PARTIAL PURIFICATION AND CHARACTERIZATION OF β‐GLUCOSIDASE FROM TEA SHOOT
Identifieur interne : 001848 ( Main/Exploration ); précédent : 001847; suivant : 001849PARTIAL PURIFICATION AND CHARACTERIZATION OF β‐GLUCOSIDASE FROM TEA SHOOT
Auteurs : Renu Rawat [Inde] ; Ashu Gulati ; Robin Joshi [Inde]Source :
- Journal of Food Biochemistry [ 0145-8884 ] ; 2011-06.
Abstract
β‐glucosidase was purified from the shoots of Camellia sinensis cv. Asha from Kangra valley following acetone precipitation, hydroxyapatite, gel filtration and ultrafiltration to apparent homogeneity. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of purified enzyme indicated a dimer with a larger subunit of ∼63 kD and a smaller subunit of ∼36 kD, molecular mass of ∼99 kD. The native form was confirmed by nondenaturating polyacrylamide gel electrophoresis. Optimum pH was 6.2, optimum temperature within 45–50C. β‐glucosidase exhibited Km value of 0.16 mM and kcat of 11,000/min with the substrate p‐nitrophenyl‐β‐D‐glucopyranoside (pNpGlc) at 37C, pH 6.2. Substrate staining with 6‐bromo‐2‐napthyl‐β‐D‐glucopyranoside ruled out the possibility of any isozymic forms. The purified enzyme showed specificity toward pNpGlc and equivalent activity toward p‐nitrophenyl‐β‐D‐fucopyranoside. The enzyme liberated geraniol, linalool, phenylethanol, benzyl alcohol on incubation with tea shoot aqueous glycosidic extract. Highest activity was observed toward pNpGlc (100%), followed by p‐nitrophenyl‐β‐D‐mannopyranoside (79%) and p‐nitrophenyl‐β‐D‐fucopyranoside (75%), p‐nitrophenyl‐β‐D‐galactopyranoside (64%) etc., implying highly active β‐glucosidase among other glycosidases.
Url:
DOI: 10.1111/j.1745-4514.2010.00422.x
Affiliations:
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">PARTIAL PURIFICATION AND CHARACTERIZATION OF β‐GLUCOSIDASE FROM TEA SHOOT</title><author><name sortKey="Rawat, Renu" sort="Rawat, Renu" uniqKey="Rawat R" first="Renu" last="Rawat">Renu Rawat</name></author><author><name sortKey="Gulati, Ashu" sort="Gulati, Ashu" uniqKey="Gulati A" first="Ashu" last="Gulati">Ashu Gulati</name></author><author><name sortKey="Joshi, Robin" sort="Joshi, Robin" uniqKey="Joshi R" first="Robin" last="Joshi">Robin Joshi</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:AB34BA994F50EF10EBEB850499AA06D9B3BD1C2C</idno><date when="2011" year="2011">2011</date><idno type="doi">10.1111/j.1745-4514.2010.00422.x</idno><idno type="url">https://api.istex.fr/document/AB34BA994F50EF10EBEB850499AA06D9B3BD1C2C/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001196</idno><idno type="wicri:Area/Istex/Curation">001196</idno><idno type="wicri:Area/Istex/Checkpoint">000269</idno><idno type="wicri:doubleKey">0145-8884:2011:Rawat R:partial:purification:and</idno><idno type="wicri:Area/Main/Merge">001874</idno><idno type="wicri:Area/Main/Curation">001848</idno><idno type="wicri:Area/Main/Exploration">001848</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">PARTIAL PURIFICATION AND CHARACTERIZATION OF β‐GLUCOSIDASE FROM TEA SHOOT</title><author><name sortKey="Rawat, Renu" sort="Rawat, Renu" uniqKey="Rawat R" first="Renu" last="Rawat">Renu Rawat</name><affiliation wicri:level="1"><country xml:lang="fr">Inde</country><wicri:regionArea>Institute of Himalayan Bioresource Technology, Council of Scientific and Industrial Research, Palampur 176061 (H.P.)</wicri:regionArea><wicri:noRegion>Palampur 176061 (H.P.)</wicri:noRegion></affiliation></author><author><name sortKey="Gulati, Ashu" sort="Gulati, Ashu" uniqKey="Gulati A" first="Ashu" last="Gulati">Ashu Gulati</name></author><author><name sortKey="Joshi, Robin" sort="Joshi, Robin" uniqKey="Joshi R" first="Robin" last="Joshi">Robin Joshi</name><affiliation wicri:level="1"><country xml:lang="fr">Inde</country><wicri:regionArea>Institute of Himalayan Bioresource Technology, Council of Scientific and Industrial Research, Palampur 176061 (H.P.)</wicri:regionArea><wicri:noRegion>Palampur 176061 (H.P.)</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Food Biochemistry</title><idno type="ISSN">0145-8884</idno><idno type="eISSN">1745-4514</idno><imprint><publisher>Blackwell Publishing Inc</publisher><pubPlace>Malden, USA</pubPlace><date type="published" when="2011-06">2011-06</date><biblScope unit="volume">35</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="953">953</biblScope><biblScope unit="page" to="975">975</biblScope></imprint><idno type="ISSN">0145-8884</idno></series><idno type="istex">AB34BA994F50EF10EBEB850499AA06D9B3BD1C2C</idno><idno type="DOI">10.1111/j.1745-4514.2010.00422.x</idno><idno type="ArticleID">JFBC422</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0145-8884</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract">β‐glucosidase was purified from the shoots of Camellia sinensis cv. Asha from Kangra valley following acetone precipitation, hydroxyapatite, gel filtration and ultrafiltration to apparent homogeneity. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of purified enzyme indicated a dimer with a larger subunit of ∼63 kD and a smaller subunit of ∼36 kD, molecular mass of ∼99 kD. The native form was confirmed by nondenaturating polyacrylamide gel electrophoresis. Optimum pH was 6.2, optimum temperature within 45–50C. β‐glucosidase exhibited Km value of 0.16 mM and kcat of 11,000/min with the substrate p‐nitrophenyl‐β‐D‐glucopyranoside (pNpGlc) at 37C, pH 6.2. Substrate staining with 6‐bromo‐2‐napthyl‐β‐D‐glucopyranoside ruled out the possibility of any isozymic forms. The purified enzyme showed specificity toward pNpGlc and equivalent activity toward p‐nitrophenyl‐β‐D‐fucopyranoside. The enzyme liberated geraniol, linalool, phenylethanol, benzyl alcohol on incubation with tea shoot aqueous glycosidic extract. Highest activity was observed toward pNpGlc (100%), followed by p‐nitrophenyl‐β‐D‐mannopyranoside (79%) and p‐nitrophenyl‐β‐D‐fucopyranoside (75%), p‐nitrophenyl‐β‐D‐galactopyranoside (64%) etc., implying highly active β‐glucosidase among other glycosidases.</div></front></TEI><affiliations><list><country><li>Inde</li></country></list><tree><noCountry><name sortKey="Gulati, Ashu" sort="Gulati, Ashu" uniqKey="Gulati A" first="Ashu" last="Gulati">Ashu Gulati</name></noCountry><country name="Inde"><noRegion><name sortKey="Rawat, Renu" sort="Rawat, Renu" uniqKey="Rawat R" first="Renu" last="Rawat">Renu Rawat</name></noRegion><name sortKey="Joshi, Robin" sort="Joshi, Robin" uniqKey="Joshi R" first="Robin" last="Joshi">Robin Joshi</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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