Zhu Shengdong, Wu Yuanxin, Yu Ziniu
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.
J Biotechnol. 2005 Apr 6;116(4):397-401. doi: 10.1016/j.jbiotec.2004.12.012.
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.
皱褶假丝酵母脂肪酶（脂肪酶OF）通过共价结合固定在一种对pH敏感的载体上，该载体在pH变化时表现出可逆的可溶-不溶特性。固定化脂肪酶能够以可溶形式进行酮洛芬酯的对映选择性水解，并且通过简单调节pH沉淀后即可回收。与游离脂肪酶相比，其对酮洛芬2-氯乙酯水解的活性和对映选择性分别提高了1.5倍和8.7倍。经过八次催化循环后，固定化酶仍具有46%的活性，其对映选择性保持不变。
