FOOD SCIENCE ›› 2009, Vol. 30 ›› Issue (13): 13-17.doi: 10.7506/spkx1002-6630-200913001

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Isolation and Identification of Antioxidant Peptides from Hydrolyzed Grass Carp Protein

REN Jiao-yan1,ZHAO Mou-ming1,*,CUI Chun1,YOU Li-jun1,WANG Hai-yan2   

  1. 1. College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, China;
    2. Technology Centre, Shanghai Tobacco (Group) Corporation, Shanghai 200082, China
  • Received:2008-11-07 Revised:2009-01-16 Online:2009-07-01 Published:2010-12-29
  • Contact: ZHAO Mou-ming E-mail:femmzhao@scut.edu.cn

Abstract:

Through separation of grass carp protein hydrolysates (GCPHs) by ultrafiltration and consecutive chromatographic methods including ion exchange chromatography (IEC), high-speed counter-current chromatography (HSCCC), and gel filtration chromatography (GFC), a peptide fraction with the relative molecular mass ranging 873-3139 D was obtained, which had the strongest antioxidant activity (the lowest IC50 for scavenging superoxide anion radical) compared to other two peptide fractions having the relative molecular mass ranging 379-873 D and 222-379 D, respectively. Basic peptides from hydrolyzed grass carp protein demonstrated greater antioxidant activity than the acidic or the neutral ones, and hydrophobic peptides in the GCPHs presented higher activities than the hydrophilic ones. By means of online RP-HPLC/ESI-MS, the amino acid sequence of the peptide with the strongest antioxidant activity was confirmed as Pro-Ser-Lys-Tyr-Glu-Pro-Phe-Val, and its relative molecular mass was determined as 966.3 D.

Key words: grass carp, antioxidant peptides, isolation, amino acid sequence, electrospray ionization mass spectrometry

CLC Number: