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Please use this identifier to cite or link to this item:
http://hdl.handle.net/2074/630
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| DC Field | Value | Language |
|---|
| contributor.author | Wallecha, Anu | - |
| contributor.author | Mishra, Saroj | - |
| date.accessioned | 2005-07-30T09:54:17Z | - |
| date.available | 2005-07-30T09:54:17Z | - |
| date.issued | 2003 | - |
| identifier.citation | Biochimica Biophysica acta, 1649, 74– 84 | en |
| identifier.uri | http://eprint.iitd.ac.in/dspace/handle/2074/630 | - |
| description.abstract | The thermo-tolerant yeast Pichia etchellsii produced two cell-wall-bound inducible B-glucosidases, BGLI (molecular mass 186 kDa) and BGLII (molecular mass 340 kDa), which were purified by a simple, three-step method, comprising ammonium sulfate precipitation, ionexchange and hydroxyapatite chromatography. The two enzymes exhibited a similar pH and temperature optima, inhibitory effect by glucose and gluconolactone, and stability in the pH range of 3.0–9.0. Placed in family 3 of glycosylhydrolase families, BGLI was more active on salicin, p-nitrophenyl B-D-glucopyranoside and alkyl B-D-glucosides whereas BGLII was most active on cellobiose. kcat and KM values were
determined for a number of substrates and, for BGLI, it was established that the deglycosylation step was equally effective on aryl- and alkylglucosides while the glycosylation step varied depending on the substrate used. This information was used to synthesize alkyl-glucosides (up
to a chain length of C10) using dimethyl sulfoxide stabilized single-phase reaction microenvironment. About 12% molar yield of octylglucoside was calculated based on a simple spectrophotometric method developed for its estimation. Further, detailed comparison of properties of the enzymes indicated these to be different from the previously cloned B-glucosidases from this yeast. | en |
| format.extent | 2804423 bytes | - |
| format.mimetype | application/pdf | - |
| language.iso | en | en |
| subject | B-Glucosidase | en |
| subject | Pichia etchellsii | en |
| subject | Alkyl-glucoside | en |
| subject | Glycosyl transferase activity | en |
| title | Purification and characterization of two B-glucosidases from a thermo-tolerant yeast pichia etchellsii | en |
| type | Article | en |
| Appears in Collections: | Biochemical Engg. and Biotechnology
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| wallechapur2003.pdf | | 2738Kb | Adobe PDF | View/Open |
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