作者: JingBo Liu , ZhiPeng Yu , WenZhu Zhao , SongYi Lin , ErLei Wang
DOI: 10.1016/J.FOODCHEM.2010.03.108
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摘要: Abstract The aim of this study was to identify potential angiotensin I-converting enzyme (ACE) inhibitory peptide from egg white protein. protein hydrolysed by Alcalase and the hydrolysates were isolated with Gel filtration get high activity fraction. fraction identified LC tandem mass spectrometric 4000 Q Trap MS. In current work, 19 peptides discovered in fractions, five which sourced ovotransferrin synthesised Fmoc solid phase method. ACE-inhibitory measured HPLC assay. 50% concentrations Arg–Val–Pro–Ser–Leu (RVPSL) 20 μM. Based on remarkable activity, it is suggested that RVPSL may have applications as a functional food, could be used nutraceutical compounds.