Abstract
Peptides having potent antioxidant activity were separated from the hydrolysate of wheat gluten by ion-exchange and gel filtration chromatography. Peptides obtained by SP Sephadex C-25 chromatography of the most active fraction (WP-3) were further separated using reversed-phase high performance liquid chromatography. The amino acid sequences of these peptides were Leu-Gln-Pro-Gly-Gln-Gly-Gln-Gln-Gly and Ala-Gln-Ile-Pro-Gln-Gln.
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