Mar 14, 1978

Enzymic activities of endo-1,4-beta-D-glucanases purified from Trichoderma viride

Biochimica Et Biophysica Acta
S P Shoemaker, R D Brown

Abstract

Endoglucanases II, III and IV (EC 3.2.1.4) from Trichoderma viride are highly active in degrading CM-cellulose or phosphoric acid swollen cellulose, and only slightly active on Avicel. The specific activities of the endoglucanases increase with the length of the cellooligosaccharide substrates. By rate and product analyses using high pressure liquid chromatography the mode of action of Endoglucanase III was differentiated from that of Endoglucanases II and IV. Endoglucanase III has a low affinity for cellobiose, reacts rapidly with cellotriose, and gradually increases in reactivity with cellooligosaccharides as degree of polymerization increases from four to six. In addition to cleaving internal glycosidic bonds of polymeric substrates, it preferentially cleaves cellobiosyl units from the non-reducing end of oligosaccharides. The cellobiosyl units are often, under initial reaction conditions, transferred to the substrate-acceptor. Endoglucanases II and IV show a preference for internal glycosidic bonds of cellooligosaccharides. The soluble products from the initial action of Endoglucanases II and IV on swollen cellulose are glucose, cellobiose, and cellotriose, which are slowly converted to glucose and some cellobiose.

  • References5
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Citations

Mentioned in this Paper

Trichoderma viride antigen
Avicel
Cellobiose
Phosphoricum acidum, phosphoric acid, Homeopathic preparation
Cell Differentiation Process
Soluble
Substrate Specificity
Polymers
Hydrolase
High Pressure Liquid Chromatography Procedure

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