Coalescence stability of emulsions containing globular milk proteins

This review summarizes a large set of related experimental results about protein adsorption and drop coalescence in emulsions, stabilized by globular milk proteins, beta-lactoglobulin (BLG) or whey protein concentrate (IATC). First, we consider the effect of drop coalescence on the mean drop size, d(32), during emulsification. Two regimes of emulsification, surfactant-rich (negligible drop coalescence) and surfactant-poor (significant drop coalescence) are observed in all systems studied. In the surfactant-rich regime, d(32) does not depend on emulsifier concentration and is determined mainly by the interfacial tension and the power dissipation density in the emulsification chamber, e. In the surfactant-poor regime and suppressed electrostatic repulsion, d(32) is a linear function of the inverse initial emulsifier concentration, 1/C-INI, which allows one to determine the threshold emulsifier adsorption needed to stabilize the oil drops during emulsification, Gamma* (the latter depends neither on oil volume fraction nor on e). Second, we study how the BLG adsorption on drop surface changes while varying the protein and electrolyte concentrations, and pH of the aqueous phase. At low electrolyte concentrations, the protein adsorbs in a monolayer. If the pH is away from the isoelectric point (IEP), the electrostatic repulsion keeps the adsorbed BLG molecules separated from each other, which precludes the formation of strong intermolecular bonds during shelf-storage as well as after heating of the emulsion. At higher electrolyte concentration, the adsorption Gamma increases, as a result of suppressed electrostatic repulsion between the protein molecules; monolayer or multilayer is formed, depending on protein concentration and pH. The adsorption passes through a maximum (around the protein IEP) as a function of pH. Third, the effect of various factors on the coalescence stability of fresh emulsions (up to several hours after preparation) was studied. Important conclusion from this part of the study is the establishment of three different cases of emulsion stabilization: (1) electrostatically-stabilized emulsions with monolayer adsorption, whose stability is described by the DLVO theory; (2) emulsions stabilized by steric repulsion, created by protein adsorption multilayers - a simple model was adapted to describe the stability of these emulsions; and (3) emulsions stabilized by steric repulsion, created by adsorption monolayers. Fourth, we studied how the emulsion stability changes with storage time and after heating. At high electrolyte concentrations, we find a significant decrease of the coalescence stability of BLG-emulsions after one day of shelf-storage (aging effect). The results suggest that aging is related to conformational changes in the protein adsorption layer, which lead to formation of extensive lateral non-covalent bonds (H-bonds and hydrophobic interactions) between the adsorbed molecules. The heating of BLG emulsions at high electrolyte concentration leads to strong increase of emulsion stability and to disappearance of the aging effect, which is explained by the formation of disulfide bonds between the adsorbed molecules. The emulsion heating at low electrolyte concentration does not affect emulsion stability - this result is explained with the electrostatic repulsion between the adsorbed molecules, which keeps them separated so that no intermolecular disulfide bonds are formed. Parallel experiments with WPC-stabilized emulsions show that these emulsions are less sensitive t variations of pH and thermal treatment; no aging effect is detected up to 30 days of storage. The observed differences between BLG and WPC are explained with the different procedures of preparation of these protein samples (freeze-drying and thermally enhanced spray-drying, respectively). Our data for emulsion coalescence stability are compared with literature results about the flocculation stability of BLG emulsions, and the observed similarities/differences are explained by considering the structure of the protein adsorption layers. (c) 2006 Elsevier B.V. All rights reserved.