Purification and structure characterization of a novel wheat gluten peptide D-WG-0-I
Based on antioxidant acitivity evualuation,a peptide D-WG-0-Ⅰ was separated and purified by Sephadex G25 column chromatography from enzymatic hydrolate of wheat gluten.The purity of D-WG-0-Ⅰ was determined as 84% with RT-HPLC.UV,IR and MALDI-TOF/TOF MS/MS spectroscopy analysis revealed that the antioxidant peptide D-WG-0-Ⅰ had the molecular weight of 1746.89 u and the amino acid sequence of Ser-Gly-Ala-Asp-Lys-Lys-pro-Ile-Lys-Ala-Asn-His.The obtained results showed that D-WG-0-Ⅰ was a novel antioxidant peptide obtained from wheat gluten.