Document Detail

Synergistic action of two different types of endo-cellulase components from Irpex lacteus (Polyporus tulipiferae) in the hydrolysis of some insoluble celluloses.
MedLine Citation:
PMID:  956146     Owner:  NLM     Status:  MEDLINE    
The substrate specificities of three endo-cellulase [EC] components, F-1, F-2, and S-1, obtained from the culture filtrate of Irpex lacteus (Polyporus tulipiferae), were investigated in detail. It was confirmed that the former is of a more random type, belonging to the carboxymethyl-cellulase (CMCcase) group, and the latter two are of a less random type, beloning to the Avicelase group. It was found that a mixture of CMCase and Avicelase shows a remarkable synergistic action in the degradation of cotton and Avicel and that CMCase lowers the degree of polymerization of both cotton and CM-cellulose faster than Avicelases, relative to the production of reducing sugar. Thus, it was assumed that cotton and similar cellulosic substrates were degraded mainly by the synergistic action of these cellulase components produced by this celluloytic fungus.
T Kanda; K Wakabayashi; K Nisizawa
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of biochemistry     Volume:  79     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1976 May 
Date Detail:
Created Date:  1976-10-20     Completed Date:  1976-10-20     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  997-1005     Citation Subset:  IM    
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MeSH Terms
Basidiomycota / enzymology*
Cellulase / metabolism*
Glucosidases / isolation & purification,  metabolism
Glycoside Hydrolases / metabolism*
Isoenzymes / metabolism*
Polyporaceae / enzymology*
Structure-Activity Relationship
Reg. No./Substance:
0/Isoenzymes; 0/Polysaccharides; 9004-32-4/Carboxymethylcellulose; EC 3.2.1.-/Glucosidases; EC 3.2.1.-/Glycoside Hydrolases; EC

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