摘要
对根霉（Ｒｈｉｚｏｐｕｓｓｐ．Ｂｃ０－０９）脂肪酶的粗酶拆分（Ｒ，Ｓ）－环氧丙醇丁酸酯的水解反应进行了初步研究，结果表明：３０°Ｃ下ｐＨ５．３时反应初速度最大；ｐＨ５．５～６．０时酶的立体选择性最高，对映体比率（Ｅ值）为５７。４２°Ｃ下ｐＨ５．５时反应初速度最大；酶的立体选择性随温度升高而下降。酶促水解反应中未观察到产物和底物抑制现象。根霉发酵液中脂肪酶的反应特性与硫酸铵沉淀法所得粗酶相吻合。
The properties of crude lipase, extracted from Rhizopus sp. Bc009 useful to optical resolution of glycidyl butyrate were preliminarily investigated. The study on the effects of pH showed that the initial rate of hydrolysis at 30C was the highest at pH 5.3; the enzyme stereoselectivity was higher at pH 5.56.0, the enantiomeric ratio (E value) was 57. The optimal temperature was at 42C. The enzyme stereoselectivity showed a slight decrease as temperature rising. Both substrate and products caused no inhibition of hydrolysis reaction. The lipase in broth showed a characteristic similar to that of crude lipase.
出处
《华东理工大学学报（自然科学版）》
CAS
CSCD
北大核心
1999年第3期276-279,共4页
Journal of East China University of Science and Technology
基金
国家"九五"攻关课题
山东大学微生物技术国家重点实验室开放课题
关键词
环氧丙醇丁酸酯
脂肪酶
根霉
催化
水解
R,S)glycidyl butyrate
optical resolution
lipase
Rhizopus sp. Bc009
