Kamiya N, Kasagi H, Inoue M, Kusunoki K, Goto M
Department of Chemical Systems and Engineering, Graduate School of Engineering, Kyushu University, 6-10-1, Hakozaki, Fukuoka 812-8581, Japan.
Biotechnol Bioeng. 1999 Oct 20;65(2):227-32. doi: 10.1002/(sici)1097-0290(19991020)65:2<227::aid-bit14>3.0.co;2-u.
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. © 1999 John Wiley & Sons, Inc.
基于在异辛烷中醇与月桂酸酯化反应的动力学研究，阐明了源自皱褶假丝酵母和洋葱假单胞菌的脂肪酶对仲醇的对映选择性识别机制。为了获得内在动力学参数，我们使用了一种表面活性剂包覆的脂肪酶，其构象在均相有机溶剂中被认为是“开放”形式。根据实验结果，发现脂肪酶的对映选择性源自两种对映体之间V(max)值的差异。当应用不同来源的脂肪酶和具有不同分子结构的底物时，观察到了相同的结果。© 1999约翰威立国际出版公司
