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• W2103608064 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." @default.
• W2103608064 created "2016-06-24" @default.
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• W2103608064 date "2013-12-01" @default.
• W2103608064 modified "2023-10-18" @default.
• W2103608064 title "Whey protein isolate polydispersity affects enzymatic hydrolysis outcomes" @default.
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• W2103608064 doi "https://doi.org/10.1016/j.foodchem.2013.05.056" @default.
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