Functional Properties of Oat Proteins in Food Systems

Oat proteins, comprising primarily globulins and prolamins, have attracted growing interest as sustainable, allergen-low ingredients for diverse food applications. Their functionality is dictated by intrinsic factors such as amino acid composition, molecular structure and surface hydrophobicity, and by extrinsic factors including pH, ionic strength and processing conditions. In aqueous systems, solubility governs the capacity of oat proteins to participate in emulsification, foaming and gelation. At interfaces, these proteins can reduce surface tension and stabilise oil–water or air–water boundaries, enabling plant-based emulsions and aerated products. Under thermal or enzymatic treatments, proteins unfold or hydrolyse to form three-dimensional networks, yielding gels with tunable texture and mouthfeel. Heat-induced denaturation and Maillard-type reactions may further modify functionality, influencing colour and digestibility. Advances in extraction and modification techniques are expanding the use of oat proteins in dairy analogues, meat substitutes and bakery goods, highlighting their potential to enhance nutritional profiles, sensory attributes and environmental sustainability in global food systems.

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Functional Properties of Oat Proteins in Food Systems publication trend

The graph below shows the total number of articles in functional properties of oat proteins in food systems across all publications each year (not limited to Nature Index journals).

Technical terms

Globulin: A water-soluble storage protein fraction in oats, crucial for gelation and foaming.

Prolamin: An alcohol-soluble storage protein fraction, influencing solubility and interfacial activity.

Solubility: The extent to which protein dissolves in aqueous media, foundational for all downstream functionality.

Emulsification: The ability of proteins to stabilise oil–water interfaces by reducing interfacial tension.

Gelation: The formation of a three-dimensional protein network, often induced by heat or enzymatic treatment, to create semi-solid textures.

Enzymatic hydrolysis: The controlled cleavage of peptide bonds by enzymes, used to modify molecular size and functional behaviour.

Foaming: The capacity of proteins to form and stabilise air-liquid interfaces, important for aerated products.

References

1. Oat protein: Review of structure-function synergies with other plant proteins. Food Hydrocolloids (2024).
2. Oat protein as plant-derived gelling agent: Properties and potential of modification. Future Foods (2021).
3. Effect of Stir-Frying on Physicochemical and Functional Properties of Oat Protein Isolates. Foods (2023).