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dc.contributor.authorPandey, Manjula
dc.contributor.authorMishra, Saroj
dc.date.accessioned2005-03-17T09:15:41Z
dc.date.accessioned2019-02-09T07:12:26Z
dc.date.available2005-03-17T09:15:41Z
dc.date.available2019-02-09T07:12:26Z
dc.date.issued1995
dc.identifier.citationJ. Fermen. & Bioeng., 80 (5), 446-453en
dc.identifier.urihttp://localhost:8080/xmlui/handle/12345678/77
dc.description.abstractumerical Modelling of Coastal Upwelling In The Bay of Bengal Pergamon,21,(5),667-670 A 4%kilobase pairs DNA fragment from thermophilic yeast Pichia etchellsii was cloned into the vector plasmid pUC19 to form plasmid pBG55 and the encoded ,Beta-glucosidase expressed in Escherichiu coli. The effect of different carbon sources on growth and enzyme synthesis was studied in the pBG55 transformant and 0.2% (w/v) cellobiose found to be the most suitable carbon source for enzyme biosynthesis. The level of intracellularly produced Beta-glucosidase was slightly reduced on 0.2% (w/v) glucose and 0.2% (w/v) maltose. The partially purified enzyme from the Beta-glu transformant was active against a wide range of aryl Beta-glucosides and B-linked disaccharides and the preferred substrates were p-nitrophenyl-Beta-o-glucoside (PNPG), cellobiose, gentiobiose, sophorose and sucrose. While maximum enzyme activity of 62 U/1 was against pNPG at SO’C, the activities in the range of 120-170 U/1 were against various Beta-linked disaccharides at 37’C. The enzyme displayed glucose tolerance and a temperature optima profile slightly different from that exhibited by the native yeast glycosylated enzyme. The Beta-glucosidase in the crude extract of pBG55 transformant was identified as a stably produced protein of 200 kDa by PAGE-Zymogram analysis.en
dc.format.extent905563 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.subjectcloning,en
dc.subjectglucosidase expression,en
dc.subjectPichia etch&ii ,‘l-glucosidase]en
dc.titleCloning and Expression of P-Glucosidase Gene from the Yeast Pichia etchellsii
dc.typeArticleen


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