsustainable process may limit patient access to oligonucleotide-based therapeutics at a large scale.

The new collaborative partnership builds on work at CPI’s Medicines Manufacturing Centre to revolutionise the manufacture of novel oligonucleotide-based medicines. The aim of this industry ‘grand challenge’ is to develop an alternative process that is scalable, sustainable, and cost-effective.

The process in development uses bio-catalysis using a template that enables the building blocks of oligonucleotides to stitch together in a high-fidelity manner. This new enzyme-driven method has the potential to deliver oligonucleotides of superior purity to those made using chemical synthesis while reducing the carbon footprint of their manufacture. Ultimately, the successful commercialisation of this manufacturing approach would lower the cost of producing oligonucleotide-based therapeutics, removing a barrier to wider patient access.

The research will take place at the 91ֱ�� Institute of Biotechnology (MIB), part of The University of Manchester, which has been developing the technology to date.

Claire MacLeod, Oligonucleotides Grand Challenge Lead at CPI, said:

“As a technology innovation catalyst, bringing exemplary teams together to develop advanced technologies and manufacturing solutions that benefit people, and our planet, is what we do. This oligonucleotide project is a brilliant example of this. We are proud to bring our expertise in delivering collaborative innovation projects and our high-tech facilities to solve this grand challenge together with industry leading teams at MIB, AstraZeneca and Novartis.”

Sarah Lovelock, Senior Lecturer at 91ֱ�� Institute of Biotechnology, said:

“We are excited to be involved in this partnership with leading industrial experts from CPI, AstraZeneca, and Novartis, to translate our approaches to oligonucleotide synthesis into sustainable manufacturing processes. We are hopeful that this collaboration will facilitate the large-scale production of oligonucleotides to ensure the widest possible access to this emerging class of therapeutics.”

Barrie Cassey, Technology Lead – Medicines Manufacturing, at CPI, said:

“CPI is a trusted delivery partner of the UK government’s Medicines Manufacturing Challenge and is well placed to lead the way in transforming the sustainability and viability of manufacturing technologies for this powerful new drug modality.

“In collaboration with our academic and industry partners, we aim to improve the processes for oligonucleotide manufacture to boost efficiency and sustainability across the pharmaceutical industry, and ultimately improve patient access to these life-changing medicines.

“Many pharmaceutical companies have rich pipelines of oligonucleotide-based drug candidates that could benefit from an alternative production process. CPI and partners are keen to engage with pharma companies as the project develops the novel technology into a viable approach for oligonucleotide manufacture.”

The , founded in 2020, is a global consortium of hundreds of scientists around the world with the collective goal of supporting euglenoid science through collaborative and integrative omics between academics and industry. Professor Rob Field, director of the 91ֱ�� Institute of Biotechnology, sits on the steering committee for the EIN and he and his lab will be part of the cross-discplinary network of scientists working to understand and discover the capabilities of the 800-strong species and strains of Euglena.

The EIN has today published a , outlining the case for a concerted effort to generate high quality reference genomes for the nearly 1,000 known species of euglenoids.

Euglenoids are part of the protist group, home to eukaryotic organisms that do not fit into animal, plant, or fungi groups. These diverse single-celled organisms are found in an exceptionally wide range of ecosystems around the world.

Multiple euglenoid species have translational applications, showing great promise in the production of biofuels, nutraceuticals, bioremediation, cancer treatments, and even as robotics design simulators. Their enormous potential has been largely untapped due to a lack of high-quality reference genomes.

Euglenoid genomes present a particular sequencing challenge because they are an example of secondary endosymbiosis – housing mitochondria, chloroplasts, and remnants of genetic material from organisms they enveloped to acquire these organelles.

As a result, fewer than 20 species have been explored at any level for translational potential through genomics. The EIN believes the time is right to address this.

Through generating high quality reference genomes for the known species of euglenoids, the EIN will work to:

• Understand the basic biology of euglenoids;
• Understand the evolution of euglenoids;
• Maximise euglenoid applications in ecological and environmental management;
• And explore, translate, and commercialise euglenoid products.

Data collected by the EIN will be openly available to the scientific community through the . Once in the ENA, annotated genomes can be imported into resources such as Ensembl Protists and presented in a uniform and FAIR way to research communities.

Professor Field's interest in this area goes back to 2015 when he and his lab were , including using it for creating a range of sugars and other natural products.  They've since gone on to which could prove useful for the pharmaceutical industry. Together with the rest of the network they hope to work together to better understand the more than 800 species of Euglena and exploit their potential. 

