Purification and characterization of two B-glucosidases from a thermo-tolerant yeast pichia etchellsii

dc.creatorWallecha, Anu
dc.creatorMishra, Saroj
dc.date.accessioned2005-07-30T09:54:17Z
dc.date.accessioned2019-02-09T07:12:01Z
dc.date.accessioned2022-07-11T08:52:07Z
dc.date.available2005-07-30T09:54:17Z
dc.date.available2019-02-09T07:12:01Z
dc.date.available2022-07-11T08:52:07Z
dc.date.created2005-07-30T09:54:17Z
dc.date.created2019-02-09T07:12:01Z
dc.date.issued2003
dc.description.abstractThe 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.
dc.identifierBiochimica Biophysica acta, 1649, 74– 84
dc.identifierhttp://localhost:8080/xmlui/handle/12345678/630
dc.identifier.urihttps://demo7.dspace.org/handle/10673/8205
dc.languageen
dc.subjectB-Glucosidase
dc.subjectPichia etchellsii
dc.subjectAlkyl-glucoside
dc.subjectGlycosyl transferase activity
dc.titlePurification and characterization of two B-glucosidases from a thermo-tolerant yeast pichia etchellsii
dc.typeArticle
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