Maillard induced aggregation of individual milk proteins and interactions involved

Cardoso, Hugo B.; Wierenga, Peter A.; Gruppen, Harry; Schols, Henk A.

doi:10.1016/j.foodchem.2018.10.061

Cited by 24 publications

(19 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The formation of disulphide bonds is promoted by the presence of reducing sugars and low water activity during the heating process. 38,39 Peptide size distribution…”

Section: Peptide Formation and Average Peptide Lengthmentioning

confidence: 99%

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

et al. 2020

View full text Add to dashboard Cite

show abstract

“…The formation of disulphide bonds is promoted by the presence of reducing sugars and low water activity during the heating process. 38,39 Peptide size distribution…”

Section: Peptide Formation and Average Peptide Lengthmentioning

confidence: 99%

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

et al. 2020

View full text Add to dashboard Cite

show abstract

“…However, free amino groups decreased with prolonged incubation times ( Figure 1 ), indicating that the MR occurred but did not proceed beyond the early stage, most likely resulting in the formation of other MR products (MRPs) than CML. The heating conditions used to induce protein glycation as well as the MR itself can promote protein aggregation [ 37 ]. This is a crucial determinant as it has been shown before that heating- and glycation-induced aggregation of BLG results in the formation of sRAGE binding ligands [ 28 , 29 ].…”

Section: Discussionmentioning

confidence: 99%

Binding of CML-Modified as Well as Heat-Glycated β-lactoglobulin to Receptors for AGEs Is Determined by Charge and Hydrophobicity

Zenker

Teodorowicz

Ewaz

et al. 2020

IJMS

View full text Add to dashboard Cite

Intake of dietary advanced glycation end products (AGEs) is associated with inflammation-related health problems. Nε-carboxymethyl lysine (CML) is one of the best characterised AGEs in processed food. AGEs have been described as ligands for receptors present on antigen presenting cells. However, changes in protein secondary and tertiary structure also induce binding to AGE receptors. We aimed to discriminate the role of different protein modifications in binding to AGE receptors. Therefore, β-lactoglobulin was chemically modified with glyoxylic acid to produce CML and compared to β-lactoglobulin glycated with lactose. Secondary structure was monitored with circular dichroism, while hydrophobicity and formation of β-sheet structures was measured with ANS-assay and ThT-assay, respectively. Aggregation was monitored using native-PAGE. Binding to sRAGE, CD36, and galectin-3 was measured using inhibition ELISA. Even though no changes in secondary structure were observed in all tested samples, binding to AGE receptors increased with CML concentration of CML-modified β-lactoglobulin. The negative charge of CML was a crucial determinant for the binding of protein bound CML, while binding of glycated BLG was determined by increasing hydrophobicity. This shows that sRAGE, galectin-3, and CD36 bind to protein bound CML and points out the role of negatively charged AGEs in binding to AGE receptors.

show abstract

“…IF also contain significant levels of advanced glycation endproducts (AGE) materials including the early stage product furosine, and well-characterised AGEs including N E -(carboxymethyl)lysine (CML), N E -(carboxyethyl)lysine (CEL), pyrraline, and protein crosslinks, such as pentosidine (from Lys and Arg residue linked by a pentose), glyoxal lysine dimer (GOLD), methylglyoxal lysine dimer (MOULD), and Arg-derived products such as argpyrimidine and hydroimidazolone isomers [56,[65][66][67][68][69][70][71][72]. The levels of these materials have been examined using a wide variety of both direct and indirect methodologies [66,73,74].…”

Section: Presence Of Oxidation Glycation and Racemised Whey Proteinmentioning

confidence: 99%

Whey proteins: targets of oxidation, or mediators of redox protection

Giblin

Yalçın

Biçim

et al. 2019

Free Radical Research

View full text Add to dashboard Cite

Bovine whey proteins are highly valued dairy ingredients. This is primarily due to their amino acid content, digestibility, bioactivities and their processing characteristics. One of the reported bioactivities of whey proteins is antioxidant activity. Numerous dietary intervention trials with humans and animals indicate that consumption of whey products can modulate redox biomarkers to reduce oxidative stress. This bioactivity has in part been assigned to whey peptides using a range of biochemical or cellular assays in vitro. Superimposing whey peptide sequences from gastrointestinal samples, with whey peptides proven to be antioxidant in vitro, allows us to propose peptides from whey likely to exhibit antioxidant activity in the diet. However, whey proteins themselves are targets of oxidation during processing particularly when exposed to high thermal loads and/or extensive processing (e.g. infant formula manufacture). Oxidative damage of whey proteins can be selective with regard to the residues that are modified and are associated with the degree of protein unfolding, with a-Lactalbumin more susceptible than b-Lactoglobulin. Such oxidative damage may have adverse effects on human health. This review summarises how whey proteins can modulate cellular redox pathways and conversely how whey proteins can be oxidised during processing. Given the extensive processing steps that whey proteins are often subjected to, we conclude that oxidation during processing is likely to compromise the positive health attributes associated with whey proteins.

show abstract

Maillard induced aggregation of individual milk proteins and interactions involved

Cited by 24 publications

References 39 publications

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

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

Binding of CML-Modified as Well as Heat-Glycated β-lactoglobulin to Receptors for AGEs Is Determined by Charge and Hydrophobicity

Whey proteins: targets of oxidation, or mediators of redox protection

Contact Info

Product

Resources

About