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

Main Article Content

S. Karnjanapratum
S. Benjakul
Y. C. O'Callaghan
M. B. O'Keeffe
R. J. FitzGerald
N. M. O'Brien

Keywords

Gelatin hydrolysate, Unicorn leatherjacket, Antioxidant activity, Identification, UPLC, mass spectrometry

Abstract

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 µmol TE/g solid). Therefore, peptides from unicorn leatherjacket skin gelatin hydrolysate could be further employed as functional food ingredient.

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