期刊
JOURNAL OF FOOD SCIENCE
卷 76, 期 8, 页码 C1149-C1155出版社
WILEY-BLACKWELL
DOI: 10.1111/j.1750-3841.2011.02367.x
关键词
ACE-inhibitory activity; anticoagulation activity; DPPH radical-scavenging activity; egg white; peptide
资金
- Chinese 863 research program [2007AA10Z329]
A bioactive peptide Arg-Val-Pro-Ser-Leu (RVPSL) obtained from egg white protein was characterized by LC-MS and further chemically synthesized by the Fmoc solid phase method and investigated in terms of its angiotensin converting enzyme (ACE)-inhibitory activity, antioxidant property, and anticoagulation activity, as well as its stability in a simulated gastrointestinal digestion. The peptide exhibited an ACE-inhibitory activity with an IC50 value of 20 mu M. Also, the peptide could efficiently quench the (1,1)-diphenyl-2-picrylhydrazyl free radicals and exhibit high anticoagulation activity with a complete inhibition at 100 mM. Moreover, the peptide has a good stability against protease digestion. These results suggest that the peptide RVPSL may have potential to be used in nutraceuticals and functional food. Keywords: ACE-inhibitory activity, anticoagulation activity, DPPH radical-scavenging activity, egg white, peptide
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