Structural Analysis of Antioxidative Peptides from Soybean β-Conglycinin

Hua Ming Chen, Koji Muramoto, Fumio Yamauchi

    Research output: Contribution to journalArticlepeer-review

    513 Citations (Scopus)


    Protease hydrolyses of a soybean protein, β-conglycinin (7S protein), yielded antioxidative activity against the peroxidation of linoleic acid in an aqueous system at pH 7.0. Six antioxidative peptides were isolated from the hydrolysate prepared with protease S by size exclusion chromatography and reversed-phase HPLC. The amino acid sequences of the peptides were determined using a gasphase protein sequencer and electron spray mass spectrometry. The peptides were composed of 5–16 amino acid residues, including hydrophobic amino acids, valine or leucine, at the N-terminal positions, and proline, histidine, or tyrosine in the sequences.

    Original languageEnglish
    Pages (from-to)574-578
    Number of pages5
    JournalJournal of Agricultural and Food Chemistry
    Issue number3
    Publication statusPublished - 1995 Mar 1


    • Antioxidative peptide
    • soybean protein
    • β-conglycinin

    ASJC Scopus subject areas

    • Chemistry(all)
    • Agricultural and Biological Sciences(all)


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