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|Title: ||Whey protein isolate polydispersity affects enzymatic hydrolosis outcomes|
|Authors: ||O'Loughlin, Ian B.|
Murray, Brian A.
Fitzgerald, Richard J.
Robinson, A. A.
Holton, T. A.
Kelly, Tom A.
Whey protein isolate
Essential amino acids
|Issue Date: ||24-May-2013|
|Citation: ||I.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|
|Series/Report no.: ||Food Chemistry;vol 141(3)|
|Abstract: ||The 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|
The work herein was funded by Enterprise Ireland (EI) as part of the Food for Health Ireland project. I. B. O’Loughlin is a Teagasc Walsh Fellow supported by EI grant number CC/2008/0001/A.
|Appears in Collections:||Food Chemistry & Technology|
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