TY - JOUR
T1 - Enantioselective recognition mechanism of secondary alcohol by surfactant-coated lipases in nonaqueous media
AU - Kamiya, Noriho
AU - Kasagi, Hideaki
AU - Inoue, Masahito
AU - Kusunoki, Koichiro
AU - Goto, Masahiro
PY - 1999/10/20
Y1 - 1999/10/20
N2 - The enantioselective recognition mechanism of secondary alcohol by lipases originated from Candida rugosa and Pseudomonas cepacia was elucidated on the basis of the kinetic study of the esterification of alcohol with lauric acid in isooctane. To obtain inherent kinetic parameters, we utilized a surfactant-coated lipase whose conformation is considered to be an 'open' form in a homogeneous organic solvent. Based on the experimental results, the enantioselectivity of lipases was found to be derived from the difference in the V(max) values between the two enantiomers. The same result was observed when lipases of different origin and substrates with different molecular structures were applied.
AB - The enantioselective recognition mechanism of secondary alcohol by lipases originated from Candida rugosa and Pseudomonas cepacia was elucidated on the basis of the kinetic study of the esterification of alcohol with lauric acid in isooctane. To obtain inherent kinetic parameters, we utilized a surfactant-coated lipase whose conformation is considered to be an 'open' form in a homogeneous organic solvent. Based on the experimental results, the enantioselectivity of lipases was found to be derived from the difference in the V(max) values between the two enantiomers. The same result was observed when lipases of different origin and substrates with different molecular structures were applied.
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U2 - 10.1002/(SICI)1097-0290(19991020)65:2<227::AID-BIT14>3.0.CO;2-U
DO - 10.1002/(SICI)1097-0290(19991020)65:2<227::AID-BIT14>3.0.CO;2-U
M3 - Article
C2 - 10458745
AN - SCOPUS:0033589368
SN - 0006-3592
VL - 65
SP - 227
EP - 232
JO - Biotechnology and Bioengineering
JF - Biotechnology and Bioengineering
IS - 2
ER -