Enzyme beads for controlled alcohol oxidations in chemical synthesis
Lead Research Organisation:
University of Oxford
Department Name: Oxford Chemistry
Abstract
Biocatalysis offers great advantages in selectivity for oxidation of primary alcohols. Alcohol dehydrogenase enzymes are available for many alcohol oxidation steps, but a barrier to their implementation is their dependence on the cofactor NAD+. This project provides a novel solution to this challenge by developing enzyme beads that recycle NAD+ to oxidise primary alcohol functionalities in controlled ways, while releasing H2 gas as a bonus byproduct. This exploits a strong synergy between new cofactor recycling routes under development in the Vincent group and robust, broad-specificity alcohol dehydrogenase enzymes developed by the industrial partner, Johnson Matthey Catalysis and Chiral Technologies.
Publications
Reeve HA
(2017)
Enzymes as modular catalysts for redox half-reactions in H2-powered chemical synthesis: from biology to technology.
in The Biochemical journal
Studentship Projects
| Project Reference | Relationship | Related To | Start | End | Student Name |
|---|---|---|---|---|---|
| BB/M017095/1 | 01/10/2015 | 30/09/2019 | |||
| 1658860 | Studentship | BB/M017095/1 | 01/10/2015 | 30/09/2019 | Michalis Posidias |
| Description | We have results showing that we can increase the conversion and selectivity of alcohol to carbonyls using a number of enzymatic approaches; this is challenging to achieve with traditional chemical methods. The conversions achieved are already competitive with those described in the literature. |
| Exploitation Route | This type of chemical reaction is useful in a number of chemical sectors for the production of pharmaceuticals and other fine chemicals. |
| Sectors | Chemicals,Manufacturing, including Industrial Biotechology,Pharmaceuticals and Medical Biotechnology |
| URL | http://vincent.chem.ox.ac.uk/ |