Furostanol glycoside 26-O-β-glucosidase from the leaves of Solanum torvum

A 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 monomeri...

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Main Authors: Dumrongkiet Arthan, Prasat Kittakoop, Asim Esen, Jisnuson Svasti
Other Authors: Mahidol University
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Published: 2018
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Online Access:https://repository.li.mahidol.ac.th/handle/123456789/22926
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spelling th-mahidol.229262018-08-20T14:25:34Z Furostanol glycoside 26-O-β-glucosidase from the leaves of Solanum torvum Dumrongkiet Arthan Prasat Kittakoop Asim Esen Jisnuson Svasti Mahidol University Thailand National Center for Genetic Engineering and Biotechnology Virginia Polytechnic Institute and State University Agricultural and Biological Sciences Biochemistry, Genetics and Molecular Biology Chemistry Pharmacology, Toxicology and Pharmaceutics A 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. 2018-08-20T06:48:48Z 2018-08-20T06:48:48Z 2006-01-01 Article Phytochemistry. Vol.67, No.1 (2006), 27-33 10.1016/j.phytochem.2005.09.035 00319422 2-s2.0-29144497987 https://repository.li.mahidol.ac.th/handle/123456789/22926 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=29144497987&origin=inward
institution Mahidol University
building Mahidol University Library
continent Asia
country Thailand
Thailand
content_provider Mahidol University Library
collection Mahidol University Institutional Repository
topic Agricultural and Biological Sciences
Biochemistry, Genetics and Molecular Biology
Chemistry
Pharmacology, Toxicology and Pharmaceutics
spellingShingle Agricultural and Biological Sciences
Biochemistry, Genetics and Molecular Biology
Chemistry
Pharmacology, Toxicology and Pharmaceutics
Dumrongkiet Arthan
Prasat Kittakoop
Asim Esen
Jisnuson Svasti
Furostanol glycoside 26-O-β-glucosidase from the leaves of Solanum torvum
description A 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.
author2 Mahidol University
author_facet Mahidol University
Dumrongkiet Arthan
Prasat Kittakoop
Asim Esen
Jisnuson Svasti
format Article
author Dumrongkiet Arthan
Prasat Kittakoop
Asim Esen
Jisnuson Svasti
author_sort Dumrongkiet Arthan
title Furostanol glycoside 26-O-β-glucosidase from the leaves of Solanum torvum
title_short Furostanol glycoside 26-O-β-glucosidase from the leaves of Solanum torvum
title_full Furostanol glycoside 26-O-β-glucosidase from the leaves of Solanum torvum
title_fullStr Furostanol glycoside 26-O-β-glucosidase from the leaves of Solanum torvum
title_full_unstemmed Furostanol glycoside 26-O-β-glucosidase from the leaves of Solanum torvum
title_sort furostanol glycoside 26-o-β-glucosidase from the leaves of solanum torvum
publishDate 2018
url https://repository.li.mahidol.ac.th/handle/123456789/22926
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