Dr. ThankGod Echezona Ebenezer, Founding President of EIN and a Bioinformatician at the European Bioinformatics Institute (EMBL-EBI), UK, said: “The Euglena International Network will play a crucial role in helping to assemble specialists on euglenoids to increase our understanding of euglenoids biology and its translational applications. This could be useful to furthering our understanding of the evolution of parasitism, , , or supporting ”.

The Euglena International Network is an affiliated network to the Earth BioGenome Project and the International Society of Protistologists.

Leading image photo credit: Bożena Zakryś, EIN photo contest winner 2021

Inline photo credit: Phillip Siambi, Caleigh Mitchell, Denise Gibbs, Ryan Cullen, Tracy Richardson and Scott Farrow

In the UK, the space sector is worth over £16.4 billion per year and employs more than 45,000 people, while satellites and space tech underpins £360 billion per year of wider economic activity. Globally, projections reveal that the space economy

To optimise opportunities in this booming market, organisations such as the European Space Agency are looking to build space habitats, including a and ultimately . However, these types of ambitious projects will require breakthroughs in new materials to help construct resilient structures and infrastructure.

In response to this challenge, Dr Vivek Koncherry - a University alumnus and now CEO of Graphene Innovations 91ֱ��, a start-up based at the - is looking to build pressurised vessels that will create a modular space station for Low Earth Orbit. These pioneering vessels are to be made from graphene-enhanced carbon fibre as the addition of this 2D material will lightweight the habitat, as well as lending its thermal management properties to help regulate extremes of temperature.

Dr Koncherry has been working closely with global architects SOM, who have been studying the complexity of space habitation for many years as they look to .

As space explorers of the future look to go beyond the Earth’s orbit, travelling from a graphene space ship to begin building bases on the Moon – or even Mars – Dr Koncherry’s colleague Dr Aled Roberts, also part of the GEIC, is conducting research to develop bio-based building materials.

Dr Roberts, who is also part of the , explains that one of the biggest challenges for “off-world habitat construction” is the transportation of building materials, which can cost upwards of £1m 'per brick’. Until the conceptual can be built, one solution, says Dr Roberts, could be using local resources, such as lunar or Martian soil to make building materials. This thinking has led to proposed products like (aka extraterrestrial regolith biocomposites), a material using the local planetary soil and a bio-based binder to make sturdy bricks to build space habitats.

To support this lunar or Martian construction work, artificial intelligence (AI) researchers at 91ֱ�� - who are expert in developing autonomous systems and resilient AI-powered robots - have helped develop sophisticated software to enable ‘co-bots’ to aid astronauts in exploration, in construction and in monitoring these new structures.

This work has been led by Professor Michael Fisher and his colleagues that form the . A specialism at 91ֱ�� involves designing and building AI-powered autonomous robots that can work in the harshest of environment, such as space, and can reliably undertake a wide range of tasks “on their own”.

Previous research in this field has looked to support improved capability of NASA’s Astronaut-Rover teams and the 91ֱ�� team continue their collaboration with NASA. Future manned missions to the Moon and Mars are expected to use autonomous rovers and robots to assist astronauts during extravehicular activity (EVA), including science, technical and construction operations.

“An important feature of the 91ֱ�� work is to develop and apply systems making sure these robots are trustworthy and do what we expect,” explained Professor Fisher.

Once a space habitat has been built, its human occupants will need to survive in their new environment - and NASA researchers have identified hydroponics as a suitable method for growing food in outer space. 91ֱ�� agri-tech experts are looking at the future of food production, which includes the application of hydroponics in vertical farming production.

Dr Beenish Siddique, founder of (below) , a UK government-backed enterprise which is also based in the GEIC, is leading a team to develop a pioneering a hydrogel called GelPonics.

This growth medium conserves water and filters out pathogens to protect plants from disease, while automated technology includes the use of a graphene-based sensor that allows remote monitoring and management of the irrigation management system. This process is much less labour intensive and ultimately the GelPonics system is designed to be used in the harshest of environments.

Combining two strengths – advanced materials and trustworthy automation – to create a USP for space

Space is a fast-growing opportunity for exponential market growth - and provides an arena for the UK engineering sector to apply its world-leading expertise. The R&D being pioneered by experts at The University of Manchester to deliver revolutionary innovation in space habitat technology provides a model approach.

