FOOD SCIENCE ›› 1993, Vol. 14 ›› Issue (3): 3-7.

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Immobilization of Trypsin on the Anion Exchange Resin

 BAI  Hong,   Ge-Shi-Jun   

  • Online:1993-03-15 Published:2011-12-29

Abstract:  The immobilizatin of trypsin, the kinetics and stability of the immobilized enzyme were studied. After removing the impurity, the anion exchange resin GM 201 was firstly treated with glutaraldehyde, then reacted with trypsin, and the trypsin was immobilized on the matrix. The Km value, obtained by kinetical study, of the immobilized trypsin was higher than that of trypsin, and the optimum pH value and the optimum temperature of the immobiliized enzyme were also changed. The heat stability of the immobilized enzyme is slightly decreased, but the storage stability of the immobilized enzyme in solutions from slightly acidic to basic were higher than that of soluble enzyme. Operational stability test showed that the immobilized trypsin was stable for casein hydrolysis and affinity chromatography of soybean trysin inhibitors.

Key words: Trypsin Immobilized trypsin Protein hydrolysis