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Chem. J. Chinese Universities ›› 2010, Vol. 31 ›› Issue (6): 1152.

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Purification and Characterization of New Special Saikosaponin-glycosidase

FU Yao-Yao1,2, AN Jia-Yan2, YU Hong-Shan2*, SONG Hai-Mei2, SU Xiao-Feng2, LU Ming-Chun2, ZHANG Chun-Zhi2, JIN Feng-Xie2*   

  1. 1. College of Science, Yanbian University, Yanji 133002, China;
    2. College of Bio. & Food Technology, Dalian Polytechnic University, Dalian 116034, China
  • Received:2009-09-02 Online:2010-06-10 Published:2010-06-10
  • Contact: JIN Feng-Xie. E-mail: fxjin@dlpu.edu.cn; YU Hong-Shan. E-mail: hongshan@dlpu.edu.cn
  • Supported by:

    国家自然科学基金(批准号: 30371744, 20476017)和辽宁省教育厅高等学校创新团队项目(批准号: 2007T006, 2008T008)资助.

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Abstract:

Radix bupleuri, a well-known traditional Chinese herb-drug, is often used to treat common cold with fever. One of the major physiologically active ingredients in radix bupleuri is saikosaponin which has the properties of anti-inflammation, anti-hypersusceptibility, anti-thrombus. The natural structures of saikosaponins are not suitable for physiological or pharmacological effects, the enzymatic transforming generally improves the bioactivity of natural productions. In this paper, a new special saikosaponin-glycosidase hydrolyzing 3-O-β-(1→3)-glucoside and 3-O-β-fucoside of saikosaponin A or B2 was isolated from Aspergillus oryzae c42 strain, purified and characterized. The methods of centrifugation, ammonium sulfate precipitation, ion-exchange chromatography on DEAE-cellulose column and vertical slab polyacrylamide gel electrophoresis(PAGE) were used to purify the enzyme, and its partial characteristics were studied. The molecular weight of saikosaponin-glycosidase was about 58000 by SDS-PAGE. The enzyme hydrolyzed 3-O-β-(1→3)-glucoside of saikosaponin A or B2 into 3-O-β-fucoside-saikosapogenin A or B2, and further hydrolyzed 3-O-β-fucoside of 3-O-β-fucoside-saikosapogenin A or B2 into their aglycone(saikosapogenin A or B2) exhibiting significant differences from all previously reported glycosidases. The optimum temperature of the saikosaponin-glycosidase was 40 ℃; the optimum pH was 5.0. The activity of this enzyme was not apparently affected by Na+ and K+ ions, but it was significantly inhibited by Cu2+, Hg2+ and Ag+ ions; and slightly affected by Ca2+ and Mg2+ ions. Further study on saikosaponin-glycosidase will bring new insight to the understanding of glycosidases.

Key words: Saikosaponin-glycosidase; Aspergillus oryzae c42 strain; Saikosaponin A; Saikosaponin B2

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