91ֱ�� has combined two of its key engineering strengths – advanced materials and autonomous systems – to find a unique proposition on space tech innovation.

Dr Vivek Koncherry says: “If you want to implement nanomaterials - or indeed the next generation of advanced materials - into space application you will also need automation.

“In 91ֱ��, everything comes together – you have expertise in both advanced materials and automated systems. The skilled people we need to work with are based in the same place, which creates a unique proposition.”

Dr Koncherry has built a pilot digital manufacturing line, designed to handle materials of the future by integrating robotics, AI and IoT systems in his state-of-the-art Alchemy Lab based in the GEIC (above). He has an ambition to grow the manufacturing base in Greater 91ֱ�� and from this provide a model to underpin the UK’s national capability to making advanced products.

"Dr Koncherry adds: “Space is at the tipping point of being accessible to the commercial mainstream - the opportunities this provides are boundless. Just like in the original industrial revolution, 91ֱ�� now finds itself with the right innovation at the right time to capitalise on the space revolution.”

To find out more about The University of Manchester’s contribution to the space sector read: 

The beer is uniquely brewed using a novel strain of yeast, a hybrid, developed by the the (MIB) and Cloudwater.

‘Tales From The Future’ will be available in a limited batch directly from the Cloudwater website. The 750ml bottles are available to buy singly or as a pack. This 91ֱ��-made beer will also be available from Cloudwater’s taproom.

Budding yeast has been integral to beer brewing since its conception, and recent discoveries of new wild yeast species have paved the way for exploiting the extant biodiversity in strain development. In 2017, Professor Daniela Delneri, from the MIB, and her team, isolated a new natural yeast species, Saccharomyces jurei, high up in the foothills of the French Alps.

It is set apart from other similar brewing yeasts as it has the ability to thrive at lower temperatures, has a different flavour profile, and is able to ferment maltose and maltotriose, two abundant sugars present in the wort. This opened up an array of new possibilities for brewers, including the development of new breeding protocols to combine the S. jurei genome with the genomes of commercially available strains to create a multitude of hybrids with different fermentation characteristics.

It is from this discovery that Paul Jones, CEO of Cloudwater Brew Co. first saw the potential opportunity to work with the MIB to create a yeast specific to Cloudwater’s needs. In a recent study, supported by a Knowledge Transfer Partnership (KTP) with Cloudwater Brew Co., Delneri’s team and KTP Associate Konstantina Giannakou, they crossed this newly discovered yeast strain with a common ale yeast (Saccharomyces cerevisae) to produce new starter hybrid strains that could influence the aroma and flavour profile of the beer.

Paul said of the partnership: “We are excited to be launching this beer following on from our work with The University of Manchester. This beer represents the possibilities of joining academia with industry and the importance of projects facilitated by this Knowledge Transfer Partnership. We cannot wait to share the fruits of our labour.”

Professor Daniela Delneri says: “It is brilliant to be able to work directly with Cloudwater Brew Co. to realise the potential of our new yeast species. Based on our work, S. jurei’s hybrids afford brewers more flexibility and options when brewing beers with different flavours and aromas. From here we can build on our work to create new yeast strains for different brewing needs.

“In fact, we have now also developed a method to turn typically sterile yeast hybrids into fertile cells able to produce a plethora of offspring which can be screened for desirable biotechnological traits. Such advances allow us to combine and select desirable traits from different yeast species via multigenerational breeding, paving the way for a swathe of new and exciting products”.

To launch the beer, Cloudwater Brew Co., in partnership with the MIB, will be hosting an event at the Cloudwater Taproom on Thursday 25 August.  Additionally, at 7pm a dedicated tasting session will take place where ‘Tales From The Future’ will feature alongside five other beers from the Barrel Project. More information

To illustrate the utility of their platform, they have engineered an enzyme that can successfully degrade poly(ethylene) terephthalate (PET), the plastic commonly used in plastic bottles. 

In recent years, the enzymatic recycling of plastics has emerged as an attractive and environmentally friendly strategy to help alleviate the problems associated with plastic waste. Although there are a number of existing methods for recycling plastics, enzymes could potentially offer a more cost-effective and energy efficient alternative. In addition, they could be used to selectively breakdown specific components of mixed plastic waste streams that are currently difficult to recycle using existing technologies.  

Although promising as a technology, there are considerable hurdles that need to be overcome for enzymatic plastic recycling to be used widely on a commercial scale. One challenge, for instance, is that natural enzymes with the ability to break down plastics typically are less effective and are unstable under the conditions needed for an industrial-scale process.  

