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Processive endoglucanase active in crystalline cellulose hydrolysis by the brown rot Basidiomycete Gloeophyllum trabeumAuthor(s): Roni Cohen; Melissa R. Suzuki; Kenneth E. Hammel
Source: Applied and environmental microbiology. Vol. 71, no. 5 (May 2005): pages 2412-2417.
Publication Series: Miscellaneous Publication
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DescriptionBrown 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 ß- glucosidase, it is now clear that this brown rot fungus produces enzymes capable of yielding assimilable glucose from crystalline cellulose.
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CitationCohen, Roni; Suzuki, Melissa R.; Hammel, Kenneth E. 2005. Processive endoglucanase active in crystalline cellulose hydrolysis by the brown rot Basidiomycete Gloeophyllum trabeum. Applied and environmental microbiology. Vol. 71, no. 5 (May 2005): pages 2412-2417.
KeywordsEndoglucanase, crystalline cellulose hydrolysis, brown rot, Basidiomycetes, Gloephyllum trabeum
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