Novel antioxidative peptides from the protein hydrolysate of oysters (Crassostrea talienwhanensis)

• Published in: Food chemistry 2014-02, Vol.145, p.991-996
• Main Authors: Wang, Qiukuan, Li, Wei, He, Yunhai, Ren, Dandan, Kow, Felicia, Song, Linlin, Yu, Xingju
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Antioxidants - analysis; Antioxidants - chemistry; Antioxidants - isolation & purification; Antioxidants - metabolism; Antioxidative peptide; Biological and medical sciences; China; Chromatography, Gel; Chromatography, High Pressure Liquid; Chromatography, Reverse-Phase; Crassostrea - chemistry; Crassostrea talienwhanensis; Dietary Proteins - analysis; Dietary Proteins - chemistry; Dietary Proteins - isolation & purification; Dietary Proteins - metabolism; Dietary Supplements; Food toxicology; Free Radical Scavengers - analysis; Free Radical Scavengers - chemistry; Free Radical Scavengers - isolation & purification; Free Radical Scavengers - metabolism; Hydrolysate; Hydroxyl Radical - antagonists & inhibitors; Medical sciences; Microchemistry; Oligopeptides - analysis; Oligopeptides - chemistry; Oligopeptides - isolation & purification; Oligopeptides - metabolism; Oyster Crassostrea talienwhanensis; Peptide Fragments - analysis; Peptide Fragments - chemistry; Peptide Fragments - isolation & purification; Peptide Fragments - metabolism; Protein Hydrolysates - chemistry; Protein Hydrolysates - metabolism; Radical scavenging activity; Shellfish - analysis; Spectrometry, Mass, Electrospray Ionization; Subtilisin; Subtilisin - metabolism; Tandem Mass Spectrometry; Toxicology
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2013.08.099

•Purified & identified novel antioxidative peptides from oyster protein hydrolysate.•The novel peptides are Pro-Val-Met-Gly-Asp and Gln-Hist-Gly-Val.•Novel technique nano-ESI-MS/MS applied to analyse the amino acid sequences.•Determined optimum protein hydrolytic reaction conditions using subtilisin.•Findings assist Chinese industry in utilizing cheap source of bioactive materials. 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 440Da) were proline-valine-methionine-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.