Abstract
Mixtures of bovine caseins can serve as a benchmark for understanding the functionality of microbial-based recombinant caseins at oil–water interfaces. In this work we show that, in the presence of Ca2+, the individual casein fractions form viscoelastic networks at the oil–water interface with comparable stiffness. In the absence of Ca2+, αs2- and β-casein interfacial network formation was strongly inhibited over the full deformation regime. For αs1-casein, the network stiffness was increased in the absence of Ca2+ at small deformations (<15%), but at large deformations (>50%) it was completely disrupted, to a similar stiffness as αs2- and β-casein. The interfacial structure formed by κ-casein was largely unaffected by Ca2+ due to limited phosphorylation. We hypothesize that the differences between calcium-sensitive caseins lie in the conformation they assume at the interface. Both αs2- and β-casein adsorb in a train-tail conformation with a tail extending into the aqueous bulk phase, whereas αs1-casein adsorbs in a loop-train conformation, with a loop that extends less into the bulk phase. The tail-train configuration is hypothesized to increase the inter-molecular Ca2+ bridging thereby increasing the interfacial stiffness of αs2- and β-casein.Blending the casein fractions revealed a strong negative effect of β-casein on the interfacial modulus, which was more pronounced at a higher concentration. The presence of Ca2+ remained important for interfacial network formation of a casein blend. Without Ca2+, the interfacial network was less stiff, more viscous, and behaved like a 2d polymer solution.With this work we showed that casein interfacial network formation at oil–water interfaces is mediated by Ca2+ bridging. Blending the different casein fractions decreased the interfacial viscoelastic properties through the presence of β-casein. These results indicate that future work on recombinant caseins should focus on single genetic variants, since a blend of variants will likely decrease interfacial functionality.
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