Journal
FOOD CHEMISTRY
Volume 239, Issue -, Pages 453-463Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2017.06.112
Keywords
In silico screening; Smooth-hound viscera; ACE-inhibitory peptides; Ultra-filtration; Molecular docking
Funding
- Ministry of Higher Education and Scientific Research, Tunisia
- Generalitat Valenciana in Spain [GV/2015/138]
- JAEDOC-CSIC
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Smooth-hound viscera hydrolysates (SHVHs) were prepared by treatment with Neutrase (SHVH-N) and Purafect (SHVH-P). Hydrolysates were then separated according to their molecular weight, using the ultra-filtration membrane system, into 5 fractions (>= 50, 50-5, 5-3, 3-1 and <= 1 kDa). Fractions showed different amino acid compositions and angiotensin I-converting enzyme (ACE) inhibitory potentials. The SHVH-P-FV (<= 1 kDa) and SHVH-N-FIV (3-1 kDa) fractions showed the best ACE-inhibitory activities with IC50 values of 53.31 and 75.05 mu g/ml, respectively. According to their high ACE-inhibitory potential, FIV and FV were fractionated by RP-HPLC and then analyzed by LC-MS/MS to identify peptide sequences. A systematic peptidomic study resulted in the identification of numerous novel sequences. Furthermore, in silico data, based on the molecular docking simulation, showed that GPAGPRGPAG, AVVPPSDKM, TTMYPGIA, and VKPLPQSG could bind ACE active site with low interaction scores. Indeed, they share hydrogen bonds and Van der Waals and electrostatic interactions with ACE catalytic pockets. (C) 2017 Elsevier Ltd. All rights reserved.
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