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QIGLF, a novel angiotensin I‐converting enzyme‐inhibitory peptide from egg white protein
Author(s) -
Yu Zhipeng,
Zhao Wenzhu,
Liu Jingbo,
Lu Jing,
Chen Feng
Publication year - 2011
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.4266
Subject(s) - chemistry , circular dichroism , peptide , egg white , enzyme , chromatography , sephadex , tandem mass spectrometry , biochemistry , protease , protein secondary structure , proteolytic enzymes , mass spectrometry
BACKGROUND: Novel angiotensin I‐converting enzyme (ACE)‐inhibitory peptides from egg white protein can be rapidly screened by liquid chromatography/tandem mass spectrometry (LC/MS/MS). In this study, several peptides with higher ACE‐inhibitory activity were prepared from egg white protein by enzymatic hydrolysis with Alcalase, purified with Sephadex G25, identified by LC/MS/MS and their structure determined by circular dichroism (CD) spectroscopy. RESULTS: Peptide sequences DHPFLF, HAEIN and QIGLF that showed ACE‐inhibitory activity were investigated further for their stability in gastrointestinal solution and for changes in their secondary structure in solution mixtures. QIGLF exhibited the highest activity (IC 50 = 75 µmol L −1 ) and was resistant to digestion by proteases of the gastrointestinal tract. The CD spectrum of QIGLF showed the presence of the α‐helix conformation. CONCLUSION: Three peptides were identified by LC/MS/MS and synthesised by Fmoc solid phase synthesis. Of the three, only the peptide sequence QIGLF was a potential ACE inhibitor, with an IC 50 value of 75 µmol L −1 . Moreover, QIGLF showed low gastrointestinal enzyme susceptibility and contained a relatively high amount of α‐helix. Copyright © 2011 Society of Chemical Industry