Purification and characterization of antioxidative peptides derived from rice bran protein hydrolysates

Abayomi Peter Adebiyi, Ayobamitale O. Adebiyi, Junko Yamashita, Tomohisa Ogawa, Koji Muramoto

Research output: Contribution to journalArticlepeer-review

85 Citations (Scopus)


Rice bran protein fraction (RBPF)-albumin, globulin, glutelin and prolamin were hydrolyzed with proteases M, N, P, S and pepsin under their optimal conditions for 24 h. Hydrolysates of various hydrolysis periods were collected and subjected to peptide mapping and the antioxidative activity measured by the 2,2-Azino-bis-3-ethylbenzothiazoline-6-sulfonic Acid (ABTS) method. Protease M hydrolysates showed high degree of hydrolysis (DH), but low antioxidative activity. On the contrary, pepsin hydrolysates showed low DH with high activity. Albumin and globulin hydrolysates had higher DH values, but lower values for glutelin and prolamin. The globulin hydrolysate (Opep2) from 2 h-pepsin hydrolysis was separated by using three consecutive purification steps with RP-HPLC. Nineteen antioxidative peptides were isolated and their amino acid sequences were determined by a gas-phase protein sequencer and MALDI-TOF mass spectrometry. These peptides were composed of 6-30 amino acid residues with molecular masses ranging from 670-3,611 Da. Tyr-Leu-Ala-Gly-Met-Asn had the highest antioxidative activity among them.

Original languageEnglish
Pages (from-to)553-563
Number of pages11
JournalEuropean Food Research and Technology
Issue number4
Publication statusPublished - 2009 Feb


  • Amino acid sequence
  • Antioxidative peptides
  • Proteases
  • Rice bran protein


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