Purification and biochemical characterization of antioxidant peptide from horse mackerel (Magalaspis cordyla) viscera protein.
Peptides
; 32(7): 1496-501, 2011 Jul.
Article
em En
| MEDLINE
| ID: mdl-21640151
ABSTRACT
In the present study, a peptide having high antioxidant properties was isolated from horse mackerel viscera protein, Magalaspis cordyla. In vitro gastrointestinal digestion was employed to obtain potential protein hydrolysate and was subjected to consecutive chromatographic methods using fast protein liquid chromatography (FPLC) connected to diethyl amino ethyl (DEAE) anion exchange column and Sephadex G-25 gel filtration column. The activity of the fractions was tested against DPPH and hydroxyl radicals and the isolated peptide showed 89.2 and 59.1 percentage of scavenging. The amino acid sequence of purified peptide was determined using ESI-MS/MS as Ala-Cys-Phe-Leu (518.5 Da), it exhibited high activity against polyunsaturated fatty acid (PUFA) peroxidation than that of natural antioxidant, α-tocopherol.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oligopeptídeos
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Picratos
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Hidrolisados de Proteína
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Compostos de Bifenilo
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Perciformes
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Vísceras
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Sequestradores de Radicais Livres
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Radical Hidroxila
Limite:
Animals
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article