A shift from animal protein- to plant protein-based foods is crucial in transitioning toward a more sustainable global food system. Among food products typically stabilized by animal proteins, food foams represent a major category. Wheat proteins are ubiquitous and structurally diverse, which offers opportunities for exploiting them for food foam and air-water interface stabilization. Notably, they are often classified into those that are soluble in aqueous systems (albumins and globulins) and those that are not (gliadins and glutenins). However, gliadins are at least to an extent water extractable and thus surface active. We here provide a comprehensive overview of studies investigating the air-water interfacial and foaming properties of the different wheat protein fractions. Characteristics in model systems are related to the functional role that wheat proteins play in gas cell stabilization in existing wheat-based foods (bread dough, cake batter, and beer foam). Still, to further extend the applicability of wheat proteins, and particularly the poorly soluble glutenins, to other food foams, their modification is required. Different physical, (bio)chemical, and other modification strategies that have been utilized to alter the solubility and therefore the air-water interfacial and foaming properties of the gluten protein fraction are critically reviewed. Such approaches may open up new opportunities for the application of (modified) gluten proteins in other food products, such as plant-based meringues, whippable drinks, or ice cream. In each section, important knowledge gaps are highlighted and perspectives for research efforts that could lead to the rational design of wheat protein systems with enhanced functionality and overall an increased applicability in food industry are proposed.
Keywords: food foam; gas cells; gliadin; gluten; protein modification.
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