Purification and characterization of laminaran hydrolases from Trichoderma viride

At least three extracellular laminaran hydrolases which hydrolyzed laminaran (β-1,3:1,6-glucan) from Eisenia bicyclis were secreted in wheat bran solid medium by Trichoderma viride U-1. These three enzymes, lam AI, AII, and B, were purified to electrophoretic homogeneity. Their molecular masses were...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2003-06, Vol.67 (6), p.1349-1357
Main Authors: Nobe, R. (Miyazaki Univ. (Japan). Faculty of Agriculture), Sakakibara, Y, Fukuda, N, Yoshida, N, Ogawa, K, Suiko, M
Format: Article
Language:English
Subjects:
Biological and medical sciences
EISENIA BICYCLIS
ELECTROPHORESIS
extracellular enzyme
Fundamental and applied biological sciences. Psychology
Fungal Proteins - isolation & purification
Glucan 1,3-beta-Glucosidase - isolation & purification
Glucan 1,3-beta-Glucosidase - metabolism
Glucan Endo-1,3-beta-D-Glucosidase - isolation & purification
Glucan Endo-1,3-beta-D-Glucosidase - metabolism
GLUCANS
Glycoside Hydrolases - isolation & purification
Glycoside Hydrolases - metabolism
HYDROLASES
Laminaria digitata
MOLECULAR WEIGHT
Multienzyme Complexes
OLIGOSACCHARIDES
Polysaccharides - metabolism
PURIFICATION
Substrate Specificity
Trichoderma - enzymology
TRICHODERMA VIRIDE
β-1,3-glucanase
β-1,6-glucanase
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Description
Summary:At least three extracellular laminaran hydrolases which hydrolyzed laminaran (β-1,3:1,6-glucan) from Eisenia bicyclis were secreted in wheat bran solid medium by Trichoderma viride U-1. These three enzymes, lam AI, AII, and B, were purified to electrophoretic homogeneity. Their molecular masses were estimated to be 70.1, 70.4, and 45.0 kDa for lam AI, AII, and B, respectively, by SDS-PAGE. Whereas both lam AI and AII could hydrolyze laminarin from Laminaria digitata, lam AII showed higher activity against Laminaria laminarin rather than Eisenia laminaran. On the other hand, lam B preferentially hydrolyzed pustulan, a β-1,6-glucan. Laminarioligosaccharide was hydrolyzed by lam AI and AII but not B, whereas gentiooligosaccharide was hydrolyzed by only lam B. It showed that lam AI and AII were specific for β-1,3-linkages, but lam B was specific for β-1,6-linkages. These results indicated that T. viride U-1 has a multiple glucanolytic enzyme system.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.67.1349