Purification and characterization of three antioxidant peptides from protein hydrolyzate of croceine croaker (Pseudosciaena crocea) muscle

Food Chem. 2015 Feb 1:168:662-7. doi: 10.1016/j.foodchem.2014.07.117. Epub 2014 Aug 5.

Abstract

Three antioxidant peptides were purified from protein hydrolysate of croceine croaker (Pseudosciaena crocea) muscle prepared using pepsin and alcalase, and identified as Tyr-Leu-Met-Ser-Arg (PC-1), Val-Leu-Tyr-Glu-Glu (PC-2), and Met-Ile-Leu-Met-Arg (PC-3) with molecular weights of 651.77, 668.82, and 662.92Da, respectively. PC-1 exhibited the highest scavenging activities on DPPH (EC50 1.35mg/ml), superoxide (EC50 0.450mg/ml), and ABTS (EC50 0.312mg/ml) radicals, but PC-2 exhibited the strongest hydroxyl radical scavenging activity (EC50 0.353mg/ml) among the three peptides. PC-1 also showed effective inhibition on lipid peroxidation in the model system. The good activities of isolated peptides might be benefit from the smaller size and hydrophobic and/or aromatic amino acids within their sequences.

Keywords: Antioxidant activity; Croceine croaker (Pseudosciaena crocea); Peptide; Protein hydrolysate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antioxidants / analysis
  • Antioxidants / chemistry*
  • Antioxidants / isolation & purification
  • Lipid Peroxidation
  • Mass Spectrometry
  • Muscles / chemistry
  • Muscles / metabolism*
  • Pepsin A / metabolism
  • Peptides / analysis
  • Peptides / chemistry*
  • Peptides / isolation & purification
  • Perciformes / metabolism*
  • Proteins / chemistry
  • Proteins / metabolism
  • Subtilisins / metabolism

Substances

  • Antioxidants
  • Peptides
  • Proteins
  • Subtilisins
  • Pepsin A