Purification and characterization of three antioxidant peptides from protein hydrolyzate of croceine croaker (Pseudosciaena crocea) muscle.
Food Chem
; 168: 662-7, 2015 Feb 01.
Article
em En
| MEDLINE
| ID: mdl-25172761
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
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Perciformes
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Músculos
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Antioxidantes
Limite:
Animals
Idioma:
En
Revista:
Food Chem
Ano de publicação:
2015
Tipo de documento:
Article