β-葡聚糖酶的分离纯化和特性研究*

对里氏木霉所产β-葡聚糖酶粗酶液通过饱和硫酸铵沉淀、Sephadex G-100 柱层析和DEAE-Sephadex A-50 柱层析进行纯化，比活提高14.60倍,活力回收6.62%。酶特性研究表明，最适温度和pH分别为60℃和5.0，在pH低于5.0时酶较稳定,酶的热稳定性在60℃以下。 Cu～2+、 Mn～2+ 、Mg～2+ 、Fe～3+ 和K+对酶有抑制作用, Zn～2+、Ca～2+、 Co2+和 Fe～2+ 有激活作用。

PURIFICATION AND PROPERTIES OF β-GLUCANASE PRODUCED FROM STRAIN GXC OF TRICHODERMA REESEI

The β-glucanase from strain GXC of Trichoderma reesei was purified in three steps which comprised ammonium sulfate precipitation, Sephadex G-100 chromatography, and DEAE-Sephadex A-50 chromatography. The purified enzyme showed an activity increase of 14.60 fold, and an activity recovery of 6.62%. The optimal temperature and pH of the enzyme were 60℃ and 5.0，respectively . The β-glucanase was more stable at low pH than at high pH, and was relatively stable below 60℃ . Cu～2+, Mn～2+, Mg～2+, Fe～3+ and K+ had inhibitory effect on the enzyme activity; Zn～2+, Ca～2+, Co～2+ and Fe～2+ could stimulate the activity.