Journal
FOOD CHEMISTRY
Volume 203, Issue -, Pages 367-374Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2016.02.097
Keywords
ACE-I inhibition; In silico; Barley proteins; Peptides; IC50; Mass spectrometry
Funding
- NutriCerealIreland project - Food Institutional Research Measure of the Irish Department of Agriculture, Food and Marine [FIRM 11/SF/317]
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Angiotensin-I-converting enzyme (ACE-I) plays a key role in control of hypertension, and type-2 diabetes mellitus, which frequently co-exist. Our current work utilised in silico methodologies and peptide databases as tools for predicting release of ACE-I inhibitory peptides from barley proteins. Papain was the enzyme of choice, based on in silico analysis, for experimental hydrolysis of barley protein concentrate, which was performed at the enzyme's optimum conditions (60 degrees C, pH 6.0) for 24 h. The generated hydrolysate was subjected to molecular weight cut-off (MWCO) filtration, following which the non-ultrafiltered hydrolysate (NUFH), and the generated 3 kDa and 10 kDa MWCO filtrates were assessed for their in vitro ACE-I inhibitory activities. The 3 kDa filtrate (1 mg/ml), that demonstrated highest ACE-I inhibitory activity of 70.37%, was characterised in terms of its peptidic composition using mass spectrometry and 1882 peptides derived from 61 barley proteins were identified, amongst which 15 peptides were selected for chemical synthesis based on their predicted ACE-I inhibitory properties. Of the synthesized peptides, FQLPKF and GFPTLKIF were most potent, demonstrating ACE-I IC50 values of 28.2 mu M and 41.2 mu M respectively. (C) 2016 Elsevier Ltd. All rights reserved.
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