In vitro and in silico evaluation of multifunctional properties of bioactive synthetic peptides identified in milk fermented with Lactococcus lactis NRRL B-50571 and NRRL B-50572

Abstract The aim of this study was to investigate the multifunctional properties of specific synthetic peptides previously identified in milk fermented with Lactococcus lactis NRRL B-50571 and NRRL B-50572 on the inhibition of enzymes involved in hypertension (ACE), type 2 diabetes (DPP-IV) and thrombosis (thrombin). Moreover, in vitro gastrointestinal digestion was performed in order to know the stability of peptides and its effect on the biological activities. Also, in silico analysis was employed for the prediction of sequences after digestion. Results showed that peptide inhibitory activities on ACE, DPP-IV and thrombin were enhanced after digestion. After in vitro digestion, peptide NAVPITPTLN showed the best efficiency to inhibit DPP-IV. Likewise, NAVPITPTLN and QEPVLGPVRGPFIIV showed high thrombin inhibitory activities, and HPHPHLSFMAIPP and SLPQNIPPL presented high ACE inhibitory activities. In vitro and in silico studies indicated that these peptides are precursors of multifunctional peptide sequences. Therefore, this study suggests that the specific synthetic peptides previously identified in milk fermented with Lactococcus lactis NRRL B-50571 and NRRL B-50572 offer potential beneficial health effects in the management of hypertension, thrombosis and diabetes.