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Tuning heat-induced colloidal aggregation of whey proteins, sodium caseinate and gum arabic: Effect of protein composition, preheating and gum arabic level

Loveday, Simon M., Ye, Aiqian, Anema, Skelte G., Singh, Harjinder
Food research international 2014 v.62 pp. 128-136
active sites, electrostatic interactions, gum arabic, heat, heat treatment, hydrophobic bonding, ionic strength, pH, protein composition, sodium caseinate, whey protein
Heating can drive the colloidal complexation of negatively-charged proteins and polysaccharides by strengthening hydrophobic interactions and denaturing proteins, thereby exposing reactive sites for covalent and noncovalent bonding. We have previously shown that stable colloidal aggregates comprising whey protein, sodium caseinate and gum arabic can be produced by careful selection of heat treatment, pH and protein type. Here we tested how the size, composition, charge and morphology of colloidal aggregates are affected by the amounts of whey protein, sodium caseinate and gum arabic, as well as the thermal history of the proteins. Increasing amounts of whey protein resulted in larger particles, which were more prone to precipitate. Preheating whey protein slightly enhanced aggregation, and this effect was mitigated when sodium caseinate was present during preheating (chaperone effect). Increasing amounts of gum arabic produced larger particles with less charge, but the gum arabic effect was statistically confounded with ionic strength. We believe that both covalent (disulphide) and noncovalent interactions among protein molecules are required to overcome electrostatic repulsion at pH7 and form stable aggregates.