Interfacial rheology of sodium caseinate/high acyl gellan gum complexes: Stabilizing oil-in-water emulsions

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Abstract

In this work, the effects of pH and high acyl gellan gum concentration on the adsorption kinetics and interfacial dilatational rheology of sodium caseinate/high acyl gellan gum (CN/HG) complexes were investigated using a pendant drop tensiometer. In addition, stability related properties including interfacial protein concentration, droplet charge, size, microstructure and creaming index of emulsions were studied at different HG concentration (0–0.2 wt%) and pH values (4, 5.5 and 7). The results showed that HG adsorbed onto the CN mainly through electrostatic interactions which could lead to increase the interfacial pressure (π), rates of protein diffusion (k _diff), and molecular penetration (k _p). The CN/HG complexes formed thick adsorption layers around the oil droplets which significantly increased the surface dilatational modulus with the increasing HG concentration. The CN/HG complexes appeared to form more elastic interfacial films after a long-term adsorption time compared with CN alone, which could reduce the droplet coalescence and thus prevented the growth of emulsion droplets. All four phosphorylated proteins of CN (α _s1-, α _s2-, β-, and κ-casein) were adsorbed at the oil-water (O/W) interface as confirmed by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), and surface protein coverage increased progressively with increasing HG concentration at pH 5.5, but decreased at pH 7. The CN/HG stabilized emulsions at pH 5.5 revealed the higher net charges and smaller z-average diameters than those at pH 4 and pH 7. This study provides valuable information on the use of CN/HG complexes to improve the stability and texture of food emulsions.

Graphical abstract

Highlights

•Interactions between sodium caseinate (CN) and high acyl gellan gum (HG) studied.
•At pH 5.5, CN/HG interaction was mainly driven by electrostatic attractions.
•CN/HG complex improved the adsorption of CN at the oil-water interface.
•CN/HG complex could form stronger interfacial films than protein alone.
•Cooperative adsorption onto oil-water interface improved emulsion stability.

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Food proteins: a review on their emulsifying properties using a structure-function approach.

Ricky Lam, Michael Nickerson (2013)

Proteins are of great interest due to their amphiphilic nature, which allows them to reduce the interfacial tension at the oil-water interface. The incorporation of proteins at the oil-water interface has allowed scientists to utilise them to form emulsions (O/W or W/O), which may be used in food formulations, drug and nutrient delivery. The systematic study of the proteins at the interface and the factors that affect their stability (i.e., conformation, pH, solvent conditions, and thermal treatment) has allowed for a broader use of these emulsions tailored for various applications. In this review, the factors affecting the stability of emulsions using food proteins will be discussed. The use of polysaccharides to complex with proteins will also be explored in relation to enhancing emulsion stability.