Separation, Purification and Enzymatic Properties of β-Glucosidase from Tridchoderma viride

doi:10.7506/spkx1002-6630-201405030

Abstract

Abstract:

An extracellular β-glucosidase produced by Trichoderma viride AS3.3711 was separated and purifiedby ammonium acetate precipitation, dialysis and Sephadex G-150 column chromatography. The results of enzymecharacterization showed that the protein concentration of the purified enzyme solution was 8.12 mg/mL, and the β-glucosidaseactivity was 4.08 U/mL, with a purification factor of 18.48. Its molecular weight was 66.0 kD. The β-glucosidase fromTrichoderma viride displayed a strong stability under acidic conditions and its optimum pH value was 5.0. In the range of60–70 ℃, it could still maintain a high enzyme activity for a long time with an optimum reaction temperature of 60 ℃.Some metal ions including Ca2+, Mg2+ and K+ improved its activity with Ca2+ having the strongest effect. However, Zn2+ andFe3+ inhibited the enzyme. Heavy metal ions such as Ag+, Cu2+ and Hg2+ almost totally inactivated its activity.

Key words: Tridchoderma viride, β-glucosidase, separation and purification, enzymatic properties

LIU Ying, HAN Chun-ran, ZHANG Shuai, ZHANG Wei-wei, DOU Bo-xin. Separation, Purification and Enzymatic Properties of β-Glucosidase from Tridchoderma viride[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201405030.

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Separation, Purification and Enzymatic Properties of β-Glucosidase from Tridchoderma viride

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