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dc.contributor.authorArmesilla, Angel Luis
dc.contributor.authorThurston, Christopher F.
dc.contributor.authorYague, Ernesto
dc.date.accessioned2007-01-24T14:42:50Z
dc.date.available2007-01-24T14:42:50Z
dc.date.issued1994
dc.date.submitted2007-01-24
dc.identifier.citationFEMS Microbiology Letters, 116(3): 293-299
dc.identifier.issn0378-1097
dc.identifier.pmid8181702
dc.identifier.doi10.1111/j.1574-6968.1994.tb06718.x
dc.identifier.urihttp://hdl.handle.net/2436/7745
dc.descriptionMetadata only
dc.description.abstractThe 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.
dc.language.isoen
dc.publisherBlackwell Publishing
dc.relation.urlhttp://www3.interscience.wiley.com/journal/119276698/abstract
dc.subjectAgaricus bisporus
dc.subjectCEL1
dc.subjectCellulose
dc.subjectProteins
dc.titleCEL1: a novel cellulose binding protein secreted by Agaricus bisporus during growth on crystalline cellulose.
dc.typeJournal article
dc.format.digYES
html.description.abstractThe 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.


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