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Two‐Step biocatalytic conversion of an ester to an aldehyde in reverse micelles
Author(s) -
Yang Fangxiao,
Russell Alan J.
Publication year - 1994
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260430307
Subject(s) - chemistry , micelle , lipase , hydrolysis , organic chemistry , candida antarctica , aldehyde , alcohol dehydrogenase , substrate (aquarium) , cofactor , biocatalysis , solvent , alcohol , redox , pulmonary surfactant , yeast , ether , oleyl alcohol , enzyme , catalysis , reaction mechanism , biochemistry , oceanography , aqueous solution , geology
Lipases from Candida cyclindracea (L‐1754) and wheat germ (L‐3001) have been used to hydrolyze esters to their corresponding alcohols and acids in reverse micelles. Alcohol dehydrogenase from baker's yeast (YADH) was subsequently used to reduce the alcohol products to aldehydes. Cofactor recycling in the redox reaction was achieved using a sacrificial cosubstrate, as described previously. Four surfactants (sodium dioctylsulfosuccinate, Nonidet P‐40 with Triton X‐35, polyoxyethylene, 10‐cetyl‐ether, polyoxyethylene sorbitan trioleate) were employed to determine the effect of amphiphile on ester hydrolysis and redox reaction rates separately. The effect of type of organic solvent, W 0 [(water]/[surfactant)], and substrate concentration on separte enzyme activity were also investigated. A brief investigation of a single phase, two‐step reaction catalyzed by the combination of lipase and YADH in reverse micelles is also reported. The activities of the enzymes are significantly different when used together instead of independently. © 1994 John Wiley & Sons, Inc.