Functional stabilization of trypsin by conjugation with beta-cyclodextrin-modified carboxymethylcellulose.
Prep Biochem Biotechnol
; 33(1): 53-66, 2003 Feb.
Article
en En
| MEDLINE
| ID: mdl-12693815
Bovine pancreatic trypsin was chemically modified by a beta-cyclodextrin-carboxymethylcellulose polymer using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as coupling agent. The conjugate retained 110% and 95% of the initial esterolytic and proteolytic activity, respectively, and contained about 2 mol of polymer per mol of trypsin. The optimum temperature for trypsin was increased to 8 degrees C after conjugation. The thermostability of the enzyme was increased to about 16 degrees C after modification. The conjugate prepared was also more stable against thermal incubation at different temperatures ranging from 45 degrees C to 60 degrees C. In comparison with native trypsin, the polymer-enzyme complex was more resistant to autolytic degradation at pH 9.0, retaining about 65% of the initial activity after 3h incubation. In addition, modification protected trypsin against denaturation in the presence of sodium dodecylsulfate.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Carboximetilcelulosa de Sodio
/
Tripsina
/
Ciclodextrinas
/
Beta-Ciclodextrinas
Tipo de estudio:
Evaluation_studies
Idioma:
En
Revista:
Prep Biochem Biotechnol
Asunto de la revista:
BIOQUIMICA
/
BIOTECNOLOGIA
Año:
2003
Tipo del documento:
Article
País de afiliación:
Cuba
Pais de publicación:
Reino Unido