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Bio-Design and Manufacturing  2020 Vol.3 No.1 P.106~112

10.1631/jzus.2002.0106


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


Author(s):  SUN Jian-yi, LI Wei-fen, XU Zi-rong, GU Sai-hong

Affiliation(s):  Feed Science Institute of Animal Science College, Zhejiang University, Hangzhou 310029, China

Corresponding email(s):   jyisun@mail.hz.zj.cn

Key Words:  Trichoderma reesei, &beta, -glucanase, purification and characterization, stability


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SUN Jian-yi, LI Wei-fen, XU Zi-rong, GU Sai-hong. Purification and some properties of a β-glucanase from a strain, Trichoderma reesei GXC[J]. Journal of Zhejiang University Science D, 2020, 3(1): 106~112.

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author="SUN Jian-yi, LI Wei-fen, XU Zi-rong, GU Sai-hong",
journal="Journal of Zhejiang University Science D",
volume="3",
number="1",
pages="106~112",
year="2020",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.2002.0106"
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%T Purification and some properties of a β-glucanase from a strain, Trichoderma reesei GXC
%A SUN Jian-yi
%A LI Wei-fen
%A XU Zi-rong
%A GU Sai-hong
%J Journal of Zhejiang University SCIENCE D
%V 3
%N 1
%P 106~112
%@ 1869-1951
%D 2020
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.2002.0106

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T1 - Purification and some properties of a β-glucanase from a strain, Trichoderma reesei GXC
A1 - SUN Jian-yi
A1 - LI Wei-fen
A1 - XU Zi-rong
A1 - GU Sai-hong
J0 - Journal of Zhejiang University Science D
VL - 3
IS - 1
SP - 106
EP - 112
%@ 1869-1951
Y1 - 2020
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.2002.0106


Abstract: 
&beta;-glucanase was purified from a solid-state culture of Trichoderma 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 &beta;-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 &beta;-glucanase was relatively stable at below 40 °C for 60 min. The Km of the enzyme on &beta;-glucan was 10.86 mg/ml, and the Vmax on &beta;-glucan was 14286 μmol of glucose equivalents per mg of the pure enzyme per min. The &beta;-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 &beta;-glucanase activity was stimulated by Co2+ ions, Ca2+ ions, Zn2+ ions, and Fe2+ ions at 1 mmol/L and 5 mmol/L, respectively.

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