An electrolysis technique developed at JGU could make an important contribution to the electrification of the chemical industry
Johannes Gutenberg Universitaet Mainz
image:
Professor Dr. Carsten Streb (l.) and Dr. Soressa Abera Chala of the Department of Chemistry at JGU who developed the new electrolysis technique with which formate and hydrogen can be obtained from glycerol
view moreCredit: photo/©: Tobias Rios-Studer
Researchers at Johannes Gutenberg University Mainz (JGU) have developed a method which gives access to the valuable raw materials formate and hydrogen from the waste product glycerol. Formates are the salts of formic acid and are widely used in the chemical industry, while hydrogen can serve, for example, as an energy carrier to power vehicles. The new method can be operated with sustainable electricity and does not produce CO2. The results of the research have been recently published by the team in the journal Advanced Energy Materials. Professor Carsten Streb of JGU's Department of Chemistry, who supervised the study, pointed out: "The approach we have devised could make a significant contribution to the electrification of the chemical industry. This is a major driver for large-scale commercial developments to reduce industrial CO2 emissions. Processes which currently require considerable amounts of petroleum or natural gas could in future be operated using sustainable electricity."
CO2-neutral production of formate
The new process is based on the established method of water electrolysis. This involves the use of electricity to split water into hydrogen and oxygen. Employing so-called hybrid electrolysis, the researchers used glycerol in addition to water as a source material; the former is created in large quantities as a byproduct of biodiesel production. The second product generated during electrolysis was thus the corresponding formate rather than oxygen. Formates are usually produced from petroleum, but the corresponding process is associated with the emission of large amounts of CO2. Streb added: "On the other hand, the electrochemical generation of formates from glycerol is CO2-neutral if it is undertaken using green electricity." In chemical terms, what the researchers have achieved by means of their electrolysis of glycerol is to break down the glycerol, which has a three-carbon atom backbone, to create a formate that contains just a single carbon atom.
New catalyst developed
The new process is based on an innovative catalyst developed by the researchers. On the molecular level, the catalyst combines in close vicinity the two metals copper and palladium. Streb revealed: "We have not only managed to create this catalyst, but already have a very good idea what the material does and how we can optimize its operation." Theoretical and experimental insights into this were provided by a cooperating team at the National Taiwan University of Science and Technology.
Subsequently, the team headed by Streb plans to investigate whether it is possible to replace the expensive noble metal palladium in the catalyst with earth-abundant metals. The team also targets the development of a new method to convert formate into methanol – the demand for methanol is substantially greater than that for formate. This may prove possible by means of the introduction of a second reductive electrolysis process.
Developments in the SusInnoScience Top-level Research Area
The research performed at JGU was undertaken in the context of the Top-level Research Area SusInnoScience (Sustainable chemistry as the key to innovation in resource-efficient science in the Anthropocene), the purpose of which is to develop sustainable chemical and biotechnological production processes. This Top-level Research Area at JGU is funded through the Research Initiative of the State of Rhineland-Palatinate. The corresponding work was additionally a feature of the Sustainable Processes and Materials program of the Rhine-Main Universities (JGU, Goethe University Frankfurt am Main, and Technical University of Darmstadt). It is also noteworthy that five of the postdocs involved were sponsored by the Alexander von Humboldt Foundation. "This is an international project that benefits considerably from the fact that we are able to recruit international talent through the Humboldt Foundation," concluded Streb.
Journal
Advanced Energy Materials
Method of Research
Experimental study
Subject of Research
Not applicable
Article Title
Molecular Bottom-Up Design of Single-Site Copper-Palladium Catalysts for Selective Glycerol Electro-Oxidation
Article Publication Date
22-Jan-2026
Biosynthesis of medicarpin in engineered
yeast
Nanjing Agricultural University The Academy of Science
Developing an efficient biosynthesis method, therefore, is a key step in making the production of this antitumor and antibacterial isoflavonoid efficient and sustainable.
While the Fabaceae plant family from which medicarpin is extracted is quite common and includes peas, alfalfa, acacia, and carob, the substance is in relatively low quantities within those plants. Furthermore, crops are susceptible to climate fluctuations and land use restrictions. Chemical synthesis is still a multi-step process beset by high production costs and environmental pollution concerns.
With a ready supply, medicarpin could become more widely used in the treatment of osteoporosis, inflammatory disease, and other indications.
As senior author Yongjun Wei, Chengwei Li, and colleagues at Zhengzhou University, the University of Nottingham, and Henan University of Technology, point out in a recent paper（DOI:10.1016/j.bidere.2026.100071 ）, “The biosynthesis of medicarpin in S. cerevisiae involves the coordination of multiple interconnected metabolic pathways, including glycolysis, the pentose phosphate pathway (PPP), the shikimate pathway, and the isoflavonoid biosynthesis pathway.”
“Synthetic biology and microbial biomanufacturing represent a powerful, third paradigm for producing complex natural productions,” Wei tells GEN. “This platform has the potential to provide a reliable, scalable, environmentally friendly source of bioactive compounds…potentially overcoming supply chain and sustainability challenges associated with conventional methods.”
The team’s success hinged upon developing yeast strains adept at flavonoid synthesis. Ultimately, they engineered 26 strains of S. cerevisiae, overexpressing and mutating endogenous yeast genes that were vital for flavonoid synthesis, and creating a downstream flavonoid biosynthetic pathway in engineered yeasts.
