Immobilization of oxydoreductases on inorganic supports based on alumina: The role of mutual correspondence of enzyme-support hydrophobic-hydrophilic characters

In two previous reports, the immobilization by adsorption of lactate dehydrogenase and alcohol dehydrogenase on modified and unmodified alumina with different pore structure had been studied. A similar investigation of tyrosinase and glucose oxidase immobilized by adsorption on alumina is continued...

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Bibliographic Details
Published in:Biotechnology and bioengineering 1988-09, Vol.32 (7), p.916-919
Main Authors: Sokolovskii, V. D., Kovalenko, G. A.
Format: Article
Language:English
Subjects:
aluminum oxide
Biological and medical sciences
Biotechnology
Enzyme engineering
Fundamental and applied biological sciences. Psychology
glucose oxidase
Immobilization of enzymes and other molecules
Immobilization techniques
immobilized enzymes
Methods. Procedures. Technologies
monophenol monooxygenase
supports
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Summary:In two previous reports, the immobilization by adsorption of lactate dehydrogenase and alcohol dehydrogenase on modified and unmodified alumina with different pore structure had been studied. A similar investigation of tyrosinase and glucose oxidase immobilized by adsorption on alumina is continued in this report. An attempt to clarify the factors which define immobilized enzyme activity and stability has been made on the basis of corresponding enzyme-support characteristic matching.
ISSN:0006-3592
1097-0290
DOI:10.1002/bit.260320711