TY - JOUR
T1 - Purification and characterization of antioxidative peptides derived from rice bran protein hydrolysates
AU - Adebiyi, Abayomi Peter
AU - Adebiyi, Ayobamitale O.
AU - Yamashita, Junko
AU - Ogawa, Tomohisa
AU - Muramoto, Koji
N1 - Funding Information:
Acknowledgments This work was supported by the funds of The Iij-ima Memorial Foundation. APA gratefully acknowledges the Japanese Ministry of Education, Culture, Science and Technology for granting him scholarship to undergo his study in Japan.
Copyright:
Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2009/2
Y1 - 2009/2
N2 - 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.
AB - 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.
KW - Amino acid sequence
KW - Antioxidative peptides
KW - Proteases
KW - Rice bran protein
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U2 - 10.1007/s00217-008-0962-3
DO - 10.1007/s00217-008-0962-3
M3 - Article
AN - SCOPUS:58849118402
VL - 228
SP - 553
EP - 563
JO - European Food Research and Technology
JF - European Food Research and Technology
SN - 1438-2377
IS - 4
ER -