Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7592633 | Food Chemistry | 2015 | 6 Pages |
Abstract
Multiple proteases were optimized to hydrolyze the rice residue protein (RRP) to produce novel antioxidant peptides. An antioxidant peptide fraction (RRPB3) with IC50 of 0.25Â mg/ml was purified from the RRP hydrolysate using membrane ultrafiltration followed by size exclusion chromatography and reversed-phase FPLC. RRPB3 was found to include four peptides (RRPB3 I-IV) and their amino acid sequences were RPNYTDA (835.9Â Da), TSQLLSDQ (891.0Â Da), TRTGDPFF (940.0Â Da) and NFHPQ (641.7Â Da), respectively. Furthermore, four peptides were chemically synthesized and their antioxidant activities were assessed by DPPH radical scavenging, ABTS radical scavenging assay and FRAP-Fe3+ reducing assay, respectively. Both RRPB3 I and III showed synergistic antioxidant activity compared to each of them used alone. All four synthetic peptides showed excellent stability against simulated gastrointestinal proteases. Therefore, the peptides isolated from RRP may be used as potential antioxidants in the food and drug industries.
Keywords
RRPDPPHBHTTPTZABTSFPLCFRAPOPA1,1-diphenyl-2-picrylhydrazyl2,4,6-tripyridyl-S-triazineo-PhthalaldehydeBasic Local Alignment Search ToolBlastferric reducing ability of plasmafast protein liquid chromatographySynthesisAntioxidant activitybutylated hydroxytoluenePeptideshigh-pressure liquid chromatographyHPLC
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Qiao-Juan Yan, Lin-Hua Huang, Qian Sun, Zheng-Qiang Jiang, Xia Wu,