Nonporous magnetic materials as enzyme supports: Studies with immobilized chymotrypsin
- 1 January 1977
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 19 (1), 101-124
- https://doi.org/10.1002/bit.260190109
Abstract
Chymotrypsin has been immobilized to several nonporous magnetic materials. Nickel particles were considered to be most suitable as immobilized enzyme supports. Chymotrypsin immobilized to nonporous magnetic supports was not fouled significantly by6 either whole milk or clarified yeast homogenate. AE-cellulose-chymotrypsin was rapidly fouled by both these materials and chymotrypsin immobilized to acrylic-based ion exchangers was slowly fouled. Immobilized enzyme activity was found to be inverted proportional to particle diameter for nonporous rock magnetite particles. Immobilization by adsorption and then glutaraldehyde crosslinking was used to produce controlled amounts of chymotrypsin on the particles. Esterolytic activity increased with enzyme loading but caseinolytic activity did not increase. Chymotrypsin is inhibited by metal ions from the magnetic supports. It is partially protected by use of a preliminary protein coating and may be reactivated by incubation with EDTA or BSA.This publication has 15 references indexed in Scilit:
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