Cross-linked enzyme aggregates: A simple and effective method for the immobilization of penicillin acylase

被引：431

作者：

Cao, LQ ^{[1
]}

van Rantwijk, F ^{[1
]}

Sheldon, RA ^{[1
]}

机构：

[1] Organ Chem & Catalysis Lab, NL-2628 BL Delft, Netherlands

来源：

ORGANIC LETTERS | 2000年 / 2卷 / 10期

关键词：

D O I：

10.1021/ol005593x

中图分类号：

O62 [有机化学];

学科分类号：

070303 [有机化学]; 081704 [应用化学];

摘要：

Penicillin G acylase (penicillin amidohydrolase, E.C. 3.5.1.11) was immobilized in a simple and effective way by physical aggregation of the enzyme, using a precipitant, followed by chemical cross linking to form insoluble cross-linked enzyme aggregates (CLEAs), These had the same activity in the synthesis of ampicillin as cross-linked crystals of the same enzyme, but the accompanying hydrolysis of the side-chain donor was much less. Penicillin G acylase CLEAs also catalyzed the synthesis of ampicillin in a broad range of organic solvents.

引用

页码：1361 / 1364

页数：4

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