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http://hdl.handle.net/2074/318
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| Title: | Expression and characterization of Pichia etchellsii B-glucosidase in Escherichia coli |
| Authors: | Pandey, Manjula
Mishra, Saroj |
| Keywords: | Cellulose hydrolysis
Oligosaccharide biosynthesis
Yeast enzyme expression
Broad-substrate-specificity enzyme |
| Issue Date: | 1997 |
| Citation: | Gene,190(1), 45-51 |
| 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 w... |
| URI: | http://eprint.iitd.ac.in/dspace/handle/2074/318 |
| Appears in Collections: | Biochemical Engg. and Biotechnology
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| pandeyexp97.pdf | | 707Kb | Adobe PDF | View/Open |
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