Cross-linked enzyme aggregates (CLEA®s): stable and recyclable biocatalysts

Author:

Sheldon R.A.1

Affiliation:

1. Department of Biotechnology, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands

Abstract

The key to obtaining an optimum performance of an enzyme is often a question of devising an effective method for its immobilization. In the present review, we describe a novel, versatile and effective methodology for enzyme immobilization as CLEAs (cross-linked enzyme aggregates). The method is exquisitely simple (involving precipitation of the enzyme from aqueous buffer followed by cross-linking of the resulting physical aggregates of enzyme molecules) and amenable to rapid optimization. We have shown it to be applicable to a wide variety of enzymes, including, in addition to a wide variety of hydrolases, lyases, e.g. nitrile hydratases and oxynitrilases, and oxidoreductases such as laccase and galactose oxidase. CLEAs are stable, recyclable catalysts exhibiting high catalyst productivities. Because the methodology is essentially a combination of purification and immobilization into one step, the enzyme does not need to be of high purity. The technique is also applicable to the preparation of combi-CLEAs, containing two or more enzymes, for use in one-pot, multistep syntheses, e.g. an oxynitrilase/nitrilase combi-CLEA for the one-pot conversion of benzaldehyde into (S)-mandelic acid, in high yield and enantiomeric purity.

Publisher

Portland Press Ltd.

Subject

Biochemistry

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3