Abstract
Pea protein is a popular and sustainable plant-based protein with broad applications in the food industry. However, functionalities such as emulsification are still lacking. Protein functionality is defined by its structure, and protein structure can be modified through denaturation. In this work, the impacts of cold denaturation on emulsifying abilities of pea protein are studied. Commercial pea protein is treated with ethanol, shear forces, and low temperatures. Emulsions are prepared and characterized using creep experiments over time. Creep data are modeled using the Burger model, and the often-overlooked creep ringing region is fit with the Jeffreys model. Using these methods together provides valuable insight into emulsion structure and flow. Furthermore, rheological parameters favorably correlate with bioinformatic estimates of emulsion network strength derived from surface hydrophobicity and zeta potential measurements. Findings show that protein pre-treatments improve rheological stability of emulsions, and these impacts are most obvious at high concentrations, making these treatments good for protein supplementation in the food industry.
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