Abstract

Recent work suggests that using blends of dairy and plant proteins could be a promising way to mitigate sustainability and functionality concerns. Many proteins form viscoelastic layers at fluid interfaces and provide physical stabilization to emulsion droplets; yet, the interfacial behavior of animal-plant protein blends is greatly underexplored. In the present work, we considered pea protein isolate (PPI) as a model legume protein, which was blended with well-studied dairy proteins (whey protein isolate (WPI) or sodium caseinate (SC)). We performed dilatational rheology at the air-water and oil-water interface using an automated drop tensiometer to chart the behavior and structure of the interfacial films, and to highlight differences between films made with either blends, or their constituting components only.The rheological response of the blend-stabilized interfaces deviated from what could be expected from averaging those of the individual proteins and depended on the proteins used; e.g. at the air-water interface, the response of the caseinate-pea protein blend was similar to that of PPI only. At the oil-water interface, the PPI and WPI-PPI interfaces gave comparable responses upon deformation and formed less elastic layers compared to the WPI-stabilized interface. Blending SC with PPI gave stronger interfacial layers compared to SC alone, but the layers were less stiff compared to the layers formed with WPI, PPI and WPI-PPI. In general, higher elastic moduli and more rigid interfacial layers were formed at the air-water interface, compared to the oil-water interface, except for PPI.

Highlights

  • Many food products are multiphase systems, such as foams and emulsions

  • Clear differences were found between the individual proteins; at the end of the experiment, pea protein isolate (PPI)-stabilized interfaces showed the highest surface pressure of 28.8 ± 0.8 mN/m, sodium caseinate (SC) was at 25.9 ± 0.8 mN/m, and whey protein isolate (WPI) was the lowest at 23.3 ± 1.3 mN/m

  • The WPI-PPI blend-stabilized interface followed the surface pressure curve of the PPI-stabilized interface until a surface pressure of 29.0 ± 1.3, which could be indicative of a preferential adsorption of pea proteins

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Summary

Introduction

Many food products are multiphase systems, such as foams and emulsions. These products often contain proteins, which are amphiphilic molecules that adsorb at the air-water or oil-water interface, and thereby play a crucial role in the formation and stability of the systems. Foams and emulsions have a high specific surface area (i.e., are interface-dominated systems) and their stability strongly depends on the protein’s interfacial properties [4,5]. Globular dairy proteins such as bovine serum albumin (BSA), lysozyme and β-lactoglobulin (β-lg) adsorb slower but form stronger viscoelastic films, which is attributed to their ability to form densely packed monolayers with in-plane protein-protein interactions at both the air- and oil-water interface [10,11]

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