Abdelhedi Ola, Nasri Rim, Mora Letica, Jridi Mourad, Toldrá Fidel, Nasri Moncef
Laboratoire de Génie Enzymatique et de Microbiologie, Université de Sfax, Ecole Nationale d'Ingénieurs de Sfax, B.P. 1173-3038 Sfax, Tunisia.
Laboratoire de Génie Enzymatique et de Microbiologie, Université de Sfax, Ecole Nationale d'Ingénieurs de Sfax, B.P. 1173-3038 Sfax, Tunisia.
Food Chem. 2018 Jan 15;239:453-463. doi: 10.1016/j.foodchem.2017.06.112. Epub 2017 Jun 21.
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 ≤1kDa). Fractions showed different amino acid compositions and angiotensin I-converting enzyme (ACE) inhibitory potentials. The SHVH-P-FV (≤1kDa) and SHVH-N-FIV (3-1kDa) fractions showed the best ACE-inhibitory activities with IC values of 53.31 and 75.05µg/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.
用中性蛋白酶（SHVH-N）和Purafect（SHVH-P）处理制备光滑猎犬内脏水解物（SHVHs）。然后使用超滤膜系统根据其分子量将水解物分离成5个级分（≥50、50-5、5-3、3-1和≤1kDa）。这些级分显示出不同的氨基酸组成和血管紧张素I转换酶（ACE）抑制潜力。SHVH-P-FV（≤1kDa）和SHVH-N-FIV（3-1kDa）级分显示出最佳的ACE抑制活性，IC值分别为53.31和75.05μg/ml。根据它们较高的ACE抑制潜力，对FIV和FV进行反相高效液相色谱（RP-HPLC）分级分离，然后通过液相色谱-串联质谱（LC-MS/MS）分析以鉴定肽序列。一项系统的肽组学研究鉴定出了许多新序列。此外，基于分子对接模拟的计算机模拟数据表明，GPAGPRGPAG、AVVPPSDKM、TTMYPGIA和VKPLPQSG可以以低相互作用分数结合ACE活性位点。实际上，它们与ACE催化口袋共享氢键、范德华力和静电相互作用。
