Heat-induced gelation, rheology and stability of oil-in-water emulsions prepared with patatin-rich potato protein

The Effect of Heat- and Salt Treatment on the Stability and Rheological Properties of Chickpea Protein-Stabilized Emulsions

“…According to Mulla et al [38], non-thermal methods like highpressure or high-hydrostatic pressure processing enhance the rheological, thermal, and functional properties of legume proteins with minimal effect on macro-and micronutrients and properties related to swallowing and digestion. Literature data indicate that both the high pressure and the number of passes through the homogenizer affect the physicochemical and functional properties of emulsions, as well as their stability [33,34,39,40]; but it should be emphasized that HPH-induced effects are strongly dependent on matrix characteristics and treatment conditions [41]. In the protein-stabilized emulsion, as a result of high-pressure treatment, in addition to the reduction in size and homogeneity of the fat globules, there may also be protein unfolding and exposure of some reactive groups, such as free sulfhydryl and hydrophobic groups, thus further enhancing the functionality of proteins [39].…”

“…The Turbiscan tool enables quick identification and monitoring of destabilization mechanisms in emulsion systems [33,34,42]. It detects migration (sedimentation, creaming) or particle size change (coalescence) of a dispersed phase over time, which leads to a variation in backscattering (BS) and transmission (T) of light intensity [43].…”

“…It detects migration (sedimentation, creaming) or particle size change (coalescence) of a dispersed phase over time, which leads to a variation in backscattering (BS) and transmission (T) of light intensity [43]. The instrument makes it possible to determine and compare the kinetics of destabilization of many samples and to determine the stability parameter-Turbiscan Stability Index (TSI) [33,34,43].…”

“…Finally, once the temperature returned to 20 • C, the decrease in moduli plateaued, and the specimen reached its final G ′ < G ′′ , suggesting its liquid state remains similar to before heating. It should be mentioned that a higher denaturation temperature of proteins in their water dispersion compared to the denaturation temperature in emulsion has also been demonstrated for other protein systems, because proteins undergoing surface denaturation during adsorption at the water-oil interface are more susceptible to thermal denaturation [33,34,64].…”

“…In our previous studies [33,34], we have shown that the number of cycles of the emulsion passing through the HP homogenizer can affect the properties of the protein-stabilized emulsion. This time, not only the emulsions but also their water protein dispersions were pre-processed in the HP homogenizer.…”