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Carboxypeptidase a immobilization on activated styrene–maleic anhydride systems
Author(s) -
Dua R. D.,
Kumar Sanjay,
Vasudevan Padma
Publication year - 1985
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.260270517
Subject(s) - immobilized enzyme , enzyme , maleic anhydride , chemistry , carboxypeptidase , styrene , thermal stability , enzyme assay , copolymer , polymer chemistry , chromatography , organic chemistry , polymer
The copolymer styrene–maleic anhydride (SMA) was activated to various forms to create enzyme coupling groups. Carboxypeptidase A (CPA) was Immobilized on these supports to enhance their thermal and chemical stability. Immobilized enzyme retained 60–70% of the original activity. When kept at 60°C, while free enzyme was deactivated within 30 min, the immobilized enzyme retained 40% of initial activity at the end of 3 h. The half‐life of free enzyme was only 21 min, while for immobilized enzyme it was enhanced up to 3 h. Also, the immobilized enzyme could be repeatedly used over 50 times retaining almost 50% of original activity.
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