Chang, Chang, et al. “High angiotensin I‐converting enzyme inhibitory activity, bioaccessibility and bioavailability of milk protein hydrolysate by commercial proteases formulated with Pseudomonas aeruginosa protease.” International Journal of Dairy Technology 76.3 (2023): 544-553. https://doi.org/10.1111/1471-0307.12959
Milk protein hydrolysate was optimally prepared by Protamex and PaproA (MP-PP) exhibiting excellent angiotensin I-converting enzyme (ACE) inhibitory activity (89.6%) at 0.5 mg/mL and protein recovery rate (79.0%). Meanwhile, MP-PP was stable for acid–base and heat treatments, and even presented 80.5% of ACE inhibitory activity after handling in gastrointestinal fluids. However, transepithelial transportation via Caco-2 cell monolayer lowered ACE inhibition of MP-PP. Following the fractionation of MP-PP, IESPPEI was identified as an outstanding ACE inhibitory peptide (IC50 of 6.4 μM), comparable with commercial VPP and IPP. Overall, MP-PP and IESPPEI are potential functional ingredients to develop antihypertensive products.