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Effects of β‐cyclodextrin–dextran polymer on stability properties of trypsin
Author(s) -
Fernández Michael,
Villalonga Maria L.,
Caballero Julio,
Fragoso Alex,
Cao Roberto,
Villalonga Reynaldo
Publication year - 2003
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.10707
Subject(s) - thermostability , trypsin , dextran , chemistry , cyclodextrin , enzyme , polymer , incubation , immobilized enzyme , chromatography , biochemistry , organic chemistry
Dextran modified with the mono‐6‐pentylene‐diamino‐6‐deoxy‐β‐cyclodextrin derivative was evaluated as a thermoprotectant additive for trypsin. The optimum temperature for trypsin activity was increased by 7°C in the presence of this polymer. The enzyme thermostability was increased from 48.5 to 64°C over 10 min of incubation, and the activation free energy of thermoinactivation at 50°C was increased by 4.1 kJ/mol in the presence of the additive. Trypsin was 6‐fold more resistant to autolytic inactivation at alkaline pH in the presence of the polymer. © 2003 Wiley Periodicals, Inc. Biotechnol Bioeng 83: 743–747, 2003.