Functional Properties of Potato Proteins in Food Systems

Potato proteins, predominantly comprising patatin and a range of protease inhibitors, have emerged as versatile functional ingredients in diverse food matrices. Their unique composition, rich in essential amino acids and exhibiting favourable techno‐functional attributes, positions them as sustainable alternatives to animal‐derived proteins. Key functional properties include gelation, emulsification, foaming and water‐binding capacity, each influenced by processing conditions such as pH, temperature and applied pressure. Gelation behaviour is governed by the unfolding and aggregation of patatin molecules, leading to networks whose texture and water retention can be fine‐tuned. Emulsifying capacity arises from surface adsorption and interfacial film formation by soluble protein fractions, stabilising oil‐in‐water dispersions under various shear and pH conditions. Potato protein isolates also exhibit antioxidant and bioactive properties, further enhancing their value in functional and health‐promoting foods. Advances in green extraction methods and protein fractionation have improved purity and yield, while novel processing techniques enable targeted modulation of structure–function relationships. The global push towards plant‐based and clean‐label formulations underscores the practical relevance of potato proteins in meat analogues, dairy alternatives, dressings, gels and bakery products.

Research from Nature Portfolio

No recent Nature Portfolio content available.

Functional Properties of Potato Proteins in Food Systems publication trend

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

Technical terms

Patatin: The major storage glycoprotein in potato tubers (40–45 kDa) responsible for gel network formation and emulsification.

Protease inhibitor: Small water‐soluble proteins (7–21 kDa) in potatoes that contribute to interfacial film strength and modulate aggregation behaviour.

Gelation: The process by which soluble proteins unfold, aggregate and form a three-dimensional network that entraps water, determining texture and firmness.

Emulsification: Stabilisation of oil-in-water dispersions by proteins adsorbed at the interface, preventing droplet coalescence under mechanical or thermal stress.

High-pressure processing: A non-thermal technique applying 300–600 MPa to induce conformational changes in proteins, enabling gelation or modification of functional properties while preserving heat-labile compounds.

References

1. Comparison of Thermal and High-Pressure Gelation of Potato Protein Isolates. Foods (2020).
2. Influence of pH, Temperature and Protease Inhibitors on Kinetics and Mechanism of Thermally Induced Aggregation of Potato Proteins. Foods (2021).
3. High Hydrostatic Pressure (HHP)-Induced Structural Modification of Patatin and Its Antioxidant Activities. Molecules (2017).
4. The Nutritional Value and Biological Activity of Concentrated Protein Fraction of Potato Juice. Nutrients (2019).
5. Potato Industry By-Products as a Source of Protein with Beneficial Nutritional, Functional, Health-Promoting and Antimicrobial Properties. Applied Sciences (2021).
6. Interfacial moduli at large strains and stability of emulsions stabilised by plant proteins at high bulk shear rates. Food Hydrocolloids (2024).