Abstract
The surface tension of freshly created food protein powder isolates was measured in aqueous solutions as a function of concentration, hydrolysis, and temperature. The surface tension of the solutions was measured immediately to best predict their surface-active behavior in a spray-drying scenario, where instantaneous values are more relevant than equilibrium surface tension measurements. Whole whey protein, hydrolyzed whey proteins (degrees of hydrolysis of 4, 9.5, 12, 17, and 20.2%), soy protein, pea protein isolates, and gelatin powders were diluted in a range of concentrations (0.04–2 g/L) and their surface tension values were reported at 23 ± 1°C. It was found that at higher concentrations hydrolyzed whey proteins at degrees of hydrolysis of 9.5 and 12%, and soy protein isolates in particular, showed excellent surface activity (shown through a decrease in surface tension) compared to nonhydrolyzed whey protein and gelatin. When comparing the influence of the degree of hydrolysis of whey proteins, the reverse was observed at lower concentrations (0.04–0.1 g/L), with the nonhydrolyzed whey protein reducing surface tension values more effectively than their hydrolyzed counterparts. Additionally, the protein solutions (2 g/L) were maintained at higher temperatures of 40, 50, and 60°C and the surface tension values were measured. There was a general improvement of surface activity of proteins indicated by the reduced surface tension of solutions at these temperatures compared with the pure water values. The protein solutions were also spray dried with maltodextrin (MD30) and the powder particle surface composition and structures were analyzed via X-ray photoelectron spectroscopy and scanning electron micrography. There was a trend of correlation between the surface activities of protein in solution with that of the surface composition of protein found on the powder particles. However, there were morphological indicators that corresponded well to the amount of protein present on the surface.
Published Version
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