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

• Type: Article in International Scientific Journal
• Date: 2011

Authors

Tavares, TG (Author) Other; Contreras, MM (Author) Other; Amorim, M (Author) Other; Martin Alvarez, PJ (Author) Other; Pintado, ME (Author) Other; Recio, I (Author) Other; F. Xavier Malcata (Author) Other

Journal

Title: International Dairy Journal

Vol. 21 No. 3

Pages: 926-933

ISSN: 0958-6946

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 44 Citations

Scopus - 55 Citations

Other information

Authenticus ID: P-002-JFB

DOI: 10.1016/j.idairyj.2011.05.013

Abstract (EN): 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. (c) 2011 Published by Elsevier Ltd.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 8