| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 9604420 | Journal of Biotechnology | 2005 | 5 Pages |
Abstract
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.
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Authors
Shengdong Zhu, Yuanxin Wu, Ziniu Yu,