1887

Abstract

Multiple forms of -glucosidase (EC 3.2.1.21) of were produced when the fungus was grown in a cellulose medium. One -glucosidase was purified 16fold from 6-d-old culture filtrates by ion-exchange and gel-filtration chromatography. The purified enzyme was free of cellulase activity. It hydrolysed aryl --glucosides and --linked diglucosides. It was optimally active at pH 5·4, at 65 °C. The apparent values for -nitrophenyl --glucoside (PNPG) and cellobiose were 0·29 and 0·83 m, respectively. Glucose, fucose, nojirimycin and gluconolactone inhibited -glucosidase competitively. At high (> 1 m) substrate concentration, -glucosidase catalysed a parallel transglycosylation reaction. The transglycosylation product formed from cellobiose appeared to be a -linked tetramer of glucose. Admixtures of -glucosidase and cellulase components showed that the concept of cellobiose inhibition of cellulases was not valid for all components of the cellulase system of . -Glucosidase supplementation also stimulated cellulose hydrolysis by cellulases when there was no accumulation of cellobiose in reaction mixture.

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1993-11-01
2021-07-28
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