Highly proteolytic bacteria from semi-ripened chiapas cheese elicit angiotensin-I converting enzyme inhibition and antioxidant activity

Chiapas cream cheese (CCH) manufacturing process involves a long acid-enzymatic coagulation period of full-fat cow raw milk to achieve an acid and crumbly cheese. These sensorial aspects are related to lactic acid bacteria activity during ripening. Our main objective was to test the hypothesis that CCH contained highly proteolytic strains able to release bioactive compounds upon milk-protein hydrolysis. First, the proteolysis of CCH was evaluated considering the peptide and amino acid profiles of cheese samples collected from Veracruz (AVCH) and Tabasco (HTCH). The angiotensin-converting-enzyme (ACE) inhibitory activity in cheese water-soluble fractions was evaluated. Thereafter, strains from both CCH samples were isolated and selected based on their proteolytic capability, genetic fingerprint differentiation and growth conditions. Finally, a range of activities in vitro were tested in milk fractions fermented with selected strains. CCH showed ACE inhibitory activity: IC50 = 1.75–2.75 mg/mL. Interestingly, AVCH contains 0.78 g/kg of the antihypertensive γ-aminobutyric acid. Three highly proteolytic strains showed ACE and high antioxidant activities upon milk fermentation. In conclusion, CCH contain proteolytic strains able to release bioactive compounds from milk proteins and potentially useful to produce functional ingredients and foods.