Immobilization of lipase on a new inorganic ceramics support, toyonite, and the reactivity and enantioselectivity of the immobilized lipase

被引：61

作者：

Kamori, M

Hori, T

Yamashita, Y

Hirose, Y

Naoshima, Y

机构：

[1] Okayama Univ Sci, Fac Informat, Okayama 7000005, Japan

[2] Amano Pharmaceut, Nishiharu, Aichi 4818543, Japan

[3] Toyo Denka Kogyo, Kochi 7808525, Japan

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2000年 / 9卷 / 4-6期

关键词：

immobilization; inorganic support; lipase; acylation; biotransformation;

D O I：

10.1016/S1381-1177(99)00105-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A porous ceramics support, Toyonite 200-M (TN-M), for the immobilization of lipases was prepared hydrothermally from the minerals of kaolinite. Compared with some other commercial solid supports, the TN-M one exhibited better stability and higher selectivity for lipase proteins, and lipase PS (Pseudomonas cepacia) immobilized on the ceramics support showed higher reactivity for organic substrates than the free crude enzyme. (C) 2000 Elsevier Science B.V. All rights reserved.

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页码：269 / 274

页数：6

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