FOOD SCIENCE ›› 2009, Vol. 30 ›› Issue (5): 179-183.doi: 10.7506/spkx1002-6630-200905041

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Characteristics and Enzyme System of Inulinase from Penicillium sp.B01

WEI Wei 1,LIU Zhao-pu1,*,WANG Lin2,LONG Xiao-hua1   

  1. (1.Key Laboratory of Marine Biology, Jiangsu Province, College of Resources and Environmental Sciences, Nanjing Agricultural
    University, Nanjing 210095, China;2.Huai’an Institute of Supervision and Inspection on Product Quality, Huai’an 223001,
    China)
  • Received:2008-03-25 Revised:2008-07-09 Online:2009-03-01 Published:2010-12-29
  • Contact: LIU Zhao-pu1,*, E-mail:sea@njau.edu.cn

Abstract:

With inluin as the reaction substrate, the effects of pH value, temperature, substrate concentration, metal ion and reaction time on the activity of inulinase from Penicillium sp.B01 were investigated. The results showed that the maximal inulinase activity may be observed at 55 ℃ and pH 4.6; under the conditions of pH 4.6 to 5.4 and below 60 ℃, the inulinase activity is stable; Ca2+ promotes the inulinase activity, but Cu2+ significantly inhibits it. Moreover, the crude inulinase of Penicillium sp.B01 was separated by native-polyacrylamide gel electrophoresis (native-PAGE), and six distinct protein bands were obtained. Then the seperated inulinase was tested with inulin and triphenyl tetrazolium chloride (TTC) was used for activity staining. But only three bands were found to have inulinase activity. The analysis of reaction product by TLC and HPLC further proved that these three bands have the exoinulinase activity, and confirmed that the main composition of reaction product is fructose.

Key words: inulinase, enzymatic property, native-PAGE, TLC, HPLC

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