FOOD SCIENCE ›› 2009, Vol. 30 ›› Issue (1): 169-172.doi: 10.7506/spkx1002-6630-200901040

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Study on Immobilization ofα-Amylase with 3-Aminopropyl Silica Gel as Carrier

LIU Hai-yan1,2，LI Ning1,3，LI Jing-ci1，WU Qiu-hua1，DUAN Hui-yun2，YANG Xiu-min1   

  1. (1.College of Science, Agricultural University of Hebei, Baoding 071001, China；
    2.College of Chemistry and Environmental Science, Hebei University, Baoding 071002, China；
    3.College of Food Science and Technology, Agricultural University of Hebei, Baoding 071001, China)
  • Received:2007-12-07 Revised:2008-05-20 Online:2009-01-01 Published:2010-12-29
  • Contact: LIU Hai-yan1 E-mail:LHYBD@126.COM

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Abstract:

α-Amylase was immobilized on five 3-aminopropyl silica gels with glutaraldehyde as crosslinking agent. Some factors that affect the activity of immobilized α-amylase were investigated, such as the mesh of silica gel, concentration of glutaraldehyde, reaction temperature and pH. The properties of imm obilized and free α-amylases were also compared. The results indicated that the optimum temperature of the immobilized enzyme is 75℃, which is 10℃ higher than that of the free α-amylase, and its thermal stability is better than that of free enzyme. Compared with free α-amylase, the immobilized α-amylase is also markedly improved in acid and alkaline stability, storage stability and operation stability. Furthermore, the Michealis constant (Km) of immobilized α-amylase is 2.13 mg/ml, while that of free α-amylase is 1.02 mg/ml.

Key words: α-amylase, immobilized enzyme, 3-aminopropyl silica gel

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