Lysine blockage of milk proteins in infant formula impairs overall protein digestibility and peptide release

Abstract

High levels of blocked lysine in infant formula lead to increasing average peptide length after in vitro digestion in infants.

Modification of protein structures by altering the whey protein profile and heat treatment affectsin vitrostatic digestion of model infant milk formulas

“…14 It is now acknowledged that the milk protein structures can influence nutrient bioavailability, rates of absorption and postprandial outcomes. [15][16][17][18][19] Milk protein structure can be altered by processing such as heat treatment, partly due to whey protein denaturation and aggregation. However, so far, only a few studies 20,21 have directly linked these heat-induced protein structures to protein digestion kinetics, and even less in the context of IMFs.…”

Milk Processing Affects Structure, Bioavailability and Immunogenicity of β-lactoglobulin

“…It was indeed experimentally validated that lysine modification impairs susceptibility of proteins to enzymatic digestion (reviewed in [ 173 , 183 , 184 , 185 , 186 , 187 , 188 , 189 ]). Various mechanisms to explain impaired digestion have been suggested, including direct protection of lysine as a proteolytic target site, prevention of docking of proteolytic enzymes as a result of a modified lysine residue located immediately adjacent to an intended cleavage site, or by means of cross-linking with target residues [ 190 ].…”

Enhanced Uptake of Processed Bovine β‐Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity

“…Whereas, unfolding prior to aggregation in the presence and absence of reducing sugars can facilitate enzymatic hydrolysis, it has been shown that high levels of glycation in infant formula results in impaired digestibility. [ 22 ] Thus, exploring the molecular mechanisms of interaction between heat‐treated BLG, as a potential antigen present in infant nutrition, and the human APCs is of particular interest. The aim of the present study was first to evaluate and compare heat and glycation induced changes in immunoreactivity of BLG.…”