PURIFICATION AND PROPERTIES OF β-GLUCANASE PRODUCED FROM STRAIN GXC OF TRICHODERMA REESEI
Sun Jiang
Abstract
Sun Jiang
Abstract
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.
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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.
Key concepts: Trichoderma reesei, Ammonium sulfate precipitation, Sephadex, Glucanase, Chemistry, Ammonium sulfate, Enzyme, Enzyme assay