PURIFICATION AND IDENTIFICATION OF ANTIOXIDANT PEPTIDES FROM GELATIN HYDROLYSATES OF UNICORN LEATHERJACKET SKIN

• Published in: Italian journal of food science Vol. 29; no. 1; p. 158
• Main Authors: Karnjanapratum, S, O'Callaghan, Y.C, Benjakul, S, O'Keeffe, M.B, Fitzgerald, R.J, O'Brien, N.M
• Format: Journal Article
• Language: English
• Published: Pinerolo Chiriotti Editori S.r.l 01.01.2017; Codon Publications
• Subjects: Amino acids; Anion exchanging; Antioxidants; Antioxidants (Nutrients); Biological activity; Cellulose; Chemical properties; Chromatography; Food; Functional foods & nutraceuticals; Gel filtration; Gelatin; Glycyl endopeptidase; High performance liquid chromatography; Hydrolysates; Identification and classification; Ions; Liquid chromatography; Mass spectrometry; Methods; Monacanthidae; Peptides; Physiological aspects; Protein purification; Proteins; Purification; Scavenging; Scientific imaging; Skin; Solvents
• ISSN: 1120-1770; 2239-5687
• DOI: 10.14674/1120-1770/ijfs.v588

Antioxidant peptides from a gelatin hydrolysate of unicorn leatherjacket skin prepared using a partially purified glycyl endopeptidase were purified using Sephadex G-25 gel filtration, DEAE-cellulose anion-exchange and reverse phase high-performance liquid chromatography. The fractions with the highest ABTS radical scavenging activity were analyzed using UPLC-ESI-MS/MS to identify the peptide sequences therein. Four of the identified peptides, Glu-Pro-Gly-Pro-Val-Gly (555.27 Da), Leu-Pro-Gly-Pro-Ala-Gly (511.29 Da), Leu-Asp-Gly-Pro-Val-Gly (557.30 Da) and Glu-Gly-Pro-Leu-Gly (472.24 Da), were subsequently synthesized. Glu-Gly-Pro-Leu-Gly exhibited the highest antioxidant activity (4.95 [micro]mol TE/g solid). Therefore, peptides from unicorn leatherjacket skin gelatin hydrolysate could be further employed as functional food ingredient. Keywords: gelatin hydrolysate, unicorn leatherjacket, antioxidant activity, identification, UPLC, mass spectrometry