Food science is increasingly focused on developing healthier, more sustainable, and minimally processed foods by leveraging alternative proteins, precision fermentation, functional ingredients, and circular economy approaches that reduce waste and environmental impact. At the same time, advances in analytical technologies, AI, and multiscale characterization are helping researchers optimize food structure, texture, stability, and shelf life while ensuring safety, quality, and consumer acceptance.
Crystal size and polymorphic form control texture and structure, but shift under heating and cooling — making quality hard to hold consistent.
Proteins unfold and bind into gel networks or emulsions during processing, but plant-based substitutes form different networks — changing texture, mouthfeel, and quality.
Gelatinization and retrogradation reshape starch over time, and the process is further complicated by sugar, salt, fat, and pH.
Droplet and bubble size govern texture and mouthfeel, but the link is usually tuned empirically — and structures gradually destabilize over time.
These nanoscale architectures form and reorganize continuously during processing, storage, and even digestion, meaning structure at manufacture doesn’t guarantee structure at consumption.
Small- and Wide-Angle X-ray Scattering (SAXS/WAXS) provides a non-destructive view of evolving food structures without disrupting delicate phase equilibria. By linking nanoscale organization to properties such as texture, spreadability, and mouthfeel, SAXS/WAXS help researchers develop formulations that are robust, processable, and deliver consistent consumer performance by measuring:
The polymorphic form of fats, the growth and network formation of the crystals all impact the texture and mouthfeel of the product, which needs to be accounted for when reducing fat content.
Relevant for baked goods where the starch solid form will dictate the gelatinization during processing and the digestibility. Particularly important for gluten free recipes.
Unfolding helps to make the protein more available for digestion by enzymes but also more prone to aggregation and subsequent formation of gel networks, which impacts texture and stability.
The network architecture of protein gels provides insight into texture, water retention, mechanical properties and product stability.
This is critical for avoiding coalescence and phase separation, but also to optimize nutrient encapsulation and delivery.
The nanoscale structure of the encapsulation systems is a controlling factor in the quantity of the nutrients protected within and the manner of their release to become bioavailable.
In this example, there are clear phase transitions of gamma-lactones (functional food nanocarriers) as the ratio of flavour compound increases (decreasing δ). The different phases are represented by the letters V, H and L, where L is completely disordered. The L phase is dominant at high flavour loadings, which may reduce stability and impact delivery of the functional food.