Details

Autor(en) / Beteiligte

• Villalonga, Reynaldo
• Fernández, Michael
• Fragoso, Alex
• Cao, Roberto
• Di Pierro, Prospero
• Mariniello, Loredana
• Porta, Raffaele

Titel

Transglutaminase-catalyzed synthesis of trypsin-cyclodextrin conjugates: Kinetics and stability properties

Ist Teil von

• Biotechnology and bioengineering, 2003-03, Vol.81 (6), p.732-737

Ort / Verlag

New York: Wiley Subscription Services, Inc., A Wiley Company

Erscheinungsjahr

2003

Quelle

Wiley Online Library Journals Frontfile Complete

Beschreibungen/Notizen

• Bovine pancreatic trypsin was modified by the mono‐6‐amino‐6‐deoxy derivatives of α‐, β‐, and γ‐cyclodextrin through a transglutaminase‐catalyzed reaction. The trypsin–cyclodextrin conjugates, containing about 3 mol of oligosaccharide per mole of protein, were tested for their catalytic and stability properties. The specific esterolytic activity and the kinetics constants of trypsin were significantly improved following the transglutaminase‐induced structural modifications. Trypsin–cyclodextrin conjugates were also found markedly (sixfold) more resistant to autolytic degradation at alkaline pH, and their thermal stability profile was improved by about 16°C. Moreover, they were particularly resistant to heat inactivation when treated at different temperatures ranging from 45°C to 70°C for different periods of time. © 2003 Wiley Periodicals, Inc. Biotechnol Bioeng 81: 732–737, 2003.