Effects of protein concentration and CaCl2 on cold-set thickening mechanism of β-lactoglobulin at low pH

Development of Salt- and Gastric-Resistant Whey Protein Isolate Stabilized Emulsions in the Presence of Cinnamaldehyde and Application in Salad Dressing

“…Interestingly, the particle size was larger in the emulsions containing K + than in the ones containing Na + after aggregation was first observed, which suggests that the potassium ions may have been more effective at promoting irreversible flocculation of the WPI-coated oil droplets. The ability of the monovalent ions to promote droplet aggregation can mainly be attributed to their ability to screen the electrostatic repulsion between them [24]. In contrast, the M70C30 emulsions maintained a relatively small particle size (150-200 nm) at all monovalent ion concentrations (0 to 2000 mM) after 7 days' storage, which suggests that the presence of the cinnamaldehyde increased the salt stability of these emulsions, which is consistent with previous studies [21].…”

Influence of the polydispersity of pH 2 and pH 3.5 beta-lactoglobulin amyloid fibril solutions on analytical methods

“…The different morphology of the amyloid aggregates at pH 3.5 is based on the increase in pH above pH 3.35 (Mudgal et al 2011;Loveday et al 2010). While linear fibrillary structures occur at pH values ≤pH 3.0 (Lee et al 2012;Adamcik et al 2010;Loveday et al 2010), a further increase of the pH value (≥pH3.35) next to the isoelectric point of the protein (pI = 4.7 (Lee et al 2012)) first leads to worm-like (Serfert et al 2014;Mudgal et al 2009) and then to spherical aggregated structures (Jung et al 2008;Serfert et al 2014), as far as a low protein (2.5 wt%) and ion concentration is considered.…”

“…Acid hydrolysation was described as an essential step in the formation of straight as well as worm-like fibrils that occur at pH 2 (vandenAkker et al 2016). Terminal segments with amino acid sequence -2), as it was assumed for amyloids prepared at the pH value of pH 3.35 (Mudgal et al 2011).…”

Kinetic study of β-lactoglobulin thermal aggregation at low pH

“…During the development of this modification process, among various pHs screened, the selected pH adjustment to 3.35 resulted in maximum solubility and highest apparent viscosity upon dispersion of the modified powders (Hudson et al, 2000). The changes that occur to b-lg during this modification process as affected by protein concentration and CaCl 2 were investigated using a b-lg model system at the pH of this modification process (3.35) and constant heating time (Mudgal et al, 2009(Mudgal et al, , 2011. In the present study, effects of protein concentration and heating time were investigated at pH 3.35 to obtain an understanding of b-lg thermal aggregation with time during this modification process.…”