β-Glucosidase catalyzing specific hydrolysis of an iridoid β-glucoside from Plumeria obtusa

An iridoid β-glucoside, namely plumieride coumarate glucoside, was isolated from the Plumeria obtusa (white frangipani) flower. A β-glucosidase, purified to homogeneity from P. obtusa, could hydrolyze plumieride coumarate glucoside to its corresponding 13-O-coumarylplumieride. Plumeriaβ-glucosidase...

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Main Authors: Doungkamol Boonclarm, Thakorn Sornwatana, Dumrongkiet Arthan, Palangpon Kongsaeree, 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/123456789/22995
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spelling th-mahidol.229952018-08-20T14:13:18Z β-Glucosidase catalyzing specific hydrolysis of an iridoid β-glucoside from Plumeria obtusa Doungkamol Boonclarm Thakorn Sornwatana Dumrongkiet Arthan Palangpon Kongsaeree Jisnuson Svasti Mahidol University Biochemistry, Genetics and Molecular Biology Medicine An iridoid β-glucoside, namely plumieride coumarate glucoside, was isolated from the Plumeria obtusa (white frangipani) flower. A β-glucosidase, purified to homogeneity from P. obtusa, could hydrolyze plumieride coumarate glucoside to its corresponding 13-O-coumarylplumieride. Plumeriaβ-glucosidase is a monomeric glycoprotein with a molecular weight of 60.6 kDa and an isoelectric point of 4.90. The purified β-glucosidase had an optimum pH of 5.5 for p-nitrophenol (pNP)-β-D-glucoside and for its natural substrate. The Km values for pNP-β-D-glucoside and Plumeriaβ-glucoside were 5.04±0.36 mM and 1.02±0.06 mM, respectively. The enzyme had higher hydrolytic activity towards pNP-β-D-fucoside than pNP-β-D-glucoside. No activity was found for other pNP-glycosides. Interestingly, the enzyme showed a high specificity for the glucosyl group attached to the C-7″ position of the coumaryl moiety of plumieride coumarate glucoside. The enzyme showed poor hydrolysis of 4-methylumbelliferyl-β-glucoside and esculin, and did not hydrolyze alkyl-β-glucosides, glucobioses, cyanogenic-β-glucosides, steroid β-glucosides, nor other iridoid β-glucosides. In conclusion, the Plumeriaβ-glucosidase shows high specificity for its natural substrate, plumieride coumarate glucoside. ©Institute of Biochemistry and Cell Biology, SIBS, CAS. 2018-08-20T06:50:25Z 2018-08-20T06:50:25Z 2006-08-01 Article Acta Biochimica et Biophysica Sinica. Vol.38, No.8 (2006), 563-570 10.1111/j.1745-7270.2006.00196.x 17457270 16729145 2-s2.0-33747349036 https://repository.li.mahidol.ac.th/handle/123456789/22995 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=33747349036&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 Biochemistry, Genetics and Molecular Biology
Medicine
spellingShingle Biochemistry, Genetics and Molecular Biology
Medicine
Doungkamol Boonclarm
Thakorn Sornwatana
Dumrongkiet Arthan
Palangpon Kongsaeree
Jisnuson Svasti
β-Glucosidase catalyzing specific hydrolysis of an iridoid β-glucoside from Plumeria obtusa
description An iridoid β-glucoside, namely plumieride coumarate glucoside, was isolated from the Plumeria obtusa (white frangipani) flower. A β-glucosidase, purified to homogeneity from P. obtusa, could hydrolyze plumieride coumarate glucoside to its corresponding 13-O-coumarylplumieride. Plumeriaβ-glucosidase is a monomeric glycoprotein with a molecular weight of 60.6 kDa and an isoelectric point of 4.90. The purified β-glucosidase had an optimum pH of 5.5 for p-nitrophenol (pNP)-β-D-glucoside and for its natural substrate. The Km values for pNP-β-D-glucoside and Plumeriaβ-glucoside were 5.04±0.36 mM and 1.02±0.06 mM, respectively. The enzyme had higher hydrolytic activity towards pNP-β-D-fucoside than pNP-β-D-glucoside. No activity was found for other pNP-glycosides. Interestingly, the enzyme showed a high specificity for the glucosyl group attached to the C-7″ position of the coumaryl moiety of plumieride coumarate glucoside. The enzyme showed poor hydrolysis of 4-methylumbelliferyl-β-glucoside and esculin, and did not hydrolyze alkyl-β-glucosides, glucobioses, cyanogenic-β-glucosides, steroid β-glucosides, nor other iridoid β-glucosides. In conclusion, the Plumeriaβ-glucosidase shows high specificity for its natural substrate, plumieride coumarate glucoside. ©Institute of Biochemistry and Cell Biology, SIBS, CAS.
author2 Mahidol University
author_facet Mahidol University
Doungkamol Boonclarm
Thakorn Sornwatana
Dumrongkiet Arthan
Palangpon Kongsaeree
Jisnuson Svasti
format Article
author Doungkamol Boonclarm
Thakorn Sornwatana
Dumrongkiet Arthan
Palangpon Kongsaeree
Jisnuson Svasti
author_sort Doungkamol Boonclarm
title β-Glucosidase catalyzing specific hydrolysis of an iridoid β-glucoside from Plumeria obtusa
title_short β-Glucosidase catalyzing specific hydrolysis of an iridoid β-glucoside from Plumeria obtusa
title_full β-Glucosidase catalyzing specific hydrolysis of an iridoid β-glucoside from Plumeria obtusa
title_fullStr β-Glucosidase catalyzing specific hydrolysis of an iridoid β-glucoside from Plumeria obtusa
title_full_unstemmed β-Glucosidase catalyzing specific hydrolysis of an iridoid β-glucoside from Plumeria obtusa
title_sort β-glucosidase catalyzing specific hydrolysis of an iridoid β-glucoside from plumeria obtusa
publishDate 2018
url https://repository.li.mahidol.ac.th/handle/123456789/22995
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