Specific and nonspecific glucanases from Trichoderma viride

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Abstract
Six endoglucanases (Endo I, II, III, IV, V, and VI), three exoglucanases (Exo I, II, and III), and a β‐glucosidase (β‐gluc I) isolated from a commercial cellulase preparation of Trichoderma viride origin were examined as to their activities on xylan ex oat spelts. Endo I, II, and III as well as Exo II and III showed no activity toward xylan and were classified as specific glucanases. Less specificity was found for the endoglucanases Endo IV, V, and VI, Exo I, and β‐gluc I, whose enzymes were able to hydrolyze xylan. With respect to product formation these xylanolytic cellulases fit the classification of xylanases generally accepted in the literature. Kinetic experiment with xylan, CM‐cellulose, and p‐nitrophenyl‐β‐D‐glucoside revealed that Endo IV, V, an VI and Exo I prefer to hydrolyze β‐1, 4‐D‐glucosidic linkages. β‐Gluc I showed no clear substrate preference.