Journal
FOOD CHEMISTRY
Volume 119, Issue 1, Pages 226-234Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2009.06.015
Keywords
Rice endosperm protein (REP); Neutrase hydrolysate from rice endosperm protein (NHREP); Antioxidant peptides; Isolation and identification; MALDI-TOF/TOF MS/MS
Funding
- Program for New Century Excellent Talents in University [NCET-06-0488]
- 111 Project [1307029]
- Program for Changjiang Scholars and Innovative Research Team in University [PCSIRT0627]
- National Key Technology R&D Program in the 11th Five year Plan of China [2006BAD05A01]
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The defatted rice endosperm protein (REP) was, respectively, digested by five different protease treatments (Alcalase, Chymotrypsin, Neutrase, Papain and Flavorase), and Neutrase appears to be the most desirable for producing high quality antioxidant peptides from REP. Specially, the DPPH and hydroxyl radical scavenging activities of NHREP were higher than its superoxide radical scavenging activity, and the percentage inhibition of autooxidation of NHREP (80.09%) was similar to that of alpha-tocopherol (86.59%) on day 5. Furthermore, NHREP was purified consecutively, and the antioxidant peptides were identified to be Phe-Arg-Asp-Glu-His-Lys-Lys (FRDEHKK, 959.5 Da) and Lys-His-Asp-Arg-Gly-Asp-Glu-Phe (1002.5 Da) by MALDI-TOF/TOF MS/MS. Lastly, FRDEHKK was chemically synthesised. It significantly inhibited lipid peroxidation in an linoleic acid emulsion system more effectively than alpha-tocopherol, and enhanced the viability of t-BHP induced cytotoxicity up to 74.38% (for MRC-5) and 78.39% (for RAW264.7) at 80 mu g/ml. Conclusively, it was feasible to produce natural antioxidants from REP. (C) 2009 Elsevier Ltd. All rights reserved.
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