Abstract
The ability of proteolytic Lactobacillus strains to hydrolyze milk proteins to release angiotensin I-converting enzyme inhibitory peptides was evaluated. The peptide profiles were obtained from the 3 and 5 kDa water-soluble extract (WSE) and subsequently separated by reversed-phase high performance liquid chromatography. WSE of fermented milks supplemented with different levels of WPC70 and Calcium caseinate (1.0, 1.5, or 2.0%) were passed through 3 and 5 kDa ultra cutoff membrane for optimization of peptides production. WSE of permeates and retentates were analyzed for peptides production and angiotensin-converting enzyme inhibitory activity. Peptides production and angiotensin-converting enzyme inhibitory activity were maximum at 1.0% WPC70 for Lactobacillus helveticus (V3), 1.5% WPC70 for Lactobacillus rhamnosus (NS4), and (NS6) or 2.0% Calcium caseinate for V3, NS4, and NS6 cultures. However, Lactobacillus strains were capable in hydrolyzing milk proteins to generate potent angiotensin I-converting enzyme inhibitory peptides and could be used to prepare fermented milks with antihypertensive activity.
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