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Highly efficient immobilization of glycosylated enzymes into polyurethane foams
Author(s) -
Bakker Martin,
van de Velde Fred,
van Rantwijk Fred,
Sheldon Roger A.
Publication year - 2000
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/1097-0290(20001105)70:3<342::aid-bit11>3.0.co;2-a
Subject(s) - polyurethane , chemistry , enzyme , immobilized enzyme , biocatalysis , covalent bond , leaching (pedology) , aspergillus , chromatography , biochemistry , organic chemistry , catalysis , microbiology and biotechnology , biology , ecology , ionic liquid , soil water
Glycosylated enzymes, including aminoacylase from Aspergillus melleus, chloroperoxidase from Caldariomyces fumago, and phytase from Aspergillus ficuum, were covalently immobilized into polyurethane foams with very high enzyme loadings of up to 0.2 g protein per gram dry foam. The immobilization efficiency (retained activity) ranged from 100% at a low loading to 60% at high loadings. In contrast to many other immobilization methods no leaching of the enzyme from the support took place under the reaction conditions. In short, a universal method for the immobilization of enzymes from fungal sources was developed, affording a highly active, stable, and reusable biocatalyst. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 70: 342–348, 2000.