Purification and characterization of antioxidative peptides derived from rice bran protein hydrolysates
2009
Adebiyi, Abayomi Peter | Adebiyi, Ayobamitale O. | Yamashita, Junko | Ogawa, Tomohisa | Muramoto, Koji
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.
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