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dc.contributor.authorWamalwa Benson Munyali.
dc.contributor.authorSakka Makiko.
dc.contributor.authorShiundu Paul Mwanza.
dc.contributor.authorOhmiya Kunio.
dc.contributor.authorKimura Tetsuya.
dc.contributor.authorSakka Kazuo.
dc.date.accessioned2013-06-22T08:53:29Z
dc.date.available2013-06-22T08:53:29Z
dc.date.issued2006-10
dc.identifier.citationApplied and environmental microbiology, Oct. 2006, p. 6851–6853en
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/pubmed/16950908
dc.identifier.urihttp://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/38046
dc.descriptionFull Texten
dc.description.abstractCelB (BH0603) from Bacillus halodurans is a modular glycoside hydrolase with a family 5 catalytic module, an immunoglobulin-like module, and module PfamB of unknown function. The recombinant PfamB module bound to Avicel and was essential for CelB hydrolytic function. We propose that module PfamB be designated a new carbohydrate-binding module.en
dc.language.isoenen
dc.subjectCarbohydrate-binding moduleen
dc.subjectCelB (BH0603)en
dc.subjectAlkaliphilic Bacterium Bacillus haloduransen
dc.titleEssentiality of a newly identified carbohydrate-binding module for the function of CelB (BH0603) from the Alkaliphilic Bacterium Bacillus haloduransen
dc.typeArticleen
local.publisherDepartment of Chemisty, University of Nairobien


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