Nano-BioScience Research Group, DTU-Food, Technical University of Denmark, Lyngby, Denmark.
Department of Mechanical Engineering, Technical University of Denmark, Lyngby, Denmark.
Crit Rev Food Sci Nutr. 2020;60(1):64-83. doi: 10.1080/10408398.2018.1512950. Epub 2019 Jan 11.
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, 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.
黏蛋白是长糖蛋白分子，负责覆盖全身上皮表面的黏液层的凝胶性质。黏蛋白作为主要的唾液蛋白，也是食物口腔加工和消化的重要蛋白质。本文综述了唾液黏蛋白和唾液与几种食物蛋白和食物蛋白乳液的相互作用及其与食物口腔加工相关的功能特性。关注的目标食物蛋白是乳清蛋白（乳铁蛋白和β-乳球蛋白）和非乳清蛋白（酪蛋白、明胶、半乳凝集素/凝集素和富含脯氨酸的蛋白）。大多数研究表明，静电吸引（带正电荷的食物蛋白与黏蛋白上带负电荷的部分之间，主要在黏蛋白的糖基化区域）是它们之间相互作用的主要模式。另一方面，由于其天然的自组装胶束结构，酪蛋白仅通过非共价相互作用吸引唾液蛋白。此外，最近关于β-乳球蛋白（BLG）-黏蛋白相互作用的研究阐明了疏水相互作用以及氢键等亲水相互作用的重要性。此外，研究人员观察到唾液对酪蛋白和乳清蛋白以及表面活性剂稳定乳液的强烈聚集作用。此外，蛋白质乳液表面电荷的符号和密度对乳液与唾液混合时的行为有很大影响。其他研究还表明，除了唾液的流速外，唾液与乳清蛋白之间的相互作用还取决于 pH 值。总的来说，讨论了食物蛋白和食物蛋白乳液与黏蛋白/唾液蛋白之间相互作用在口腔感知中的作用，以及蛋白质的物理化学和结构变化。
