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Processive endoglucanase active in crystalline cellulose hydrolysis by the brown rot basidiomycete Gloeophyllum trabeum
Year:
2005
Authors :
Cohen, Roni
;
.
Volume :
71
Co-Authors:
Cohen, R., Department of Bacteriology, University of Wisconsin, Madison, WI 53706, United States, Sigma-Aldrich Israel, Ltd., 97770 Jerusalem, Israel
Suzuki, M.R., Institute for Microbial and Biochemical Technology, USDA Forest Products Laboratory, Madison, WI 53726, United States
Hammel, K.E., Department of Bacteriology, University of Wisconsin, Madison, WI 53706, United States, Institute for Microbial and Biochemical Technology, USDA Forest Products Laboratory, Madison, WI 53726, United States, Institute for Microbial and Biochemical Technology, USDA Forest Products Laboratory, One Gifford Pinchot Drive, Madison, WI 53726, United States
Facilitators :
From page:
2412
To page:
2417
(
Total pages:
6
)
Abstract:
Brown rot basidiomycetes have long been thought to lack the processive cellulases that release soluble sugars from crystalline cellulose. On the other hand, these fungi remove all of the cellulose, both crystalline and amorphous, from wood when they degrade it. To resolve this discrepancy, we grew Gloeophyllum trabeum on microcrystalline cellulose (Avicel) and purified the major glycosylhydrolases it produced. The most abundant extracellular enzymes in these cultures were a 42-kDa endoglucanase (Cel5A), a 39-kDa xylanase (Xyn10A), and a 28-kDa endoglucanase (Cel12A). Cel5A had significant Avicelase activity - 4.5 nmol glucose equivalents released/min/mg protein. It is a processive endoglucanase, because it hydrolyzed Avicel to cellobiose as the major product while introducing only a small proportion of reducing sugars into the remaining, insoluble substrate. Therefore, since G. trabeum is already known to produce a β-glucosidase, it is now clear that this brown rot fungus produces enzymes capable of yielding assimilable glucose from crystalline cellulose. Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Note:
Related Files :
Basidiomycota
cellulase
crystallin
enzyme
enzyme activity
enzymes
fungi
Molecular Sequence Data
Show More
Related Content
More details
DOI :
10.1128/AEM.71.5.2412-2417.2005
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
31585
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 01:03
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Scientific Publication
Processive endoglucanase active in crystalline cellulose hydrolysis by the brown rot basidiomycete Gloeophyllum trabeum
71
Cohen, R., Department of Bacteriology, University of Wisconsin, Madison, WI 53706, United States, Sigma-Aldrich Israel, Ltd., 97770 Jerusalem, Israel
Suzuki, M.R., Institute for Microbial and Biochemical Technology, USDA Forest Products Laboratory, Madison, WI 53726, United States
Hammel, K.E., Department of Bacteriology, University of Wisconsin, Madison, WI 53706, United States, Institute for Microbial and Biochemical Technology, USDA Forest Products Laboratory, Madison, WI 53726, United States, Institute for Microbial and Biochemical Technology, USDA Forest Products Laboratory, One Gifford Pinchot Drive, Madison, WI 53726, United States
Processive endoglucanase active in crystalline cellulose hydrolysis by the brown rot basidiomycete Gloeophyllum trabeum
Brown rot basidiomycetes have long been thought to lack the processive cellulases that release soluble sugars from crystalline cellulose. On the other hand, these fungi remove all of the cellulose, both crystalline and amorphous, from wood when they degrade it. To resolve this discrepancy, we grew Gloeophyllum trabeum on microcrystalline cellulose (Avicel) and purified the major glycosylhydrolases it produced. The most abundant extracellular enzymes in these cultures were a 42-kDa endoglucanase (Cel5A), a 39-kDa xylanase (Xyn10A), and a 28-kDa endoglucanase (Cel12A). Cel5A had significant Avicelase activity - 4.5 nmol glucose equivalents released/min/mg protein. It is a processive endoglucanase, because it hydrolyzed Avicel to cellobiose as the major product while introducing only a small proportion of reducing sugars into the remaining, insoluble substrate. Therefore, since G. trabeum is already known to produce a β-glucosidase, it is now clear that this brown rot fungus produces enzymes capable of yielding assimilable glucose from crystalline cellulose. Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Scientific Publication
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