Abstract

• Animal-based globular proteins form stiff viscoelastic solid layers at interfaces. • Plant protein-based layers appear to be less stiff and more ductile. • Differences in protein conformation at the interface appear responsible for this. • Synchrotron radiation techniques are ideal to study the link microstructure-rheology. • Insights into this relation allow to find optimal modification routes for plant proteins. Proteins are an important category of stabilizers for multiphase food systems such as foams and emulsions. In recent years, a growing interest can be observed in replacing animal-based by plant-based proteins to stabilize such products. Often, these plant-based proteins have inferior functionality compared to animal-based proteins. In this review, we will discuss recent insights into possible reasons for the differences in behavior between animal-based and plant-based proteins, and present an overview of strategies to improve the performance of plant-based extracts. Improving plant-protein functionality may ultimately allow us to engineer interfaces with properties tailored to specific applications.

Highlights

  • When developing novel multiphase food products, the stability of their air–water and/or oil–water interfaces is an important design parameter

  • 4.0 nm Current Opinion in Food Science (a) Surface shear rheology on a whey protein-stabilized air–water interfacial film studied using a rheometer with a double wall ring geometry. (b) Surface pressure isotherms of whey protein and aggregated whey protein at an air–water interface studied using drop tensiometry. (c) Atomic force microscopy (AFM) images of whey protein-stabilized interfaces at various surface pressures, created using Langmuir-Blodgett deposition

  • Summary and outlook In this review, we have summarized current insights into which differences in protein structure between animalbased and plant-based globular proteins might be responsible for the lower functionality of the latter with respect to interface stabilization in foams and emulsions

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Summary

Introduction

When developing novel multiphase food products, the stability of their air–water and/or oil–water interfaces is an important design parameter. For products stabilized by proteins, animal-based proteins are still the most commonly used proteins, in view of their excellent stabilizing properties. We start with a discussion of the current views on the state and properties of interfaces stabilized by animal-based proteins, and present an overview of recent results on the microstructure and properties of interfaces stabilized by several plant-based proteins. These insights provide possible strategies to improve plant-protein functionality with respect to foam and emulsion stabilization, several of which will be discussed. Microstructure and properties of proteinstabilized interfaces In multiphase food products, based on foams and emulsions, the surface rheological properties often play an www.sciencedirect.com

Food chemistry and biochemistry
Loveday SM
20. Winter HH
Findings
45. Loveday SM
Full Text
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