TitleIsolation and identification of antioxidant peptides from enzymatically hydrolyzed rice bran protein.
Publication TypeJournal Article
Year of Publication2016
AuthorsWattanasiritham L, Theerakulkait C, Wickramasekara S, Maier CS, Stevens JF
JournalFood Chem
Date Published2016 Feb 01
KeywordsAntioxidants, Chromatography, High Pressure Liquid, Hydrolysis, Oryza, Oxidation-Reduction, Peptides, Plant Extracts, Plant Proteins, Protein Hydrolysates, Spectrometry, Mass, Electrospray Ionization, Trypsin

Khao Dawk Mali 105 rice bran protein (RBP) was fractionated into albumin (12.5%), globulin (13.9%), glutelin (70.8%) and prolamine (2.9%). The native and denatured RBP fractions were hydrolyzed with papain and trypsin for 3h at optimum conditions. The RBP fractions and their hydrolysates were evaluated for their antioxidant activity by the Oxygen Radical Absorbance Capacity (ORAC) assay. The trypsin-hydrolyzed denatured albumin exhibited the highest antioxidant activity with an ORAC value of 4.07 μmol of Trolox equivalent (TE)/mg protein. This hydrolysate was separated by using RP-HPLC and three fractions with high antioxidant activity were examined by LTQ-FTICR ESI mass spectrometry. The MW of the peptides from these fractions were 800-2100 Da. and consisted of 6-21 amino acid residues. Most of the peptides from the fractions demonstrated typical characteristics of well-known antioxidant peptides. The results suggest that trypsin-hydrolyzed denatured rice bran albumin might be useful as a natural food antioxidant.

Alternate JournalFood Chem
PubMed ID26304333
Grant ListP30 ES000210 / ES / NIEHS NIH HHS / United States
P30ES000210 / ES / NIEHS NIH HHS / United States