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The aim of the present study was in vitro assessment of ACE inhibition property of A1 and A2 cow milk casein digested with trypsin. Casein powder was reconstituted (1%, 3% and 5% concentration) and trypsin was added at 1:100 (E:S), hydrolysis was carried out for 6 h at 37 oC and samples were drawn at 2 h intervals from both A1 and A2 casein hydrolysates. Bioactive peptides are encrypted within parent protein and are inactive, upon hydrolysis it become biologically active and shows positive health impact. Both A1 and A2 casein hydrolysates manifested ACE inhibition, whereas improved activity was recorded with progress in time and degree of hydrolysis. The results stipulate that hypertension was partially control by ACE inhibitory properties of casein-derived peptides.

In vitro assessment of ACE inhibitory activity of A1 and A2 cow milk casein hydrolysate