Inhibitory effect of some fungicides on cellulase production by Alternaria spp.
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Cellobiose may exert different effects on the activities of various endoglucanases. The endoglucanases of T. reesei and Rapidase are noticeably suppressed by cellobiose at concentrations above 3 mM. On the other hand, a low molecular weight endoglucanase from T. koningii is activated by cellobiose, whereas high molecular weight endoglucanases from the same source are inhibited by cellobiose. A detailed kinetic analysis of the effects showed that the low molecular weight endoglucanase is activated by a transglycosylation mechanism, in which cellobiose acts as an additional nucleophile. At saturating concentrations of cellobiose (Ks = 15 mM) the enzyme activity is increased 6-fold. Such a specific mechanism of activation manifests itself in an acceleration of random cleavage of CM-cellulose by the low molecular weight endoglucanase, which can be recorded by a viscosimetric technique. However, its action does not accelerate the production of soluble reducing sugars.
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The extracellular endo-beta-1.4-glucanase activity of Bacteroides succinogenes S85, grown on filter paper, was poorly stimulated by cysteine, slightly inhibited by cellobiose, but strongly inhibited by ethylthiomercuribenzoate. Active fractions against hydroxy-ethylcellulose and milled filter paper were eluted from a polyacrylamide gel filtration column with an apparent molecular weight of 60,000 daltons.
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A mesophilic anaerobe, Acetivibrio cellulolyticus, isolated from a cellulose-enrichment culture, degraded cellulose by the secretion of cellulolytic enzymes into the culture medium. Both exo- and endoglucanase activities were detected and shown to be regulated by induction and catabolite repression. Endoglucanase synthesis was induced by cellulose, cellobiose and salicin. Synthesis induced during growth on cellobiose was inhibited, although not completely repressed by glucose. Exoglucanase activity was enhanced when cells were grown on insoluble or soluble poly beta-glucoside polymers. Activity was progressively inhibited by supplementing microcrystalline substrates with increasing amounts of cellobiose.
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