Purification and some properties of a β-glucanase from a strain,Trichoderma reesei GXC |
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| Authors: | Sun Jian-yi Li Wei-fen Xu Zi-rong Gu Sai-hong |
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| Institution: | (1) Feed Science Institute of Animal Science College, Zhejiang University, 310029 Hangzhou, China |
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| 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. TheK
m of the enzyme on β-glucan was 10.86 mg/ml, and theV
max 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.
Project supported by Foundation for University Key Teacher of the State Ministry of Education, the National Natural Science
Foundation of China (No. 30000118) and Zhejiang Provincial Natural Science Foundation of China (No. 399409). |
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| Keywords: | Trichoderma reesei β -glucanase purification and characterization stability |
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