Immobilization of Chloroperoxidase on Aminopropyl-Glass

Author:

Kadima Tenshuk A.1,Pickard Michael A.1

Affiliation:

1. Department of Microbiology, M 330 Biological Sciences Building, University of Alberta, Edmonton, Alberta, Canada T6G 2E9

Abstract

Chloroperoxidase (CPO) purified from Caldariomyces fumago CMI 89362 was covalently bound to aminopropyl-glass by using a modification of an established method. Acid-washed glass was derivatized by using aminopropyltriethoxysilane, and the enzyme was ionically bound at low ionic strength. Further treatment with glutaraldehyde covalently linked the enzyme to the glass beads in an active form. No elution of bound activity from glass beads could be detected with a variety of washings. The loading of enzyme protein to the glass beads was highest, 100 mg of CPO per g of glass, at high reaction ratios of CPO to glass, but the specific activity of the immobilized enzyme was highest, 36% of theoretical, at low enzyme-to-carrier ratios. No differences in the properties of the soluble and immobilized enzymes could be detected by a number of criteria: their pH-activity and pH-stability profiles were similar, as were their thermal stabilities. After five uses, the immobilized enzyme retained full activity between pH 6.0 and 6.7.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Reference32 articles.

1. Bernath F. R. and K. Venkatasubramanian. 1986. Methods of enzyme immobilization p. 230-247. In A. L. Demain and N. A. Solomon (ed.) Manual of industrial microbiology and biotechnology. American Society for Microbiology Washington D.C.

2. Development of semi-continous and continous flow bioreactors for the high level production of chloroperoxidase;Blanke S. R.;Biotechnol. Lett.,1989

3. Characterization of sand as a support for immobilized enzymes;Brotherton J. E.;Biotechnol. Bioeng.,1976

4. Oxidation of phenols by chloroperoxidase;Carmichael R. D.;Biotechnol. Lett.,1985

5. Semicontinous and continous production of chloroperoxidase by Caldariomyces fumago immobilized in k-carrageenan;Carmichael R. D.;Appl. Environ. Microbiol.,1986

Cited by 56 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

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