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dc.contributor.authorRanjith, A-
dc.contributor.authorArumughan, C-
dc.date.accessioned2013-11-21T09:28:38Z-
dc.date.available2013-11-21T09:28:38Z-
dc.date.issued2011-
dc.identifier.citationJournal of Food Science 76(6):T130-T137;Aug 2011en_US
dc.identifier.issn0022-1147-
dc.identifier.urihttp://ir.niist.res.in:8080/jspui/handle/123456789/796-
dc.description.abstractInteractions of phenolics with other food constituents and digestive enzymes are likely to have interference with the digestion and bioavailability of food and phenolics. In this study the effect of sea buckthorn proanthocyanidins on in vitro digestion of protein was evaluated. Optimization of the extraction conditions showed that maximum recovery of sea buckthorn proanthocyanidins was obtained with acidified acetone; water mixture (60% to 70%, v/v). Crude proanthocyanidin extracts thus prepared were purified using sephadex gel column chromatography and their average degree of polymerization and the effects on enzymatic hydrolysis of bovine serum albumin as influenced by their protein precipitation capacities were studied. Average degree of polymerization of proanthocyanidins in berry pulp, kernel, seed coat, and leaves was 7.4, 5.6, 8.2, and 10.6, respectively. The EC50 values for the protein precipitation by the PA of berry pulp, kernel seed coat, and leaves were 44.2, 44.1, 65.8, and 39.8 mu g, respectively. Relative enzymatic hydrolysis of the protein-proanthocyanidin complexes was 44.1% to 60.3% for pepsin and 57.5% to 67.7% for trypsin. Interactions of sea buckthorn proanthocyanidins with food proteins and digestive enzymes might alter the protein digestibility and phenolic bioavailabilty.en_US
dc.language.isoenen_US
dc.publisherWileyen_US
dc.subjectBlueberryen_US
dc.subjectRuminantsen_US
dc.subjectPolymerizationen_US
dc.subjectDimeren_US
dc.subjectProcyanidinsen_US
dc.subjectAntioxidanten_US
dc.subjectVanillin assayen_US
dc.subjectRubisco proteinen_US
dc.subjectCondensed tanninsen_US
dc.subjectTrypsinen_US
dc.subjectProanthocyanidinsen_US
dc.subjectPepsinen_US
dc.subjectHippophae rhamnoidesen_US
dc.titleSea buckthorn (Hippophae rhamnoides) proanthocyanidins inhibit in vitro enzymatic hydrolysis of proteinen_US
dc.typeArticleen_US
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