Purification and properties of beta-glucanase produced from strain GXC of Trichoderma reesei

The beta-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 60deg C and 5.0, respectively. The beta-glucanase was more stable at low pH than at high pH, and was relatively stable below 60deg C. 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.