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Abstract: β-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 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. The Km of the enzyme on β-glucan was 10.86 mg/ml, and the V_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.

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