Whey protein isolate polydispersity affects enzymatic hydrolosis outcomes
AuthorO'Loughlin, Ian B.
Murray, Brian A.
Fitzgerald, Richard J.
Robinson, A. A.
Holton, T. A.
Kelly, Tom A.
MetadataShow full item record
StatisticsDisplay Item Statistics
CitationI.B. O’Loughlin, B.A. Murray, A. Brodkorb, R.J. FitzGerald, A.A. Robinson, T.A. Holton, P.M. Kelly. Whey protein isolate polydispersity affects enzymatic hydrolysis outcomes. Food Chemistry, 2013, 141(3), 2334-2342. DOI: 10.1016/j.foodchem.2013.05.056
AbstractThe effects of heat-induced denaturation of whey protein isolate (WPI) on the enzymatic breakdown of α-La, caseinomacropeptide (CMP), β-Lg A and β-Lg B were observed as hydrolysis proceeded to a 5% degree of hydrolysis (DH) in both unheated and heat-treated (80 °C, 10 min) WPI dispersions (100 g L−1). Hydrolysis of denatured WPI favoured the generation of higher levels of free essential amino acids; lysine, phenylalanine and arginine compared to the unheated substrate. LC–MS/MS identified 23 distinct peptides which were identified in the denatured WPI hydrolysate – the majority of which were derived from β-Lg. The mapping of the detected regions in α-La, β-Lg, and CMP enabled specific cleavage points to be associated with certain serine endo-protease activities. The outcomes of the study emphasise how a combined approach of substrate heat pre-treatment and enzymology may be used to influence proteolysis with attendant opportunities for targeting unique peptide production and amino acid release
FunderTeagasc Walsh Fellowship Programme; Enterprise Ireland