Peptide profiles and angiotensin-I-converting enzyme inhibitory activity of fermented milk products: Effect of bacterial strain, fermentation pH, and storage time

Abstract

Milk was fermented to defined pH values with 13 strains of lactic acid bacteria. The products were evaluated after 1 and 7 days of cold storage, and major peptides in selected products were identified. The Streptococcus thermophilus and Lactobacillus acidophilus strains used did not give rise to products with significant angiotensin-1-converting enzyme (ACE)-inhibition. The four Lactococcus lactis strains behaved similarly in fermentation, proteolysis and ACE-inhibition. The products made with the seven Lactobacillus helveticus strains varied. The highest ACE-inhibitory activity was obtained with two highly proteolytic strains of Lb. helveticus and with the Lactococcus strains. Fermentation from pH 4.6 to 4.3 with these strains slightly increased the ACE-inhibitory activity, whilst fermentation to pH 3.5 with Lb. helveticus reduced the ACE-inhibitory activity. Cold storage dramatically increased the ACE-inhibitory activity of some products. A non-linear correlation was found between peptide amount and ACE-inhibitory activity, and peptides contributing to the ACE-inhibitory activity were identified.