Mould unlocks new route to biofuels!
Scientists at The University of Manchester have made an important discovery that forms the basis for the development of new applications in biofuels and the sustainable manufacturing of chemicals. Researchers have identified the exact mechanism and structure of two key enzymes isolated from yeast moulds that together provide a new, cleaner route to the production of hydrocarbons.
Published in back-to-back publications in Nature, the research offers the possibility of replacing the need for oil in current industrial processes with a greener and more sustainable natural process. Professor Leys and his team investigated in detail the mechanism whereby common yeast mould can produce kerosene-like odours when grown on food containing the preservative sorbic acid. They found that these organisms use a previously unknown modified form of vitamin B2 (flavin) to support the production of volatile hydrocarbons that caused the kerosene smell. Their findings also revealed the same process is used to support synthesis of vitamin Q10 (ubiquinone).
Using Diamond Light Source, the UK’s national synchrotron facility at Harwell, they were able to provide atomic level insights into this bio catalytic process, and reveal it shares similarities with procedures commonly used in chemical synthesis but previously thought not to occur in nature. In this particular study, researchers focussed on the production of alpha-olefins; a high value, industrially crucial intermediate class of hydrocarbons that are key chemical intermediates in a variety of applications, such as flexible and rigid packaging and pipes, synthetic lubricants used in heavy duty motor and gear oils, surfactants, detergents and lubricant additives.
Payne KA, White MD, Fisher K, Khara B, Bailey SS, Parker D, Rattray NJ, Trivedi DK, Goodacre R, Beveridge R, Barran P, Rigby SE, Scrutton NS, Hay S, Leys D. New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition. Nature. 2015 Jun 25;522(7557):497-501. doi: 10.1038/nature14560. Epub 2015 Jun 17. http://www.ncbi.nlm.nih.gov/pubmed/26083754
White MD, Payne KA, Fisher K, Marshall SA, Parker D, Rattray NJ, Trivedi DK, Goodacre R, Rigby SE, Scrutton NS, Hay S, Leys D. UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis. Nature. 2015 Jun 25;522(7557):502-6. doi: 10.1038/nature14559. Epub 2015 Jun 17. http://www.ncbi.nlm.nih.gov/pubmed/26083743