The antioxidative activity of hydrolysate peptides from oysters (Crassostrea talienwhanensis) was investigated. After hydrolysis with subtilisin, the yields of the peptides that were soluble in trichloroacetic acid (TCA-soluble) and the antioxidant activities of the resulting hydrolysate were determined using an orthogonal design and a hydroxyl radical scavenging reaction. The hydrolysate was fractionated using Sephadex G-15 gel filtration chromatography, and the two resulting bioactive peptides were subsequently purified by RP-HPLC with a Kromasil C18 (ODS) column. The amino acid sequences were analyzed by nano-ESI-MS/MS.

The critical reaction temperature, pH, hydrolysis time and enzyme-to-substrate (E/S) ratio were determined for the optimum hydrolysis with subtilisin, and the E/S ratio was found to be the most critical reaction condition. The amino acid sequences of the peptides (518 and 440 Da) were proline-valinemethionine- glycine-aspartic acid (PVMGA) and glutamine-histidine-glycine-valine (QHGV), respectively. These two novel peptides exhibited high antioxidative actions based on their hydroxyl and 1,1-diphenyl- 2-picrylhydrazyl (DPPH) radical scavenging activities.

Item Type:	Refereed Article
Keywords:	antioxidative peptide, hydrolysate, oyster, Crassostrea talienwhanensis, radical scavenging activity, subtilisin
Research Division:	Agricultural and Veterinary Sciences
Research Group:	Fisheries Sciences
Research Field:	Fisheries Sciences not elsewhere classified
Objective Division:	Animal Production and Animal Primary Products
Objective Group:	Fisheries - Aquaculture
Objective Field:	Aquaculture Oysters
Author:	Kow, F (Dr Felicia Kow)
ID Code:	95307
Year Published:	2014
Web of Science® Times Cited:	26
Deposited By:	NC Marine Conservation and Resource Sustainability
Deposited On:	2014-09-30
Last Modified:	2015-03-17
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