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Purification and characterisation of antioxidative peptides from unfractionated rice bran protein hydrolysates
Author(s) -
Adebiyi Abayomi P.,
Adebiyi Ayobamitale O.,
Ogawa Tomohisa,
Muramoto Koji
Publication year - 2008
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.2006.01379.x
Subject(s) - hydrolysate , chemistry , chromatography , bran , hydrolysis , protease , phytic acid , biochemistry , enzyme , organic chemistry , raw material
Summary Crude rice bran protein (CRBP) was prepared by alkaline extraction and then treated with 0.6 m HCl to remove phytic acid. The phytate‐free rice bran protein (PFRBP) was hydrolysed with proteases M, N, S, P and pepsin under optimal conditions. Hydrolysates obtained from various hydrolysis periods were subjected to analysis for their degree of hydrolysis (DH) and functional properties. The hydrolysates were fractionated by reversed‐phase column chromatography on Kaseigel ODS resin (120–140 μ m) using a stepwise gradient of aqueous ethanol, and their activities were measured. The 40% ethanol fraction of protease P 4 h‐hydrolysate was separated by successive reversed‐phase high‐performance liquid chromatography and the amino acid sequences of isolated antioxidative peptides were determined by a protein sequencer and matrix‐assisted laser desorption ionisation‐time of flight mass spectrometry. Crude rice bran protein had higher antioxidative activity than PFRBP, due to the presence of phytic acid. Phytate contents of rice bran, CRBP and PFRBP were 2.5%, 1.42% and 0%, respectively. The activity of PFRBP increased upon protease digestion. Protease M hydrolysates showed the highest DH, but the lowest antioxidative activity. Hydrolysates with DH below 10% had higher antioxidative activity than those above 20%. This result indicates that the antioxidative activity of the hydrolysates is inherent to their characteristics amino acid sequences of peptides depending on the protease specificities.