Catalytic properties of the cellulose-binding endoglucanase F from Fibrobacter succinogenes S85
The celF gene from the predominant cellulolytic ruminal bacterium Fibrobacter succinogenes encodes a 118.3-kDa cellulose-binding endoglucanase, endoglucanase F (EGF). This enzyme possesses an N-terminal cellulose-binding domain and a C-terminal catalytic domain. The purified catalytic domain display...
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Published in | Applied and Environmental Microbiology Vol. 63; no. 6; pp. 2449 - 2453 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Society for Microbiology
01.06.1997
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Subjects | |
Online Access | Get full text |
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Summary: | The celF gene from the predominant cellulolytic ruminal bacterium Fibrobacter succinogenes encodes a 118.3-kDa cellulose-binding endoglucanase, endoglucanase F (EGF). This enzyme possesses an N-terminal cellulose-binding domain and a C-terminal catalytic domain. The purified catalytic domain displayed an activity profile typical of an endoglucanase, with high catalytic activity on carboxymethyl cellulose and barley beta-glucan. Immunoblotting of EGF and the formerly characterized endoglucanase 2 (EG2) from F. succinogenes with antibodies prepared against each of the enzymes demonstrated that EGF and EG2 contain cross-reactive epitopes. This data in conjunction with evidence that the proteins are the same size, share a 19-residue internal amino acid sequence, possess similar catalytic properties, and both bind to cellulose allows the conclusion that celF codes for EG2 |
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Bibliography: | L51 9747267 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0099-2240 1098-5336 |
DOI: | 10.1128/aem.63.6.2449-2453.1997 |