To address these limitations, in a paper released today in , researchers from The University of Manchester have reported a new enzyme engineering platform that can quickly improve the properties of plastic degrading enzymes to help make them more suitable for plastic recycling at large scales. Their integrated and automated platform can successfully assess the plastic degradation ability of around 1000 enzyme variants per day.  

Dr Elizabeth Bell, who led the experimental work at the MIB, says of the platform; “The accumulation of plastic in the environment is a major global challenge. For this reason, we were keen to use our enzyme evolution capabilities to enhance the properties of plastic degrading enzymes to help alleviate some of these problems.  We are hopeful that in the future our scalable platform will allow us to quickly develop new and specific enzymes are suitable for use in large-scale plastic recycling processes.”

To test their platform, they went on to develop a new enzyme, HotPETase, through the directed evolution of IsPETase. IsPETase is a recently discovered enzyme produced by the bacterium Ideonella sakaiensis, which can use PET as a carbon and energy source. 

While IsPETase has the natural ability to degrade some semi-crystalline forms of PET, the enzyme is unstable at temperatures above 40°C, far below desirable process conditions. This low stability means that reactions must be run at temperatures below the glass transition temperature of PET (~65°C), which leads to low depolymerisation rates. 

To address this limitation, the team developed a thermostable enzyme, HotPETase, which is active at 70°C, which is above the glass transition temperature of PET.  This enzyme can depolymerise semi-crystalline PET more rapidly than previously reported enzymes and can selectively deconstruct the PET component of a laminated packaging material, highlighting the selectivity that can be achieved by enzymatic recycling.  

 Professor Anthony Green, Lecturer in Organic Chemistry, said: “The development of HotPETase nicely illustrates the capabilities of our enzyme engineering platform. We are now excited to work with process engineers and polymer scientists to test our enzyme in real world applications.  Moving forward, we are hopeful that our platform will prove useful for developing more efficient, stable, and selective enzymes for recycling a wide range of plastic materials.”

The development of robust plastic degrading enzymes such as HotPETase, along with the availability of a versatile enzyme engineering platform, make important contributions towards the development of a biotechnological solution to the plastic waste challenge. To move this promising technology forward will now require a collaborative and multidisciplinary effort involving biotechnologists, process engineers and polymer scientists from across the academic and industrial communities. With the world facing an ever-mounting waste problem, biotechnology could provide an environmentally sustainable solution. 

Biotechnology is one of the University’s research beacons – exemplars of interdisciplinary collaboration and cross-sector partnerships that lead to pioneering discoveries and improve the lives of people around the world. manchester.ac.uk/biotechnology-research  

Fuels such as this could be a way to bridge the gap between petrochemical derived fuels and cleaner energy sources. In industries such as aviation and shipping, where electrically powered vessels are currently impractical, advanced synthetic fuels offer a more sustainable alternative.

While not yet developed at an industrial scale, the team behind this advancement, which included colleagues from the Chemistry Department at The University of Manchester, were able to produce 15 litres of synthetic kerosene, enough to power a 4-meter drone for 20 minutes. Additionally, the process does not require any large-scale infrastructure and so can be made anywhere. This makes it an appealing prospect for companies and other stakeholders, including the RAF, as it could be rolled out across supply chains around the world.

With net zero and carbon emissions targets at the top of the global agenda, synthetic fuels will have a key part to play in countries achieving these goals. The RAF recently committed to finding more sustainable alternatives to fossil-derived aviation fuels, and with support from companies like C3 BIOTECH, they are one step closer to this. Eventually, similar fuel technologies will be available for commercial, as well as military applications which will further help to reduce the world’s carbon emissions.

New research published today in describes the use of natural enzymes and earth-abundant and non-toxic transition metal-catalysts to forge organic molecules, creating what is known as an amide bond, in a more efficient and sustainable manner.

Amide bonds are very important both in natural and non-natural molecules. All living organisms are made up of proteins that are held together by amide bonds which link carbon and nitrogen atoms of amino acid building blocks. Amide bonds are also present in many important pharmaceuticals that help to keep the population healthy, agrochemicals that increase crop yields and materials such as textiles.

Traditional chemical processes used to create amide bonds are unsustainable, rely on non-renewable ingredients, harmful and wasteful reagents, along with dangerous solvents, all of which lead to difficulties in purification and waste processing. To overcome these problems a team of scientists from the University of Manchester created a new method for combining natural and synthetic catalysts to overcome these issues.

