1887

Abstract

An extracellular endoglucanase (1,4--glucanohydrolase, EC 3.2.1.4) produced by 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 , of about 100000. The pH and temperature optima for its activity were 4·8 and 65°C respectively. The of the purified enzyme for CMC (sodium salt) was 3 mg ml. The enzyme displayed low activity toward salicin and -nitrophenyl --glucoside. The activity was enhanced in the presence of Na, K and Ca but effectively inhibited by Hg, Fe, Mg, Cu and NH . Inhibition studies indicated that the enzyme may be a metalloprotein and/or that it requires metal lons for its optimum activity.

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1990-10-01
2022-01-22
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