Preheat-stabilized pea proteins with anti-aggregation properties.

Area of Science:

• Food Science
• Protein Chemistry
• Materials Science

Background:

• Food protein solution stability is vital for shelf-life and sensory attributes.
• Demand for additive-free products challenges the creation of stable protein solutions, like beverages.
• Pea proteins (PPs) are a valuable plant-based protein source, but their stability can be limiting.

Purpose of the Study:

• To develop a facile method for stabilizing pea proteins (PPs) in solution.
• To investigate the structural changes and aggregation behavior of PPs under specific preheating conditions.
• To provide insights into creating heat-stable protein ingredients for the food industry.

Main Methods:

• Preheating pea proteins (PPs) at concentrations below 4% (w/v) and temperatures above 90°C.
• Utilizing far-ultraviolet circular dichroism, fluorescence spectra, and light scattering analyses to assess protein structure and aggregation.
• Employing rheological characterizations to evaluate the impact of preheating on protein network formation and stability.

Main Results:

• Preheating PPs below 4% (w/v) at >90°C induced unfolding and crosslinking via hydrophobic moieties and disulfide bonds.
• A stable, spatio-temporal interconnected system was formed, preventing initial aggregation.
• Rheological studies on higher concentration (15% w/v) samples showed reduced aggregation with increased preheating temperature and decreased preheating concentration.

Conclusions:

• A simple preheating method effectively stabilizes pea proteins (PPs) across a range of concentrations.
• The stabilized PPs form robust, heat-stable protein ingredients suitable for various food applications.
• This strategy offers a cost-effective approach for producing protein-enriched ingredients, meeting industry demands for additive-free products.