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Expression and characterization of Pichia etchellsii B-glucosidase in Escherichia coli

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Author: Pandey, Manjula; Mishra, Saroj

Advisor: Advisor

Date: 1997

Publisher:
Citation: Gene,190(1

Series/Report no.:
Item Type: Article

Keywords: Cellulose hydrolysis; Oligosaccharide biosynthesis; Yeast enzyme expression; Broad-substrate-specificity enzyme

Abstract: The B-glucosidase enzyme is important as the terminal enzyme involved in hydrolysis of cellobiose and short-chain cellodextrins generated during enzymatic cellulose degradation. Under controlled reaction conditions the enzyme also displays cello-oligosaccha-ride synthesizing ability (based on either the thermodynamic or kinetic approach). We present here the purification of the enzyme P-glucosidase (BGL) of Pichia etchellsii from recombinant pBG55 Escherichia coli clone. The kinetic parameters, substrate specificity and oligosaccharide synthesizing ability of the purified enzyme are also reported. The purified 200-kDa protein (tetramer of 50 kDa) was identified as a broad-substrate-specificity enzyme exhibiting increased temperature and glucose tolerance compared to the native yeast enzyme. Temperature directed substrate specificity for aryl fl,l-4 linkage, and B( l-2), j3( l-4), fl( l-6) and 8(2-1) linkages in various natural disaccharides was observed. Glycosylation of the enzyme was found to be unimportant for enzyme activity. With both cellobiose and glucose, oligosaccharide synthesis was detected. The implications of this information with regard to cellulose hydrolysis and oligosaccharide synthesis are discussed.
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Shankar B. Chavan
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shankar.chavan@library.iitd.ac.in
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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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