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dc.contributor.authorDumrongkiet Arthanen_US
dc.contributor.authorPrasat Kittakoopen_US
dc.contributor.authorAsim Esenen_US
dc.contributor.authorJisnuson Svastien_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherThailand National Center for Genetic Engineering and Biotechnologyen_US
dc.contributor.otherVirginia Polytechnic Institute and State Universityen_US
dc.date.accessioned2018-08-20T06:48:48Z-
dc.date.available2018-08-20T06:48:48Z-
dc.date.issued2006-01-01en_US
dc.identifier.citationPhytochemistry. Vol.67, No.1 (2006), 27-33en_US
dc.identifier.issn00319422en_US
dc.identifier.other2-s2.0-29144497987en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=29144497987&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/22926-
dc.description.abstractA β-glucosidase (torvosidase) was purified to homogeneity from the young leaves of Solanum torvum. The enzyme was highly specific for cleavage of the glucose unit attached to the C-26 hydroxyl of furostanol glycosides from the same plant, namely torvosides A and H. Purified torvosidase is a monomeric glycoprotein, with a native molecular weight of 87 kDa by gel filtration and a pI of 8.8 by native agarose IEF. Optimum pH of the enzyme for p-nitrophenyl-β-glucoside and torvoside H was 5.0. Kinetic studies showed that Kmvalues for torvoside A (0.063 mM) and torvoside H (0.068 mM) were much lower than those for synthetic substrates, pNP-β-glucoside (1.03 mM) and 4-methylumbelliferyl-β-glucoside (0.78 mM). The enzyme showed strict specificity for the β-d-glucosyl bond when tested for glycone specificity. Torvosidase hydrolyses only torvosides and dalcochinin-8′- β-glucoside, which is the natural substrate of Thai rosewood β-glucosidase, but does not hydrolyse other natural substrates of the GH1 β-glucosidases or of the GH3 β-glucosidase families. Torvosidase also hydrolyses C5-C10alkyl-β-glucosides, with a rate of hydrolysis increasing with longer alkyl chain length. The internal peptide sequence of Solanum β-glucosidase shows high similarity to the sequences of family GH3 glycosyl hydrolases. © 2005 Elsevier Ltd. All rights reserved.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=29144497987&origin=inwarden_US
dc.subjectAgricultural and Biological Sciencesen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemistryen_US
dc.subjectPharmacology, Toxicology and Pharmaceuticsen_US
dc.titleFurostanol glycoside 26-O-β-glucosidase from the leaves of Solanum torvumen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/j.phytochem.2005.09.035en_US
Appears in Collections:Scopus 2006-2010

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