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

被引：0
|
作者：
Karnjanapratum, S. [1 ]
O'Callaghan, Y. C. [2 ]
Benjakul, S. [1 ]
O'Keeffe, M. B. [3 ]
Fitzgerald, R. J. [3 ]
O'Brien, N. M. [2 ]
机构：
[1] Prince Songkla Univ, Fac Agroind, Dept Food Technol, Hat Yai 90112, Songkhla, Thailand
[2] Univ Coll Cork, Sch Food & Nutr Sci, Cork, Ireland
[3] Univ Limerick, Dept Life Sci, Limerick, Ireland
来源：
ITALIAN JOURNAL OF FOOD SCIENCE | 2017年 / 29卷 / 01期
关键词：
gelatin hydrolysate; unicorn leatherjacket; antioxidant activity; identification; UPLC; mass spectrometry; INHIBITORY PEPTIDES; BIOACTIVE PEPTIDES; PROTEIN; AUTOLYSIS; SEQUENCES; EXTRACT;
D O I：
暂无
中图分类号：
TS2 [食品工业];
学科分类号：
0832 ;
摘要：
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 mu mol TE/g solid). Therefore, peptides from unicorn leatherjacket skin gelatin hydrolysate could be further employed as functional food ingredient.
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页码：158 / 170
页数：13
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