Immobilization Of Fructosyltransferase And Catalase

This paper studied immobilization of the fructosyltransferase and catalase, and then studied the properties of the immobilized enzyme respectively.Fructosyltransferase was immobilized on eighteen kinds of ion-exchange and adsorption resins, among them D380 showed the excellent result for immobilization. Then the enzyme was immobilized through cross-linkage of glutaraldehyde. The optimum conditions for the immobilization were as follows: 200U of enzyme per g wet resin, pH 6.0, 30℃, and 6 hours, respectively. The crosslinking temperature and time were 4℃and 6 h respectively, and the concentration of the crosslinking agent (glutaraldehyde) was 0.01%. The activity yield of immobilized enzyme was above 87.6%.The optimum temperature and pH of the immobilized fructosyltransferase were 50～55℃and 6.0,respectively, whereas for free enzyme,were 45～50℃and 5.0. Thermal and pH stability were both improved by immobilization comparing with the free enzyme.The Km value was 0.60M(for sucrose),which was higher than that(0.29 M)of the free enzyme.This indicated that the affinity between enzyme and substrate decreased significantly.A kind of carrier-free technology was used in the immobilization of catalase, the enzyme was aggregated first then cross-linked by glutaraldehyde. The optimum conditions for the immobilization were as follows: the concentration of the crosslinking agent (glutaraldehyde) was 1%, and the crosslinking temperature and time were 4℃and 4h respectively.The optimum temperature of free and immobilized catalase were 40℃and 35℃,respectively, optimum pH and pH stability had no significant change, the thermal stability was better than that of free catlase.High-purity of fructooligosaccharides was prepared after glucose was removed in normal products by glucose oxidase(GOD) and catalase(CAT). So the study of the immobilization of Fructooligosaccharides and Catalase will make a foundation for the production.