Preparation, optimization, and structures of cross-linked enzyme aggregates (CLEAs)

被引：415

作者：

Schoevaart, R

Wolbers, MW

Golubovic, M

Ottens, M

Kieboom, APG

van Rantwijk, F

van der Wielen, LAM

Sheldon, RA

机构：

[1] Delft Univ Technol, Dept Biotechnol, NL-2628 BL Delft, Netherlands

[2] Delft Univ Technol, Dept Biotechnol, NL-2628 BC Delft, Netherlands

[3] Leiden Univ, Ind Fermentat Chem, NL-2300 RA Leiden, Netherlands

来源：

BIOTECHNOLOGY AND BIOENGINEERING | 2004年 / 87卷 / 06期

关键词：

immobilization; CLEA; CLEC; protein;

D O I：

10.1002/bit.20184

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The broad applicability of the cross-linking of enzyme aggregates to the effective immobilisation of enzymes is demonstrated and the influence of many parameters on the properties of the resulting CLEAs is determined, The relative simplicity of the operation ideally lends itself to high-throughput methodologies. The aggregation method was improved up to 100% activity yield for any enzyme. For the first time, the physical structures of CLEAs are elucidated. (C) 2004 Wiley Periodicals, Inc.

引用

页码：754 / 762

页数：9

共 24 条

[1] Cytosol-mimetic chemistry:: Kinetics of the trypsin-catalyzed hydrolysis of p-nitrophenyl acetate upon addition of polyethylene glycol and N-tert-butyl acetoacetamide [J].