Document Detail


Purification and characterization of laminaran hydrolases from Trichoderma viride.
MedLine Citation:
PMID:  12843664     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
At least three extracellular laminaran hydrolases which hydrolyzed laminaran (beta-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 beta-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 beta-1,3-linkages, but lam B was specific for beta-1,6-linkages. These results indicated that T. viride U-1 has a multiple glucanolytic enzyme system.
Authors:
Rika Nobe; Yoichi Sakakibara; Nobuhiro Fukuda; Naoto Yoshida; Kihachiro Ogawa; Masahito Suiko
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  67     ISSN:  0916-8451     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2003 Jun 
Date Detail:
Created Date:  2003-07-04     Completed Date:  2004-04-16     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  1349-57     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, Miyazaki University, 1-1 Gakuen Kibanadai Nishi, Miyazaki 889-2192, Japan.
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MeSH Terms
Descriptor/Qualifier:
Fungal Proteins / isolation & purification
Glucan 1,3-beta-Glucosidase / isolation & purification,  metabolism
Glucan Endo-1,3-beta-D-Glucosidase / isolation & purification,  metabolism
Glycoside Hydrolases / isolation & purification*,  metabolism*
Molecular Weight
Multienzyme Complexes
Polysaccharides / metabolism*
Substrate Specificity
Trichoderma / enzymology*
Chemical
Reg. No./Substance:
0/Fungal Proteins; 0/Multienzyme Complexes; 0/Polysaccharides; 9008-22-4/laminaran; EC 3.2.1.-/Glycoside Hydrolases; EC 3.2.1.39/Glucan Endo-1,3-beta-D-Glucosidase; EC 3.2.1.58/Glucan 1,3-beta-Glucosidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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