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Cloning and Expression of P-Glucosidase Gene from the Yeast Pichia etchellsii

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Author: Pandey, Manjula; Mishra, Saroj

Advisor: Advisor

Date: 1995

Publisher:
Citation: J. Fermen.

Series/Report no.:
Item Type: Article

Keywords: cloning,; glucosidase expression,; Pichia etch&ii ,‘l-glucosidase]

Abstract: umerical 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.
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Shankar B. Chavan
Computer Applications Division
Central Library, IIT Delhi
shankar.chavan@library.iitd.ac.in
NDLTD
Shodhganga
NDL
ePrints@IISc
etd@IISc
IR@IIT Bombay
NewsClips @IITD
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