Description
The hydrolysis of bovine whey protein concentrate (WPC), a-lactalbumin (a-La) and caseinomacropeptide (CMP), by aqueous extracts of Cynara cardunculus, was optimized using response surface methodology.
Degree of hydrolysis (DH), angiotensin-converting enzyme (ACE)-inhibitory activity and antioxidant activity were used as objective functions, and hydrolysis time and enzyme/substrate ratio as manipulated
parameters. The model was statistically appropriate to describe ACE-inhibitory activity of hydrolysates from WPC and a-La, but not from CMP.Maximum DH was 18% and 9%, for WPC and a-La, respectively. 50%
ACE-inhibitionwas produced by 105.4 (total fraction) and 25.6 mgmL-1 (<3 kDa fraction) for WPC, and 47.6 (total fraction) and 22.5 mgmL-1 (<3 kDa fraction) for a-La. Major peptides of fractions exhibiting ACEinhibition were sequenced. The antioxidant activities of WPC and a-La were 0.96 +/- 0.08 and 1.12 +/- 0.13 mmol trolox equivalent per mg hydrolysed protein, respectively.
; Contreras, M. M. 
