Purification and characterization of angiotensin-I-converting enzyme inhibitory peptides isolated from whey proteins of milk fermented with Lactobacillus plantarum QS670

Abstract

An angiotensin-converting enzyme inhibitory (ACEI) peptide with a median inhibitory concentration (IC50) of 1.26 mg/mL was purified from whey proteins resulting from a fermentation using Lactobacillus plantarum QS670. The peptide was subsequently derived from an αS1-casein, κ-casein, β-lactoglobulin, or serum albumin fraction. Analysis via liquid chromatography tandem mass spectrometry indicated that it had an amino acid sequence of Gly-Ala (GA). The GA dipeptide was also synthesized using an Fmoc solid-phase method. The GA dipeptide exhibited an IC50 of 1.22 mg/mL and was shown to be stable across both temperature (20 to 60°C) and pH (2 to 12). Digestive enzymes including pepsin, trypsin, and chymotrypsin had negligible effects on activity. The whey exerted hypotensive effects when fed to spontaneously hypertensive rats (SHR), which exhibited a blood pressure drop of 2.33 kPa. A 4-wk gavage treatment resulted in greater decreases of 7.46 kPa. Results of this study indicate that milk fermented using Lb. plantarum QS306 has potential to be used as a functional food to help prevent or reduce hypertension-associated diseases.