Immobilization of Oxydoreductases on Inorganic Supports Based on Alumina: The Role of Mutual Correspondence of Enzyme-Support Hydrophobic-Hydrophilic Characters Full article
Journal |
Biotechnology and Bioengineering
ISSN: 0006-3592 , E-ISSN: 1097-0290 |
||
---|---|---|---|
Output data | Year: 1988, Volume: 32, Number: 7, Pages: 916-919 Pages count : 4 DOI: 10.1002/bit.260320711 | ||
Tags | Biocatalysts--Activity | ||
Authors |
|
||
Affiliations |
|
Abstract:
Enzyme immobilization by adsorption on various matrices of organic or inorganic nature is certain to be the most cost-effective and technologically convenient way to obtain heterogeneous biocatalysts for commercial use. With excellent technological properties (mechanical strength, low hydrodynamic resistance, and regeneration properties), these matrices should be optimal carriers for the particular enzyme with respect to the high catalytic activity and stability of the biocatalysts obtained. At present, it is extremely difficult to select a support ideally suited for a particular enzyme. It is attractive to suggest some connection between enzyme and support characteristics, which determine the type of adsorption interaction (ionic and hydrophobic interactions), on the one hand, and the final properties of biocatalyst
obtained (catalytic activity and stability) on the other hand. In two previous reports [1,2] 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.
Cite:
Sokolovskii V.D.
, Kovalenko G.A.
Immobilization of Oxydoreductases on Inorganic Supports Based on Alumina: The Role of Mutual Correspondence of Enzyme-Support Hydrophobic-Hydrophilic Characters
Biotechnology and Bioengineering. 1988. V.32. N7. P.916-919. DOI: 10.1002/bit.260320711 WOS Scopus РИНЦ
Immobilization of Oxydoreductases on Inorganic Supports Based on Alumina: The Role of Mutual Correspondence of Enzyme-Support Hydrophobic-Hydrophilic Characters
Biotechnology and Bioengineering. 1988. V.32. N7. P.916-919. DOI: 10.1002/bit.260320711 WOS Scopus РИНЦ
Files:
Full text from publisher
Dates:
Submitted: | May 6, 1987 |
Accepted: | May 6, 1987 |
Published print: | Sep 20, 1988 |
Published online: | Feb 18, 2004 |
Identifiers:
Web of science | WOS:A1988P977800010 |
Scopus | 2-s2.0-0024080034 |
Elibrary | 23133254 |
Chemical Abstracts | 1988:625788 |
Chemical Abstracts (print) | 109:225788 |
OpenAlex | W2148541021 |