Immobilization of Candida rugosa lipase on a pH-sensitive support for enantioselective hydrolysis of ketoprofen ester.
Candida rugosa lipase (Lipase OF) was immobilized by covalent binding to a pH-sensitive support showing reversibly soluble-insoluble characteristics with pH change. The immobilized lipase could carry out the enantioselective hydrolysis of ketoprofen ester in a soluble form yet be recovered after precipitation by simply adjusting pH. Its activity and enantioselectivity for hydrolysis of 2-chloroethyl ester of ketoprofen were enhanced 1.5-fold and 8.7-fold compared with those of free lipase. After eight catalytic cycles, the immobilized enzyme was still 46% active and its enantioselectivity remained unchanged.
Zhu
Shengdong
S
School of Chemical Engineering and Pharmacy, Wuhan Institute of Chemical Technology, Hubei Key Laboratory of Novel Chemical Reactor and Green Chemical Technology, Wuhan 430073, PR China. zhusd2003@21cn.com
Wu
Yuanxin
Y
Yu
Ziniu
Z
D002175:Candida / Q000201:enzymology*; D004789:Enzyme Activation; D004800:Enzymes, Immobilized / Q000737:chemistry; D004951:Esterification; D004952:Esters; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007536:Isomerism; D007660:Ketoprofen / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry*; D008567:Membranes, Artificial
D004800:Enzymes, Immobilized; D004952:Esters; D008567:Membranes, Artificial; D007660:Ketoprofen; D008049:Lipase