Professor of Chemical Biology in the 91ֱ�� Institute of Biotechnolgy (MIB) who led the team said: “We are confident that the integrated approach we have developed can deliver important chemicals using environmentally friendly conditions at an industrial scale.

“We used bacterial cells with enzymes produced inside. Using cells prevents the enzymes coming into contact with the metal catalyst which can cause mutual deactivation. This enables very efficient production of diverse and important amide products.”

Research Fellow and co-author of the study added: “The main advantage is our process can be carried out in water instead of organic solvents that are normally used, which are toxic, flammable, harmful to user and damaging to the environment. Additionally, most existing methods are not selective, require multiple steps and lead to by-products. Our method overcomes these issues, delivering the valuable amides product we need in a clean and high yielding single process.”

The researchers used nitrile hydratase enzymes in combination with non-toxic and earth abundant copper metal catalysts. It is not normally possible to combine these different catalysts as they inactivate each other, hence they are usually used in costly multi-step processes. The team found that by using bacterial cells with the enzyme inside they were able to overcome the compatibility issues and develop an integrated process providing a more direct and environmentally friendly route. The researchers envisage that such integrated processes can revolutionise the way we make molecules for a more sustainable future.

The paper: Merging Enzymes with Chemocatalysis for Sustainable Amide Bond Synthesis. L. Bering, E. J. Craven, S. A. Sowerby Thomas, S. A. Shepherd & J. Micklefield, is published in 2022

Researchers from The University of Manchester have discovered a new way of manipulating key assembly line enzymes in bacteria which could pave the way for a new generation of antibiotic treatments.

New research published today in , describes how CRISPR-Cas9 gene editing can be used to create new nonribosomal peptide synthetase (NRPS) enzymes that deliver clinically important antibiotics. NRPS enzymes are prolific producers of natural antibiotics such as penicillin. However, up until now, manipulating these complex enzymes to produce new and more effective antibiotics has been a major challenge.

The antimicrobial resistance () infections are estimated to cause 700,000 deaths each year globally and are predicted to rise to 10 million, costing the global economy $100 trillion, by 2050. AMR also threatens many of the UN’s Sustainable Development Goals (SDGs), with an extra 28 million people that could be forced into extreme poverty by 2050 unless AMR is contained.

The 91ֱ�� team says the gene editing process could be used to produce improved antibiotics and possibly lead to the development of new treatments helping in the fight against drug-resistant pathogens and illnesses in the future. , Professor of Chemical Biology at the 91ֱ�� Institute of Biotechnology (), UK, explains: “The emergence of antibiotic-resistant pathogens is one of the biggest threats we face today.”

“The gene editing approach we developed is a very efficient and rapid way to engineer complex assembly line enzymes that can produce new antibiotic structures with potentially improved properties.”

Microorganisms in our environment, such as soil dwelling bacteria, have evolved nonribosomal peptide synthetase enzymes (NRPS) that assemble building blocks called amino acids into peptide products which often have very potent antibiotic activity. Many of the most therapeutically important antibiotics, used in the clinic today, are derived from these NRPS enzymes (e.g. penicillin, vancomycin and daptomycin).

Unfortunately, deadly pathogens are emerging which are resistant to all of these existing antibiotic drugs. One solution could be to create new antibiotics with improved properties that can evade the resistance mechanisms of the pathogens. However, the nonribosomal peptide antibiotics are very complex structures which are difficult and expensive to produce by normal chemical methods. To address this, the 91ֱ�� team use gene editing to engineer the NRPS enzymes, swapping domains that recognise different amino acid building blocks, leading to new assembly lines that can deliver new peptide products.

Micklefield added: “We are now able to use gene editing to introduce targeted changes to complex NRPS enzymes, enabling alternative amino acids precursors to be incorporated into the peptide structures. We are optimistic that our new approach could lead to new ways of making improved antibiotics which are urgently needed to combat emerging drug-resistant pathogens.”

The research paper is published in Nature Communications:

by; W. L. Thong, Y. Zhang, Y. Zhuo, K. J. Robins, J. K. Fyans, A. J. Herbert, B. J. C. Law & J. Micklefield* Nature Commun. 2021.

