Optimisation, by response surface methodology, of degree of hydrolysis and antioxidant and ACE-inhibitory activities of whey protein hydrolysates obtained with cardoon extract

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Abstract

The hydrolysis of bovine whey protein concentrate (WPC), alpha-lactalbumin (alpha-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 alpha-La, but not from CMP. Maximum DH was 18% and 9%, for WPC and alpha-La, respectively. 50% ACE-inhibition was produced by 105.4 (total fraction) and 25.6 mu g mL(-1) (<3 kDa fraction) for WPC, and 47.6 (total fraction) and 22.5 mu g mL(-1) (<3 kDa fraction) for alpha-La. Major peptides of fractions exhibiting ACE-inhibition were sequenced. The antioxidant activities of WPC and alpha-La were 0.96 +/- 0.08 and 1.12 +/- 0.13 mmol trolox equivalent per mg hydrolysed protein, respectively.
Original languageUnknown
Pages (from-to)926-933
JournalInternational Dairy Journal
Volume21
Issue number12
DOIs
Publication statusPublished - 1 Jan 2011

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