Mucins are long glycoprotein molecules responsible for the gel nature of the mucous layer that covers epithelial surfaces throughout the body. Mucins, as the major salivary proteins, are also important proteins for the food oral processing and digestion. The interactions of salivary mucins and saliva with several food proteins and food protein emulsions, as well as their functional properties related to the food oral processing were reviewed in this paper. The target food proteins of focus were whey proteins (lactoferrin and beta-lactoglobulin) and non-whey proteins (casein, gelatin, galectin/lectin, and proline-rich proteins). Most of the studies suggest that electrostatic attraction (between positively charged food proteins with negatively charged moieties of mucin mainly on glycosylated region of mucin) is the major mode of interaction between them. On the other hand, casein attracts the salivary proteins only via non-covalent interactions due to its naturally self-assembled micellar structure. Moreover, recent studies related to β-lactoglobulin (BLG)-mucin interactions have clarified the importance of hydrophobic as well as hydrophilic interactions, such as hydrogen bonding. Furthermore, in vitro studies between protein emulsions and saliva observed a strong aggregating effect of saliva on caseinate and whey proteins as well as on surfactant-stabilized emulsions. Besides, the sign and the density of the charge on the surface of the protein emulsion droplets contribute significantly to the behavior of the emulsion when mixed with saliva. Other studies also suggested that the interactions between saliva and whey proteins depends on the pH in addition to the flow rate of the saliva. Overall, the role of interactions of food proteins and food protein emulsions with mucin/saliva-proteins in the oral perception, as well as the physicochemical and structural changes of proteins were discussed.
Keywords: casein; emulsion; gelatin; lactoferrin; lectins; whey; β-lactoglobulin.