The Great British Entrepreneur Awards, in partnership with Starling Bank, acknowledges and champions the hard work and inspiring stories of entrepreneurs and businesses across the UK

91ֱ�� BioGel is a spinout company from the 91ֱ�� Institute of Biotechnology and owes its start to seed funding from the Faculty of Science and Engineering. The company produces PeptiGels and Peptilinks (synthetic hydrogels) that are used for tissue engineering, regenerative medicine, and drug discovery applications. Their work has pioneered the hydrogel space by offering cheaper and more bespoke hydrogel solutions to industry that can act as a scaffold for a range of tissue and cell cultures.

Aline will join 1,200 other entrepreneurs at the award ceremony on Monday 22 November at Grosvenor House in London. The event will see all eight regional shortlists brought together to crown the winners of each region.

In attendance will be judges, mentors, investors, and partners who will celebrate the unrivalled creativity, ambition, and resilience of entrepreneurship in the United Kingdom.

Over the last decade, the awards have celebrated some household names including Julie Deane OBE of Cambridge Satchel Co, Alan and Juliet Barratt of Grenade and Shaun Pulfrey of Tangle Teezer, as well as Steven Bartlett, the BBC’s Dragons Den’s youngest ever Dragon.

You can find out more about Aline in her recent International Women’s Day interview, and the .

The newly created hybrid yeast strains have been shown to successfully breed and produce offspring with specific desirable characteristics required for the beverage manufacturing process.

Naturally, hybrid yeasts are infertile, and their specific characteristics cannot be passed on. This previously required brewers to use selective methods to achieve the desired traits and has meant that the fermentation industries have so far missed out on potential new characteristics that the large genetic diversity of yeast hybrids affords.

The type of yeast used in the fermentation process influences how a beer tastes once it has been brewed. There are currently two main categories of yeasts, ale and lager, plus hundreds of variations used by modern day brewers in a booming global industry. Developing yeasts to give new flavours has been a goal of many brewers since the 1800s.

Now, as reported in the (PNAS), Professor Daniela Delneri, Professor of Evolutionary Genomics at the  and her team have succeeded in producing fertile yeast hybrids that are able to breed and generate a large number of progenies with diverse genetic traits.

Professor Delneri, lead author of the research said: “This research tackles the fundamental issue of hybrid sterility and multigenerational breeding. With my colleague Professor Ed Louis at the University Leicester, we were able to overcome species barriers and pinpoint the genetic traits unique to the hybrids. This technology has the ability to revolutionise the current practices for strain selection by allowing, via breeding, the rapid creation of efficient tailored yeasts carrying specific, novel, and important traits.

"As well as opening opportunities in food and drink production, this approach could be used to develop novel yeast “cell factories” that could be used in the field of industrial biotechnology to sustainably biomanufacture pharmaceuticals, chemicals and fuels.”

This research demonstrates how the potential for enhancing natural biodiversity and developing new hybrids is greater than expected and will offer new ways for industry to generate new and exciting consumer choices.

This research was carried out as part of a BBSRC-funded project in collaboration with SAB-Miller and – the world’s largest brewer. It also featured as part of the EU .

Dr. Philippe Malcorps, AB-InBev ‘yeast guru’, said "We are excited by these findings and pleased to have been able to support this research. The proof of concept opens doors to new innovations we can bring to our portfolio offering exciting new flavours via fermentation."

Researchers from (MIB), led by Professor Nicholas Turner, Dr Sarah Lovelock and Professor Anthony Green, have developed an efficient biocatalytic manufacturing route to Molnupiravir. Experimental work was led by Dr Ashleigh Burke who developed a new enzyme, cytidine aminotransferase, to allow the production of a key Molnupiravir intermediate.

The unique approach of the 91ֱ�� team is currently being further developed with industrial partners at multi-Kg scale to enable adoption by generic pharmaceutical manufacturers at large scale.

Professor Anthony Green said: “We are hopeful that our work will contribute to the challenge of developing a low-cost manufacturing route to Molnupiravir to allow the widest possible access to this promising COVID-19 therapy.”

The research undertaken by The University of Manchester team has been to allow pharmaceutical manufacturers around the world to take advantage of this development.

Sterling Pharma Solutions, a pharmaceutical contract development and manufacturing organisation (CDMO), has been engaged to support scale-up development and manufacturing activities utilising the novel enzyme developed by the 91ֱ�� team. Sterling’s CEO, Kevin Cook, said: “We are incredibly proud to be working in partnership will all those involved to help improve global access to what looks to be a very promising, life-saving treatment.”

