Apr 16, 2003

Functional stabilization of trypsin by conjugation with beta-cyclodextrin-modified carboxymethylcellulose

Preparative Biochemistry & Biotechnology
Maria L VillalongaReynaldo Villalonga


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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Mentioned in this Paper

Carbohydrate nutrients
Covalent Interaction
Surfactant [EPC]
Endogenous Surfactants
Enzymes, antithrombotic
Peptide Hydrolases

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