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Stabilization of α ‐chymotrypsin by modification with β ‐cyclodextrin derivatives
Author(s) -
Fernández Michael,
Villalonga María de Lourdes,
Fragoso Alex,
Cao Roberto,
Villalonga Reynaldo
Publication year - 2002
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba20020056
Subject(s) - thermostability , chymotrypsin , chemistry , cyclodextrin , enzyme , chemical modification , oligosaccharide , stereochemistry , trypsin , biochemistry
Bovine pancreatic α ‐chymotrypsin was chemically modified with two different β ‐cyclodextrin derivatives, named mono‐6‐formyl‐ β ‐cyclodextrin and mono‐6‐succinyl‐6‐deoxy‐ β ‐cyclodextrin. The modified enzymes contained approx. 3–5 mol of oligosaccharide/mol of protein, and retained full proteolytic and esterolytic activity. The optimum temperature for α ‐chymotrypsin was increased by 8 °C and its thermostability was enhanced by about 4–6 °C after modification. The conjugated enzymes were also more resistant to thermal inactivation at temperatures ranging from 45 to 55 °C. Additionally, the modified enzymes were 7‐fold more stable against incubation at pH 9.0. The possible influence of supramolecular interactions on the thermal stabilization of modified α ‐chymotrypsins was also studied.