In order to maximise the impact of the new enzyme technology, Prozomix Ltd, a biocatalyst discovery and contract manufacturing organisation (CMO), will employ foundation funds to produce high-quality cytidine aminotransferase and distribute it globally free-of-charge. Any company can obtain a sample by emailing Molnupiravir@prozomix.com.

Prozomix's Managing Director, Professor Simon Charnock, said: "Establishing a new and widely employable biocatalytic route for an API has arguably never been as urgent, we feel most privileged to play our part in this collaboration."

PET plastic has long been a concern due to the sheer volume of plastic created globally and its impact through non-recycled waste on the environment of drinking bottles, take-away containers and micro plastics.

Part of the reason plastic is difficult to break down is its chemical structure, which is made up of monomers – small molecules which are bonded together to form polymers. To date there have been many studies on the ability of bacteria to degrade PET plastic down into the constituent monomers. However, there has been limited study on the ability of these bacteria to recognise and uptake the corresponding monomers into their cells.

In new research published today in the journal, , researchers from studied the recognition potential of a key protein involved in cellular uptake of the monomer terephthalate (TPA), by the solute binding protein TphC.

and often plastic packaging is used only once. Despite a rise in home and industrial recycling efforts there still exists a systemic problem but also a business opportunity. Developing microbial degradation of plastics could be key in tackling this global issue.

The 91ֱ�� team used biochemical and structural techniques to determine how the substrate, TPA is recognised by TphC. Dr Neil Dixon, lead author of the research said: “Understanding how bacteria recognise and degrade xenobiotic chemicals, is important both from an ecological and biotechnological perspective. Understanding at a molecular level how these plastic breakdown products are imported into bacteria cells means that we can then use transporters in engineered cells for bioremediation applications to address pressing environment concerns.”

Using techniques which allowed the team to visualise the TphC in both open and closed conformations upon TPA binding, they then used genome mining approaches to discover homologous transporter proteins and also enzymes involved in TPA breakdown and assimilation.

These mined genomic parts provide a genetic resource for future biotechnological and metabolic engineering efforts towards circular plastic bio-economy solutions. There is great interest and potential in the use of engineered enzymes and microbes to degrade and assimilate waste plastic.

These new findings will now support the development engineered microbial cells for bio-remediation and bio-based recycling of plastic waste.

The paper, , is published in the journal Nature Communications.

Biotechnology is one of The University of Manchester’s - examples of pioneering discoveries, interdisciplinary collaboration and cross-sector partnerships that are tackling some of the biggest questions facing the planet. #ResearchBeacons

In their study, published in , a protein from human blood, combined with a compound from urine, sweat or tears, could glue together simulated moon or Mars soil to produce a material stronger than ordinary concrete, perfectly suited for construction work in extra-terrestrial environments.

The cost of transporting a single brick to Mars has been , meaning future Martian colonists cannot bring their building materials with them, but will have to utilise resources they can obtain on-site for construction and shelter. This is known as in-situ resource utilisation (or ISRU) and typically focusses on the use of loose rock and Martian soil (known as regolith) and sparse water deposits. However, there is one overlooked resource that will, by definition, also be available on any crewed mission to the Red Planet: the crew themselves.

In an article published today in the journal Materials Today Bio, scientists demonstrated that a common protein from blood plasma – human serum albumin – could act as a binder for simulated moon or Mars dust to produce a concrete-like material. The resulting novel material, termed AstroCrete, had compressive strengths as high as 25 MPa (Megapascals), about the same as the 20–32 MPa seen in ordinary concrete.

However, the scientists found that incorporating urea – which is a biological waste product that the body produces and excretes through urine, sweat and tears – could further increase the compressive strength by over 300%, with the best performing material having a compressive strength of almost 40 MPa, substantially stronger than ordinary concrete.

Dr Aled Roberts, from The University of Manchester, who worked on the project, said that the new technique holds considerable advantages over many other proposed construction techniques on the moon and Mars.

“Scientists have been trying to develop viable technologies to produce concrete-like materials on the surface of Mars, but we never stopped to think that the answer might be inside us all along”, he said.

The scientists calculate that over 500 kg of high-strength AstroCrete could be produced over the course of a two-year mission on the surface of Mars by a crew of six astronauts. If used as a mortar for sandbags or heat-fused regolith bricks, each crew member could produce enough AstroCrete to expand the habitat to support an additional crew member, doubling the housing available with each successive mission.

