Enantioselective oxidation of secondary alcohols by quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni

article


Stigter, E.C.A.

Lugt, J.P. van der

Somers, W.A.C.
Purified and reconstituted quinohaemoprotein alcohol dehydrogenase (QH-EDH) from Comamonas testosteroni is shown to oxidize secondary alcohols enantioselectively. The products formed during the oxidation of secondary alcohols were positively identified as the corresponding ketones. In the oxidation of chiral secondary n-alkyl alcohols a preference of the enzyme for the S( + )alcohols was found. The apparent kinetic parameters (Km and Vmax) for a range of n-alkyl alcohols depend on the length of the alcohol chain and the location of the hydroxyl function in the chain. The enzyme is stable up to a temperature of 37°C. Above this temperature the activity is irreversibly lost. The pH optimum of the enzyme in the conversion of secondary alcohols is 7.7.
Topics
















Alcohol oxidationEnantioselectivityQuinohaemoprotein alcohol dehydrogenaseSecondary alcoholsEnzyme kineticsEnzymesKetonesOxidationpHReaction kineticsThermal effectsThermodynamic stabilityComamonas testosteroniEnantioselectivityQuinohaemoprotein alcohol dehydrogenaseSecondary alcoholsAlcohols
TNO Identifier
233885
Repository link
https://resolver.tno.nl/uuid:97fc0a9d-6568-4ee4-b4a5-9d2b00aa574f
ISSN
13811177
Source
Journal of Molecular Catalysis B: Enzymatic, 2(6), pp. 291-297.
Pages
291-297
Files
To receive the publication files, please send an e-mail request to TNO Repository.