Functional Properties of Pea Protein Isolates

Pea protein isolates, derived primarily from Pisum sativum, represent a versatile class of plant‐based ingredients with a spectrum of functional properties that underpin their growing use in food and biotechnological applications. Comprised chiefly of storage proteins—vicilins (7S) and legumins (11S)—alongside minor albumins, these isolates exhibit distinct solubility profiles determined by pH, ionic strength and processing history. Their water and oil holding capacities enable desirable textural attributes and moisture management in meat and dairy analogues, while their emulsifying and foaming functionalities stem from protein adsorption at oil–water and air–water interfaces, mediated by surface hydrophobicity and charge distribution. Gelation behaviour, influenced by protein concentration, temperature and denaturation degree, yields thermo‐reversible or thermally irreversible networks critical for structured products. Processing variables such as extraction pH, temperature, fractionation, heating or drying techniques profoundly alter molecular conformation and aggregation state, thereby modulating interfacial rheology, viscosity and texture. Advances in bioinformatic modelling and structure–function analyses are facilitating prediction of key attributes such as emulsification efficiency and gel strength, guiding tailored modifications. Beyond conventional food systems, pea protein isolates are now exploited as nanocarriers, leveraging enzymatically crafted albumin nanomicelles for enhanced bioactive delivery across gastrointestinal barriers. Collectively, these properties position pea protein isolates as sustainable, low‐allergen alternatives to animal and soy proteins, with global relevance for plant‐based nutrition, functional foods and novel delivery platforms.

Research from Nature Portfolio

No recent Nature Portfolio content available.

Functional Properties of Pea Protein Isolates publication trend

The graph below shows the total number of articles in functional properties of pea protein isolates across all publications each year (not limited to Nature Index journals).

Technical terms

Protein solubility: measure of the proportion of protein that dissolves in aqueous solution, influencing functionality such as emulsification and gelation.

Emulsifying properties: capacity of proteins to adsorb at oil–water interfaces and stabilise droplets against coalescence.

Foaming properties: ability of proteins to form and stabilise air bubbles by creating viscoelastic interfacial films.

Gelation capacity: ability of proteins to form three‐dimensional networks upon heating or pH change, yielding gels with defined texture.

Interfacial tension: force per unit length at the interface of two immiscible phases, reduced by surface‐active proteins.

Nanomicelles: nanoscale self‐assembled structures of amphiphilic proteins, employed for encapsulation and delivery applications.

References

1. Bioinformatic Approaches for Characterizing Molecular Structure and Function of Food Proteins. Annual Review of Food Science and Technology (2023).
2. Natural Gastrointestinal Stable Pea Albumin Nanomicelles for Capsaicin Delivery and Their Effects for Enhanced Mucus Permeability at Small Intestine. Biomaterials Research (2024).
3. Combined effects of isolation temperature and pH on functionality and beany flavor of pea protein isolates for meat analogue applications. Food Chemistry (2023).
4. Role of the pea protein aggregation state on their interfacial properties. Journal of Colloid and Interface Science (2023).
5. The impact of heating and freeze or spray drying on the interface and foam stabilising properties of pea protein extracts: Explained by aggregation and protein composition. Food Hydrocolloids (2022).