An extracellular endoglucanase (1,4-~-glucanohydrolas, EC 3.2.1.4) produced by Myceliophthora thermphila D-14 (ATCC 48104) has been purified to homogeneity by ammonium sulphate precipitation and two consecutive ion-exchange chromatographic steps on DEAE-Sephadex A-50 columns. The enzyme was purified 13.8-fold and was homogeneous by analytical PAGE and SDS-PAGE. It has a high apparent Mr, of about 100OOO. The pH and temperature optima for its activity were 4.8 and 65 "C respectively. The Km of the purified enzyme for CMC (sodium salt) was 3 mg ml-l. The enzyme displayed low activity toward salicin and p-nitrophenyl P-D-glucoside.The activity was enhanced in the presence of Na+, K+ and Ca2+ but effectively inhibited by Hg2+, Fe2+, Mg2+, Cu2+ and NHZ. Inhibition studies indicated that the enzyme may be a metalloprotein and/or that it requires metal ions for its optimum activity.
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