FOOD SCIENCE ›› 2009, Vol. 30 ›› Issue (23): 237-241.doi: 10.7506/spkx1002-6300-200923053

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Intrinsic Fluorescence of Aspergillus ficuum Inulinases

WANG Jing1，JIN Zheng-yu2，JIANG Bo2，SUN Bao-guo1，CAO Yan-ping1，YU Hao-yang1   

  1. 1. College of Chemistry and Environmental Engineering, Beijing Technology and Business University, Beijing 100037, China；
    2. School of Food Science and Technology, Jiangnan University, Wuxi 214122, China
  • Received:2009-01-04 Revised:2009-03-30 Online:2009-12-01 Published:2010-12-29
  • Contact: WANG Jing E-mail:jwang810@yahoo.com.cn

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Abstract:

The intrinsic fluorescence of endo- and exo-inulinase from Aspergillus ficuum was studied by using Trp as the probe. The result indicated that the Trp of endo-inulinase was located in a more polar environment than exo-inulinase. The fluorescence intensity of endo-inulinase was changed more than exo-inulinase by NBS, which suggested that the Trp of endo-inulinase was more sensitive to the change of environment than that of exo-inulinase. The quenching of the Trp fluorescence of inulinase by acrylamide showed that the Trp of endo-inulinase was more accessible than that of exo-inulinase, which displayed the greater exposure of Trp in endo-inulinase than exo-inulinase. With pH value of the environment reducing from 8.0 to 3.5, the fluorescence intensity of endo-inulinase were quenched higher than that of exo-inulinase. The data suggested that the microenvironments of Trp residue in endo-inulinase was more sensitive to the change of pH value than that in exo-inulinase.

Key words: Aspergillus ficuum, inulinase, fluorescence

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