Tsai S W, Chiang C L
Department of Chemical Engineering, National Cheng Kung University, Tainan, Taiwan, Republic of China.
Biotechnol Bioeng. 1991 Jun 20;38(2):206-11. doi: 10.1002/bit.260380213.
Candida rugosa lipase has been used to investigate the hydrolysis of high concentration olive oil in the AOT-isooctane reversed micellar system at W(o) = 10, pH 7.1, and 37 degrees C. Results from this work show the hydrolytic reaction obeys Michaelis-Menten kinetics up to the initial substrate concentration of 1.37M, with turnover number k(cat) and Michaelis constant K(M) of 67.1 mumol/min mg enzyme and 0.717M, respectively. A competitive inhibition by the main product, oleic acid, has been found with a dissociation constant K(I) for the complex EP* of 0.089M. The rate equation was further analyzed in the time course reaction and was found in agreement with the experimental results for lower substrate concentrations, up to 0.341M. Large deviation occurred at high substrate concentrations, which may be due to the effects of large consumption of water on kinetics, on the formation of glycerol, and on the deactivation of lipase in the hydrolysis reaction as well.
皱褶假丝酵母脂肪酶已被用于研究在W(o)=10、pH 7.1和37℃条件下，AOT-异辛烷反胶束体系中高浓度橄榄油的水解情况。这项工作的结果表明，在初始底物浓度达到1.37M之前，水解反应遵循米氏动力学，转换数k(cat)和米氏常数K(M)分别为67.1μmol/(min·mg酶)和0.717M。已发现主要产物油酸存在竞争性抑制作用，复合物EP*的解离常数K(I)为0.089M。在时间进程反应中对速率方程进行了进一步分析，发现在底物浓度较低（最高0.341M）时与实验结果相符。在高底物浓度下出现了较大偏差，这可能是由于水解反应中大量消耗水对动力学、甘油形成以及脂肪酶失活的影响所致。
