Peptide profile and angiotensin-converting enzyme inhibitory activity of Prato cheese with salt reduction and Lactobacillus helveticus as an adjunct culture.

Among strategies to improve the health-related aspects of dairy products, great prominence has been given to salt reduction and the use of adjunct cultures that can favor the release of bioactive peptides during cheese ripening. This study aimed to evaluate the effect of the salt reduction, the addition of Lactobacillus helveticus LH-B02 and the ripening time of Prato cheese on the casein hydrolysis profile by capillary electrophoresis, peptide profile by mass spectrometry, and antihypertensive potential evaluated in vitro through the inhibitory activity of the angiotensin-converting enzyme (ACE). Both the salt reduction and the addition of adjunct culture favored the accumulation of the bioactive peptide β-CN (f193-209) (m/z 1881). The adjunct culture led to a higher ACE inhibitory activity during the ripening of Prato cheese, thus proving to be an effective strategy for the development of potentially bioactive cheese.