Foam‐type cakes are complex food systems. Their main ingredients are wheat flour, hen eggs, sugar, leavening agent, and, in some cases, oil and/or surfactants. In contrast to the vast amount of research outcomes on the contribution of ingredients to the quality of batter‐type cake systems, information on the functionality and importance of the ingredients and their constituents in foam‐type cake systems is lacking. This review defines foam‐type cakes, describes how they are made, summarizes the current knowledge of factors determining their quality, and identifies the current knowledge gaps.

Formation of amyloid fibrils (i.e. protein structures containing a compact core of ordered β-sheet structures) from food proteins can improve their techno-functional properties. Wheat gluten is the most consumed cereal protein by humans and extensively present in food and feed systems. Hydrolysis of wheat gluten increases the solubility of its proteins and brings new opportunities for value creation. In this study, the formation of amyloid-like fibrils (ALFs) from wheat gluten peptides (WGPs) under food relevant processing conditions was investigated. Different hydrothermal treatments were tested to maximize the formation of straight ALFs from WGPs. Thioflavin T (ThT) fluorescence measurements and transmission electron microscopy (TEM) were used to study the extent of fibrillation and the morphology of the fibrils, respectively. First, the formation of fibrils by heating solutions of tryptic WGPs [degrees of hydrolysis 2.0% (DH 2) or 6.0% (DH 6)] was optimized using a response surface design. WGP solutions were incubated at different pH, times and temperatures. DH 6 WGPs had a higher propensity for fibrillation than did DH 2 WGPs. Heating DH 6 WGPs at 2.0% (w/v) for 38 hours at 85 °C and pH 7.0 resulted in optimal fibrillation. Secondly, trypsin, chymotrypsin, thermolysin, papain and proteinase K were used to produce different DH 6 WGPs. After enzyme inactivation and subsequent heating at optimal fibrillation conditions, chymotrypsin and proteinase K DH 6 WGPs produced small worm-like fibrils whereas fibrils prepared from trypsin DH 6 WGPs were long and straight. The surface hydrophobicity of the peptides was key for fibrillation. Thirdly, peptides from the wheat gluten components gliadin and glutenin fractions formed smaller and worm-like fibrils than did WGPs. Thus, peptides of both gluten protein fractions jointly contribute in gluten fibrillation.

Drying mode and hydrothermal treatment conditions govern the formation of amyloid-like protein fibrils in solutions of dried hen egg white, Food Hydrocolloids, 112, 106276.

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Successful sucrose replacement in cake recipes requires thorough understanding of its functionalities and those of potential substitutes during cake production. We show that effective sucrose substitutes provide sufficient aqueous cake batter phase (i.e. batter liquor) with low proton mobility (assessed with time-domain 1H NMR relaxometry) and high viscosity, and ensure sufficient air incorporation during batter mixing, along with appropriate timings of starch and protein transitions during baking. Maltitol and oligofructose are very soluble and, like sucrose, provide adequate batter liquor quantities with low water mobility and high viscosity, while poorly soluble mannitol does not. However, differential scanning calorimetry and rapid viscosity analyses show that oligofructose fails to provide appropriate timings of starch gelatinisation and protein denaturation, leading to poor cake texture. That the shortcomings of mannitol (in terms of solubility) and oligofructose (in terms of biopolymer transitions) can be overcome by using mixtures thereof is relevant for the baking industry.