Animal blood was historically used as a binder for mortar. “It is exciting that a major challenge of the space age may have found its solution based on inspirations from medieval technology”, said Dr Roberts.

The scientists investigated the underlying bonding mechanism and found that the blood proteins denature, or “curdle”, to form an extended structure with interactions known as “beta sheets” that tightly holds the material together.

“The concept is literally blood-curdling,” Dr Roberts explained.

The newly published findings are the result of collaborative work between Global Bioenergies and the team of Dr. David Leys at The University of Manchester, and have been published today in . This paper describes the evolution and mechanism of isobutene forming enzymes far superior to previously used catalysts. Isobutene is a high value gaseous hydrocarbon, and one of the major building blocks of the petrochemicals industry: 15 million tonnes are produced every year to yield cosmetic ingredients, rubber and fuels.

This is the first time a member of a widespread enzyme family that depends on an unusual vitamin B2 derivative has been repurposed to yield isobutene. This has been made possible through the extensive work performed on both sides of the Channel, with laboratory guided evolution carried out at Global Bioenergies, and detailed structure analysis of the the evolved enzymes at The University of Manchester.

David Leys, group leader at the 91ֱ�� Institute of Biotechnology of The University of Manchester, says: “Our collaboration with Global Bioenergies on the subject of isobutene production combines in a unique manner quantitative molecular bioscience and industrial, high-throughput approaches. It is very satisfying to see how fundamental understanding of these enzymes obtained with European Research Council funding supports industrial application. The evolved enzymes represent several orders of magnitude improvement in the efficiency of isobutene bioproduction, directly contributing to an economically viable and renewable process, and thus a more sustainable future.”

Marc Delcourt, co-founder and CEO of Global Bioenergies, adds: “Nature Communications stands among the high-class peer-reviewed scientific journals. We are very pleased to see the work we conducted jointly with the team of Dr David Leys reaches such a striking scientific recognition. The evolved enzymes, on which GBE holds exclusive intellectual property rights for the isobutene production, will have a significant role in the environmental transition our world is now engaged in.”

As an alternative to fossil fuel derived isobutene, Global Bioenergies assembled a modified pathway for the production of isobutene from glucose. The crucial final step yielding the desired product makes use of a decarboxylase enzyme. This particular enzyme has been evolved from naturally occuring microbial decarboxylases that depend on an elaborately modified Vitamin B2 (called prenylated flavin or prFMN) for activity.

The 91ֱ�� group has been at the forefront of studying these prFMN-dependent catalysts, and determined structure and biochemical properties of isobutene yielding enzymes evolved by Global Bioenergies. The company screened an enzyme library for inherent isobutene production activity, and used directed evolution to yields variants with up to an 80-fold increase in activity. Structure determination of the evolved catalysts reveal that changes in the enzyme pocket are responsible for improved production, while solution and computational studies suggest that isobutene release is currently the limiting factor.

Global Bioenergies has developed a unique conversion process for renewable resources into isobutene, one of the main petrochemical building blocks that can be converted into ingredients for cosmetics, petrol, kerosene, LPG and plastics.

The key topics that will be discussed include:

• Emerging trends in research and development
• Data reporting, survey and statistics
• Analysis of sectors including life sciences, manufacturing, agriculture, and energy
• Emerging technologies, such as automation, AI and VR

Professor Scrutton will be joined by policymakers such as Nadhim Zahawi MP, Minister for BEIS and COVID-19 Vaccine Deployment, and Chi Onwurah MP, Shadow Minister for Science, Research and Digital, as well as business leaders such as Andy Topping, Chief Scientific Officer at Fujifilm Diosynth Biotechnologies, and sector specialists such as Professor Lionel Clarke, Chair of the UK Synthetic Biology Leadership Council.

The live panel and Q&A will discuss how UK industry - responsible for a quarter of the UK's greenhouse gas emissions - can use biotechnology to reduce its carbon footprint and contribute to the UK's net zero goals. Specifically, they will focus on how biotechnology can create more sustainable chemicals for agriculture, more efficient and greener fuels for transport, and close the gap in our economy to create a circular economy.

The event will start at 2.30pm on Thursday, 15 July. To book tickets, please .

For more information about how The University of Manchester’s biotechnology research is supporting the UK's net zero goals, please visit the net zero campaign page.

Biotechnology is one of the University's research beacons - examples of pioneering discoveries, interdisciplinary collaboration and cross-sector partnerships that are tackling some of the biggest challenges facing the planet.