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Operational stability of copolymerized enzymes at elevated temperatures
Author(s) -
Mozhaev V. V.,
Šikšnis V. A.,
Torchilin V. P.,
Martinek Karel
Publication year - 1983
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/bit.260250804
Subject(s) - polyacrylamide , covalent bond , enzyme , trypsin , chemistry , immobilized enzyme , chymotrypsin , polyacrylamide gel electrophoresis , copolymer , chromatography , biochemistry , polymer chemistry , organic chemistry , polymer
The copolymerization method of immobilization was used to obtain preparations of enzymes covalently incorporated in polyacrylamide gel. They possess properties making them suitable for practical use. First, the preparations are hundreds of times more stable against irreversible thermoinactivation than native enzymes. Second, on immobilization, the reversible conformational changes which also lower enzyme activity at elevated temperatures are completely suppressed. As a result, the temperatures of maximum activity for trypsin and α‐chymotrypsin covalently entrapped in polyacrylamide gel are 75 and 70°C, respectively—25 and 30°C higher than the corresponding values for the native enzymes. Therefore, the copolymerized enzyme preparations have a high operational stability at elevated temperatures.