Impact of Gastrointestinal Digestion Simulation on the Formation of Angiotensin-I-Converting Enzyme Inhibitory (ACE-I) Peptides from Germinated Lamtoro Gung Flour

The germination of lamtoro gung has been shown to increase the angiotensin-I-converting enzyme inhibitory (ACE-I) activity in previous studies. The 48 h germinated flour had the highest ACE-I activity. Administration of the gastrointestinal digestion (GID) simulation with commercial enzymes was expected to increase the ACE-I activity. However, the GID simulation to increase ACE-I in the germinated lamtoro gung flour has not been found. Therefore, this study aimed to evaluate the GID simulation of ACE-I peptides in sprouted lamtoro gung flour. This study also identified and characterised the peptide with the ACE-I activity. The GID simulation was performed using commercial pepsin (pH 2) and pancreatin (pH 7.5). Both simulations occurred at 37 °C for 240 min. The degree of hydrolysis, peptide concentration, and ACE-I activity was analysed. Samples with the highest ACE-I activity were then fractionated and identified, to determine the peptide responsible for the ACE-I activity. The 180 min GID simulation in the test sample showed the highest ACE-I activity (89.70%). This result was supported by an increased degree of hydrolysis (DH) and peptide concentrations throughout the GID simulation. The <1 kDa peptide fraction had the highest inhibitory activity and had the most elevated peptide portion (54.69%). Peptide sequences containing crucial amino acids were found in the <1 kDa peptide fraction. PRPPKPP, PPPPPGARAP, and PFPPSNPPP had proline in the C and N terminal residues. The peptides obtained also had other biological activities, such as a DPP IV inhibitor, an alpha-glucosidase inhibitor, and antioxidative activity. Based on the toxicity prediction, those peptides are non-toxic and safe to consume.