Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.foodres.2013.07.062
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dc.titleInhibiting enzymatic starch digestion by the phenolic compound diboside A: A mechanistic and in silico study
dc.contributor.authorLiu, T.
dc.contributor.authorYip, Y.M.
dc.contributor.authorSong, L.
dc.contributor.authorFeng, S.
dc.contributor.authorLiu, Y.
dc.contributor.authorLai, F.
dc.contributor.authorZhang, D.
dc.contributor.authorHuang, D.
dc.date.accessioned2014-10-16T08:31:32Z
dc.date.available2014-10-16T08:31:32Z
dc.date.issued2013-11
dc.identifier.citationLiu, T., Yip, Y.M., Song, L., Feng, S., Liu, Y., Lai, F., Zhang, D., Huang, D. (2013-11). Inhibiting enzymatic starch digestion by the phenolic compound diboside A: A mechanistic and in silico study. Food Research International 54 (1) : 595-600. ScholarBank@NUS Repository. https://doi.org/10.1016/j.foodres.2013.07.062
dc.identifier.issn09639969
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/94051
dc.description.abstractRetarding the starch digestion rate is the key to produce low glycemic index (GI) foods for diabetic patients in prevention of postprandial hyperglycemia. In the search for naturally-occurring starch hydrolase inhibitors as active ingredients for low GI foods, we applied a high throughput assay to screen hundreds of edible botanical materials and discovered that a phenylpropanoid sucrose ester, diboside A (1,3,6'-tri-p-coumaroyl-6-feruloyl sucrose), isolated from the root of wild buckwheat exhibited potent α-amylase inhibitory activity with an IC50 of 26.9μM. Kinetic study revealed that it is an uncompetitive inhibitor of α-amylase with a Ki of 5.1μM. Moreover, diboside A inhibits rat intestinal sucrase as a noncompetitive inhibitor with a Ki of 72.4μM. Remarkably, it has no measurable activity towards maltase. An in silico molecular docking study shows that there are two possible allosteric binding sites between diboside A and enzyme-substrate complex. Binding site one is a more probable binding site because of lower energy of the ternary complex formed by hydrogen bonds and electrostatic interactions. Our results suggest that phenylpropanoid sucrose esters have potential as an active ingredient for low GI foods. © 2013 Elsevier Ltd.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.foodres.2013.07.062
dc.sourceScopus
dc.subjectα-Amylase
dc.subjectDiboside A
dc.subjectMolecular docking
dc.subjectStarch
dc.subjectSucrase
dc.subjectUncompetitive inhibitor
dc.typeArticle
dc.contributor.departmentCHEMISTRY
dc.description.doi10.1016/j.foodres.2013.07.062
dc.description.sourcetitleFood Research International
dc.description.volume54
dc.description.issue1
dc.description.page595-600
dc.description.codenFORIE
dc.identifier.isiut000329377700072
Appears in Collections:Staff Publications

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