| Autor: |
Arámburo-Gálvez JG; Nutrition Sciences Postgraduate Program, Faculty of Nutrition and Gastronomy Sciences, Autonomous University of Sinaloa, Culiacan 80019, Sinaloa, Mexico., Tinoco-Narez-Gil R; Nutrition Sciences Postgraduate Program, Faculty of Nutrition and Gastronomy Sciences, Autonomous University of Sinaloa, Culiacan 80019, Sinaloa, Mexico., Mora-Melgem JA; Nutrition Sciences Postgraduate Program, Faculty of Nutrition and Gastronomy Sciences, Autonomous University of Sinaloa, Culiacan 80019, Sinaloa, Mexico., Sánchez-Cárdenas CA; Integral Postgraduate Program in Biotechnology, Faculty of Chemical and Biological Sciences, Autonomous University of Sinaloa, Ciudad Universitaria, Culiacan 80010, Sinaloa, Mexico., Gracia-Valenzuela MH; Laboratory for the Research and Detection of Biological Agents and Contaminants (CONAHCYT National Laboratory, LANIBIOC), Yaqui Valley Technological Institute, National Technological Institute of Mexico, Bácum 85276, Sonora, Mexico., Flores-Mendoza LK; Clinical and Research Laboratory (LACIUS, C.N., CONAHCYT National Laboratory, LANIBIOC), Deparment of Chemical, Biological, and Agricultural Sciences (DC-QB), Faculty of Biological and Health Sciences, University of Sonora, Navojoa 85880, Sonora, Mexico., Figueroa-Salcido OG; Integral Postgraduate Program in Biotechnology, Faculty of Chemical and Biological Sciences, Autonomous University of Sinaloa, Ciudad Universitaria, Culiacan 80010, Sinaloa, Mexico., Ontiveros N; Clinical and Research Laboratory (LACIUS, C.N., CONAHCYT National Laboratory, LANIBIOC), Deparment of Chemical, Biological, and Agricultural Sciences (DC-QB), Faculty of Biological and Health Sciences, University of Sonora, Navojoa 85880, Sonora, Mexico. |
| Abstrakt: |
Lupin ( Lupinus angustifolius L.) proteins are potential sources of bioactive peptides (LBPs) that can inhibit dipeptidyl peptidase IV (DPP-IV) and angiotensin I-converting enzyme (ACE-I) activity. However, the capacity of different enzymes to release LBPs, the pharmacokinetic and bioactivities of the peptides released, and their binding affinities with the active sites of DPP-IV and ECA-I are topics scarcely addressed. Therefore, we used in silico hydrolysis (BIOPEP-UWM platform) with various enzymes to predict the release of LBPs. Among the bioactive peptides identified in lupin proteins (n = 4813), 2062 and 1558 had DPP-IV and ACE-I inhibitory activity, respectively. Ficin, bromelain, and papain released the highest proportion of ACE-I (n = 433, 411, and 379, respectively) and DPP-IV (n = 556, 544, and 596, respectively) inhibitory peptides. LBPs with favorable pharmacokinetics and gastrointestinal stability tightly interacted with the active sites of ACE-I (-5.6 to -8.9 kcal/mol) and DPP-IV (-5.4 to -7.6 kcal/mol). Papain generated the most bioavailable LBPs (n = 459) with ACE-I (n = 223) and DPP-IV (n = 412) inhibitory activity. These peptides were non-toxic and gastrointestinal digestion stable. Notably, papain-based hydrolysis released some LBPs (n = 270) that inhibited both ACE-I and DPP-IV. Plant protease-based hydrolysis is a promising approach for producing lupin hydrolysates with ACE-I and DPP-IV inhibitory activities. |
