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Novel antioxidative peptides from the protein hydrolysate of oysters (Crassostrea talienwhanensis)
journal contribution
posted on 2023-05-18, 03:51 authored by Wang, Q, Li, W, He, Y, Ren, D, Kow, F, Song, L, Yu, XThe 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.
History
Publication title
Food ChemistryVolume
145Pagination
991-996ISSN
0308-8146Department/School
Institute for Marine and Antarctic StudiesPublisher
Elsevier Sci LtdPlace of publication
The Boulevard, Langford Lane, Kidlington, Oxford, England, Oxon, Ox5 1GbRights statement
Copyright 2014 ElsevierRepository Status
- Restricted