Please use this identifier to cite or link to this item: http://localhost:8080/xmlui/handle/123456789/796
Title: Sea buckthorn (Hippophae rhamnoides) proanthocyanidins inhibit in vitro enzymatic hydrolysis of protein
Authors: Ranjith, A
Arumughan, C
Keywords: Blueberry
Ruminants
Polymerization
Dimer
Procyanidins
Antioxidant
Vanillin assay
Rubisco protein
Condensed tannins
Trypsin
Proanthocyanidins
Pepsin
Hippophae rhamnoides
Issue Date: 2011
Publisher: Wiley
Citation: Journal of Food Science 76(6):T130-T137;Aug 2011
Abstract: Interactions 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.
URI: http://ir.niist.res.in:8080/jspui/handle/123456789/796
ISSN: 0022-1147
Appears in Collections:2011

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