Double emulsions stabilized by a charged complex of modified pectin and whey protein isolate.

Citation:

Rachel Lutz, Aserin, Abraham , Wicker, Louis , and Garti, Nissim. . 2009. “Double Emulsions Stabilized By A Charged Complex Of Modified Pectin And Whey Protein Isolate.”. Colloids And Surfaces, B: Biointerfaces, 72, 1, Pp. 121–127. doi:10.1016/j.colsurfb.2009.03.024.

Abstract:

Double emulsions based on naturally occurring stabilizers for food applications were studied. Two charged biopolymers, whey protein isolate (WPI) and enzymic modified pectins, interacted in aq. soln. to form a charge-charge complex that was utilized as a hydrophilic polymeric steric stabilizer improving the double emulsion stability. The main factors that influence the interaction between protein and pectin were investigated in relation to double emulsion stability: creaming, coalescence, and water transport between aq. phases. The pH detd. the size of the complex formed. Thus at pH 6, where a sol. complex was obtained between some mol. pos. charged patches on the protein and neg. charged fractions of the hydrocolloids, the double emulsion was the most stable. With the smallest droplet size (∼15 $μ$m), the lowest creaming, highest yield, and minimized water transport were obtained. The best concn. and ratio to form the sol. complex are 4% WPI and 0.5% pectin (for 30% of the W/O inner phase). The influence of the charge distribution (degree of order of the carboxylic groups) of the pectin on the assocd. complex was also investigated, and it was found that the more "ordered" pectin (U63) formed the most stable double emulsion against water transport. [on SciFinder(R)]

Last updated on 05/27/2020