Optimisation, by response surface methodology, of degree of hydrolysis and anti...

• Autor(es): Tavares, T. G. ; Contreras, M. M. ; Amorim, M. ; Martín-Álvarez, P. J. ; Pintado, M. E. ; Recio, I. ; Malcata, F. X.
• Data: 2011
• Identificador Persistente: http://hdl.handle.net/10400.14/7964
• Origem: Veritati - Repositório Institucional da Universidade Católica Portuguesa
• Tipo de Documento: Artigo
• Idioma: Inglês

Descrição

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.