|Title||Investigating the effect of temperature on the formation and stabilization of ovalbumin foams|
|Author(s)||Delahaije, Roy J.B.M.; Lech, Frederik J.; Wierenga, Peter A.|
|Source||Food Hydrocolloids 91 (2019). - ISSN 0268-005X - p. 263 - 274.|
|Publication type||Refereed Article in a scientific journal|
|Keyword(s)||Concentration - Interfacial properties - Protein - Structural characterization - Viscosity|
The effect of temperature (below denaturation temperature) on protein foam formation and stabilization is potentially large, but has received little attention. This study aims to identify the effect of temperature (15–60 °C) on ovalbumin-stabilized foams at different concentrations (0.05–50 g L−1), and place this in a theoretical perspective. With increasing temperature the initial adsorption rate (dΠ/dt) increased logarithmically from 0.006 mN m−1 s−1 at 5 °C to 0.084 mN m−1 s−1 at 60 °C. A concentration increase resulted in a linear increase of dΠ/dt. This concentration effect was also observed in the foam ability, although the foam ability increased logarithmically rather than linearly with concentration, as expected based on theory and dΠ/dt. The foam ability was hardly affected by temperature (in contrast to theory and dΠ/dt). This was attributed to the strong decrease of foam stability with increasing temperature, which was expected based on theory. At elevated temperatures, the poor foam stability interferes with the foam ability (i.e. foam stability ≈ timescale of foam formation), a situation also happening at low concentrations. When formation was faster than destabilization, the foam ability relates to the effective adsorption rate. The effective adsorption rate includes the decrease in adsorption probability with increasing surface coverage. The observed balance between the effect of adsorption rate and foam stability on foam ability is not quantitatively predictable based on current theoretical models.