Denaturation and aggregation of β-lactoglobulin—a preliminary molecular dynamics study

Molecular Dynamics Simulation for Mechanism Elucidation of Food Processing and Safety: State of the Art

“…MD simulations involving high‐temperature effect on two GDLEIL peptides (glycine–aspartic acid–leucine–glutamic acid–isoleucine–leucine) in BLG existing predominantly in native β‐sheet forms showed that hydrogen bonds were formed between them (Euston, Ur‐Rehman, & Costello, ). This finding has an important implication on the elucidation of intermolecular interactions promoting fibril formation and gelation of denatured BLG, which can be attributed to the formation of hydrogen bond between β‐sheets.…”

Formation and properties of the whey protein/κ-casein complexes in heated skim milk – A review

“…Heat-treated milk proteins have interesting functional properties that are widely applied in food, cosmetics or pharmacy. In the last few decades, extensive research has been dedicated to the understanding of the heat-induced aggregation of denatured whey proteins in milk or in its fractions (whey, whey protein isolates) as well as in model systems of individual proteins, especially β-lactoglobulin [15,20,25,38,39,43,56,61,65,[85][86][87]92,108,109,140,141,156,165,179,191]. However, the simple comparison of heat-treated whey and skim milk strongly suggests that the presence of caseins, especially κ-casein, dramatically affects the characteristics of the heat-induced protein complexes in milk [21,51,151].…”

Digestibility and structural parameters of spray-dried casein clusters under simulated gastric conditions

“…A larger difference in the SH values between the specimens dried with 150°C and 180°C was observed in A70, approximately 27% increase, compared to A60 (23%). It was reported that a heat-induced rise in SH was observed in milk proteins, and it was caused by the denaturation of their tertiary and secondary structures (Euston, Ur-Rehman, & Costello, 2007;Eynard, Iametti, Relkin, & Bonomi, 1992;Risso, Borraccetti, Araujo, Hidalgo, & Gatti, 2008;Sava, Van der Plancken, Claeys, & Hendrickx, 2005). When adjusting the pH of a milk protein solution, the change in SH value was observed to be closely linked with their solubility and functional properties (Alizadeh-Pasdar & Li-Chan, 2000;Shimizu, Saito, & Yamauchi, 1985;Voutsinas, Cheung, & Nakai, 1983).…”