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Journal of Zhejiang University-SCIENCE A

, Volume 3, Issue 1, pp 106–112 | Cite as

Purification and some properties of a β-glucanase from a strain,Trichoderma reesei GXC

  • Sun Jian-yi
  • Li Wei-fen
  • Xu Zi-rong
  • Gu Sai-hong
Life Sciences & Bioengineering
  • 45 Downloads

Abstract

β-glucanase was purified from a solid-state culture ofTrichoderma reesei on wheat bran in three steps which comprised ammonium sulfate precipitation, Sephadex G-100 chromatography, and DEAE-Sephadex A-50 chromatography. The molecular mass was determined to be 35.21 kilodaltons by sodium dodecyl sulfate-12.5% polyacrylamide gel electrophoresis. The β-glucanase at low pHs was more stable than that at high pHs, and optimum pH was 5.0. The optimum temperature was 60°C, and β-glucanase was relatively stable at below 40°C for 60 min. TheKm of the enzyme on β-glucan was 10.86 mg/ml, and theVmax on β-glucan was 14286 μmol of glucose equivalents per mg of the pure enzyme per min. The β-glucanase activity was significantly inhibited by Fe3+ ions, and was reduced in the presence of Cu2+ ions, Mn2+ ions and Mg2+ ions at 5 mmol/L and 10 mmol/L, respectively. The β-glucanase activity was stimulated by Co2+ ions, Ca2+ ions, Zn2+ ions, and Fe2+ ions at 1 mmol/L and 5 mmol/L, respectively.

Key words

Trichoderma reesei β-glucanase purification and characterization stability 

Document code

CLC number

Q814.1 

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Copyright information

© Zhejiang University Press 2002

Authors and Affiliations

  • Sun Jian-yi
    • 1
  • Li Wei-fen
    • 1
  • Xu Zi-rong
    • 1
  • Gu Sai-hong
    • 1
  1. 1.Feed Science Institute of Animal Science CollegeZhejiang UniversityHangzhouChina

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