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The gelation kinetics of β-lactoglobulin (βLg) solutions has been determined in the alkaline regime over a wide range of protein concentrations, gelling temperatures and gelation pH (pHgel), set using NaOH. The behaviour is compared with caustic-induced gelation of whey protein concentrate and the alkaline dissolution of heat-induced whey gels. The gelation time decreases significantly between neutral conditions and pHgel 9, because of the activation of the free cysteine groups and displacement to the monomeric form, and between pHgel 10 and 11, due to the base denaturation of βLg. Both transitions are associated with a significant decrease in the activation energy of gelation. At pHgel >11.5 the gelation time is observed to increase with pHgel, owing to destruction of interprotein crosslinks. These results are consistent with the recently reported observation that a minimum pH for the dissolution of βLg gels and aggregates exists around 11.6 [ Biomacromolecules 8 (2007) 1162]. This phenomenon has been assigned to the destruction of non-covalent interactions that would inhibit the final percolation of the gel. [ABSTRACT FROM AUTHOR]

Abstract: The formation of immobile gels on heat transfer surfaces (‘coring’) caused by cooling fat solutions below their cloud point was studied using a novel spinning disc apparatus (SDA). The SDA features a cooled, removable heat transfer surface with well defined heat and mass transfer characteristics. Measurements of heat flux were combined with computational fluid dynamics simulations to yield reliable estimates of the surface temperature and shear stress. Fouling studies were performed with model solutions of 5wt.% tripalmitin in a paraffin oil operating in the ‘cold start’ mode, wherein the experiment starts with the surface colder than the steady state, simulating one mode of operating a standard ‘cold finger’ experiment. Local heat flux measurements allowed the thermal fouling resistance to be monitored: deposit mass coverage and composition were also measured. The cold surface promotes the rapid formation of an initial gel layer, followed by a period of linear fouling, and finally falling rate fouling behaviour. The linear fouling rate was relatively insensitive to temperature and shear rate, while the fouling rate in the falling rate regime was found to depend on the temperature driving force for crystallisation kinetics. The solids fraction within the deposit layer increased over the duration of a 12h fouling test, indicating rapid ageing. The rheological properties of the deposits were highly sensitive to solids fraction. [Copyright &y& Elsevier]

Abstract: The literature reports an optimum NaOH concentration for the alkaline cleaning of whey deposits or gels; at NaOH concentrations higher than this optimum, cleaning proceeds much more slowly. Although this phenomenon is of great importance in the cleaning of dairy equipment, no conclusive physical explanation has yet been presented. In this study, we present strong evidence that the dissolution rate is affected by the equilibrium-swelling ratio in β-lactoglobulin (βLg) gels. The swelling ratio is greatly reduced in the presence of salts due to the polyelectrolyte screening effect of the cations. This has been observed in free-swelling βLg gels using gravimetrical analysis and in the uniaxial swelling of WPC gel deposits using fluid dynamic gauging. At high dissolution pH (>13.3), the high Na+ concentration reduces swelling in spite of the high surface charge of the protein. It is proposed that the reduction of the free volume inside the gel impedes the transport of the protein aggregates out of the NaOH penetration zone. We have also observed that the final dissolution rate of gels pre-soaked in 1M NaOH or NaCl is similar, despite the difference in pH, and much lower than for untreated gels: the high Na+ concentration in the soaked gels hinders swelling, inhibiting the disentanglement of the protein clusters regardless of the high pH. [Copyright &y& Elsevier]