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dc.contributor.authorWamalwa Benson Munyali.
dc.contributor.authorZhao Guangshan.
dc.contributor.authorSakka Makiko.
dc.contributor.authorShiundu Paul Mwanza.
dc.contributor.authorKimura Tetsuya.
dc.contributor.authorSakka Kazuo.
dc.date.accessioned2013-06-14T11:35:16Z
dc.date.available2013-06-14T11:35:16Z
dc.date.issued2007-03
dc.identifier.citationBioscience, Biotechnology, and Biochemistry Vol. 71 (2007) No. 3 P 688-693en
dc.identifier.urihttps://www.jstage.jst.go.jp/article/bbb/71/3/71_60477/_article
dc.identifier.urihttp://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/33851
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/pubmed/17341817
dc.description.abstractThe putative xyn11A structural gene (BH0899) encoding a family-11 xylanase from alkaliphilic Bacillus halodurans strain C-125 was heterologously expressed in the yeast Kluyveromyces lactis CBS 1065 and secreted to a level of 156 μg/ml under selective culture conditions in shake flasks. The Xyn11A production level in shake flask cultures of K. lactis CBS 1065 was higher than that reported for other xylanase genes placed under the control of the regulated LAC4 promoter on a plasmid containing an entire sequence of pKD1 from Kluyveromyces drosophilarium. Recombinant Xyn11A was highly active over pH range from 3 to 10, with maximal activity around pH 7. The enzyme showed a specific activity of 628 U/mg-protein on birchwood xylan as substrate, but no cellulase or β-xylosidase activity.en
dc.language.isoenen
dc.titleHigh-Level Heterologous Expression of Bacillus halodurans Putative Xylanase Xyn11A (BH0899) in Kluyveromyces lactien
dc.typeArticleen
local.publisherDepartment of Chemistry, University of Nairobien


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