Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790.

Casein hydrolysate, produced by an extracellular proteinase from Lactobacillus helveticus CP790, was fractionated by two-step reverse-phase HPLC. Only one fraction showed antihypertensive activity as measured by systolic blood pressure in spontaneously hypertensive rats after oral administration. Ten peptides in the fraction were further purified and identified by analysis of amino acid sequences. Each identified peptide was chemically synthesized, and the antihypertensive activity of each peptide was evaluated in spontaneously hypertensive rats. The synthetic peptide with a sequence of Lys-Val-Leu-Pro-Val-Pro-Gln, found in beta-casein, indicated strong antihypertensive activity from 2 to 10 h after oral administration of 2 mg of peptide/kg of BW, and the effect was maximal at 6 h after oral administration (-31.5 +/- 5.6 mm Hg). Moreover, the antihypertensive effect of the peptide was dependent on the dosage of peptide from 0.5 to 2 mg of peptide/kg of BW. Interestingly, the antihypertensive peptide showed lower inhibitory activity of angiotensin I-converting enzyme, but the activity was increased after pancreatin digestion.