Medicarpin production peaked at more than 157 μg/L in the GlaN26 strain. Optimization involved organelle engineering to knock out or knock down genes in competing pathways or with inhibitory transcription factors that would affect the targeted metabolic pathways, Wei, Li, and colleagues report.
Engineered S. cerevisiae has been used previously to generate a variety of natural products, such as cycloastragenol, which activates telomerase and has been associated with telomer elongation.
This method currently produces relatively small quantities of medicarpin, however. “The current titers remain orders of magnitude below commercially viable levels,” Wei says, and significant improvements in production efficiency and yield are essential before scale-up is feasible.”
“Our primary challenge lies in advancing the technology from a laboratory proof-of-concept to a robust industrial process,” Wei adds. “Further genetic and metabolic engineering of the yeast strains to drastically improve titer, yield, and rate under scaled fermentation conditions is necessary.”
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References
DOI
Original Source URL
https://doi.org/10.1016/j.bidere.2026.100071
About BioDesign Research
BioDesign Research is dedicated to information exchange in the interdisciplinary field of biosystems design. Its unique mission is to pave the way towards the predictable de novo design and assessment of engineered or reengineered living organisms using rational or automated methods to address global challenges in health, agriculture, and the environment.
Journal
BioDesign Research
Method of Research
Experimental study
Subject of Research
Not applicable
Article Title
De novo biosynthesis of medicarpin in metabolically engineered yeast
New AI method revolutionizes the design of enzymes
Researchers at Graz University of Technology and the University of Graz can use the technology to construct artificial biocatalysts. These new enzymes are significantly faster, more stable and more versatile than previous artificial biocatalysts
Graz University of Technology
image:
From left: Adrian Tripp, Markus Braun and Gustav Oberdorfer from the Institute of Biochemistry at TU Graz as well as Mélanie Hall from the Institute of Chemistry at Uni Graz.
view moreCredit: IBC - TU Graz
Enzymes with specific functions are becoming increasingly important in industry, medicine and environmental protection. For example, they make it possible to synthesise chemicals in a more environmentally friendly way, produce active ingredients in a targeted manner or break down environmentally harmful substances. Researchers from Gustav Oberdorfer’s working group at the Institute of Biochemistry at Graz University of Technology (TU Graz), together with colleagues from the University of Graz, have now published a study in the scientific journal Nature describing a new method for the design of customised enzymes. The technology called Riff-Diff (Rotamer Inverted Fragment Finder–Diffusion) makes it possible to accurately and efficiently build the protein structure specifically around the active centre instead of searching for a suitable structure from existing databases. The resulting enzymes are not only significantly more active than previous artificial enzymes, but also more stable.
Highly efficient biocatalysts
“Instead of putting the cart before the horse and searching databases to see which structure matches an active centre, we can now design enzymes for chemical reactions efficiently and precisely from scratch using a one-shot process,” says Gustav Oberdorfer, whose ERC project HELIXMOLD was a key basis for this breakthrough. Lead author Markus Braun from the Institute of Biochemistry at TU Graz adds: “The enzymes that can now be produced are highly efficient biocatalysts that can also be used in industrial environments thanks to their stability. This drastically reduces the screening and optimisation effort previously required and makes enzyme design more accessible to the wider biotechnology community.”
This progress was made possible by new developments in machine learning, which allow the design of much more complex structures than previous methods. Riff-Diff combines several generative machine learning models with atomistic modelling. First, structural motifs of proteins are placed around an active centre, then a generative AI model called RFdiffusion generates the complete protein molecule structure. The researchers refine this scaffold step by step using other models so that the chemically active elements are placed in it with high precision – precision at the angstrom level (1 angstrom corresponds to 0.1 nanometres) was achieved as proven by experimentally determined high-resolution protein structures.
Evolutionary short-cut
The team successfully confirmed how well the method works in the laboratory. Active enzymes for different reaction types have already been generated from 35 tested sequences. The new catalysts were significantly faster than previous computer-aided designs. In addition, the new enzymes showed high thermal stability and almost all retained their functional shape up to 90 degrees Celsius or more, which is particularly relevant for use in industrial applications. Lead author Adrian Tripp from the Institute of Biochemistry at TU Graz adds: “Although nature itself produces a large number of enzymes through evolution, this takes time. With our approach, we can massively accelerate this process and thus contribute to making industrial processes more sustainable, developing targeted enzyme therapies and keeping the environment cleaner.”
This breakthrough was also made possible by the interdisciplinary collaboration between TU Graz and the University of Graz. Mélanie Hall from the Institute of Chemistry at the University of Graz confirms the strength of the collaboration: “The integration of different areas of expertise at the interface of protein science, biotechnology and organic chemistry shows how crucial interdisciplinary approaches are for the advancement of modern biocatalysis.”
Publication: Computational enzyme design by catalytic motif scaffolding
Authors: Markus Braun, Adrian Tripp, Morakot Chakatok, Sigrid Kaltenbrunner, Celina Fischer, David Stoll, Aleksandar Bijelic, Wael Elaily, Massimo G. Totaro, Melanie Moser, Shlomo Y. Hoch, Horst Lechner, Federico Rossi, Matteo Aleotti, Mélanie Hall, Gustav Oberdorfer
In: Nature
DOI: https://doi.org/10.1038/s41586-025-09747-9
Journal
Nature
Method of Research
Computational simulation/modeling
Subject of Research
Not applicable
Article Title
Computational enzyme design by catalytic motif scaffolding
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