PURIFICATION AND IDENTIFICATION OF ANTIOXIDANT PEPTIDES FROM GELATIN HYDROLYSATES OF UNICORN LEATHERJACKET SKIN
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 high...
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Published in | Italian journal of food science Vol. 29; no. 1; p. 158 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Pinerolo
Chiriotti Editori S.r.l
01.01.2017
Codon Publications |
Subjects | |
Online Access | Get full text |
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Summary: | 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 |
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ISSN: | 1120-1770 2239-5687 |
DOI: | 10.14674/1120-1770/ijfs.v588 |