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Wolverhampton Intellectual Repository and E-Theses > Research Institutes > Research Institute in Healthcare Science > Molecular Pharmacology Research Group > CEL1: a novel cellulose binding protein secreted by Agaricus bisporus during growth on crystalline cellulose.

Please use this identifier to cite or link to this item: http://hdl.handle.net/2436/7745
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Title: CEL1: a novel cellulose binding protein secreted by Agaricus bisporus during growth on crystalline cellulose.
Authors: Armesilla, Angel Luis
Thurston, Christopher F.
Yague, Ernesto
Citation: FEMS Microbiology Letters, 116(3): 293-299
Publisher: Blackwell Publishing
Issue Date: 1994
URI: http://hdl.handle.net/2436/7745
DOI: 10.1111/j.1574-6968.1994.tb06718.x
PubMed ID: 8181702
Additional Links: http://www3.interscience.wiley.com/journal/119276698/abstract
Abstract: The cel1 gene of Agaricus bisporus encodes a protein (CEL1) that has an architecture resembling the multi-domain fungal cellulases, although the sequence of its putative catalytic core is not matched by any other in the protein and nucleic acid data bases. The N-terminal half of the putative catalytic domain of CEL1 was expressed in Escherichia coli as a fusion protein with glutathione-S-transferase. The fusion protein was used to raise a CEL1-specific antibody. CEL1 was detected as an extracellular 49.8 kDa protein in A. bisporus cellulose-grown cultures, where it bound strongly to cellulose. CEL1 was neither an endoglucanase, a cellobiohydrolase able to hydrolyze fluorogenic cellobiosides, a beta-glucosidase, a xylanase, nor a cellobiose: quinone oxidoreductase. CEL1 was present in some fractions of culture fluid separated by electrophoresis which released soluble sugars from crystalline cellulose.
Type: Article
Language: en
Description: Metadata only
Keywords: Agaricus bisporus
CEL1
Cellulose
Proteins
ISSN: 0378-1097
Appears in Collections: Molecular Pharmacology Research Group

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