Properties of endo-β-1,3-glucanase from Schizophyllum commune Fr.

The endo-β-1,3-glucanase from schizophyllum commune Fr.was separated and purified effectively,the purity was identified by electrophoresis and then the enzymological properties were discussed.It showed that after purified by DEAE-Sephadex A-50 ion exchange chromatography and Sephadex G-75 gel filtration,pure endo-β-1,3-glucanase with molecular weight of 45KD could be obtained,and its optimum temperature and pH were 45 ℃ and 5.0 respectively;Zn2+,K+,Ag+,Hg2+ and Ca2+ had an inhibitory effect on the enzyme activity while Cu2+,Fe2+ and Ba2+ stimulated the activity;Michaelis constant(Km) of the enzyme was 0.8813 mg/mL.Its secondary structure analyzed by circular dichroism showed that the percentage of α-helix,β-sheet,turn and random coil were 4.6%,49.1%,8.7% and 37.5% respectively,which represented the typical structure of β-glucanase.