Grant: Discovery Grants Program - Individual

Developing innovative processes and products from our rich array of plant protein resources is vital to Canada's economy and to our quality of life. A key attribute for a food protein is its aeration capacity, often enhanced by manipulating thermal processing to induce functional changes in the protein. Investigation of the structural basis for this functionality is challenging because aerated systems are fragile, factors governing protein conformation are still unresolved, and we have a limited understanding of how protein-stabilized bubbles interact with other components such as fibre particles. Based on past experience and high-precision instrumentation, I and my team are in a unique position to address these challenges and to discover how process history, fundamental thermodynamic transitions, and aerated food structures are interrelated so that we can optimize processing to create palatable and healthy food products. I propose to:1) Demonstrate how specific thermodynamic parameters define thermal process windows for proteins to improve their functionality2) Subject proteins to defined thermal processes and evaluate how the structures of aerated foods made from them are improved3) Determine how the dynamics of aerated foods created from protein solutions are altered as particles are incorporated. Highly precise measurements of protein solution density and ultrasonic velocity will allow fundamental thermodynamic parameters to be defined for purified and commercial proteins. Characterizing the temperature dependence of these parameters will identify temperature ranges to establish thermal process conditions for improved protein functionality. Kinetic studies of changes in functionality during thermal treatments will establish practical processes for industrial uptake of research outcomes. Microscopy, electrical resistivity, ultrasonic profiling and shear rheology will provide a thorough description of aerated food structures created from processed proteins. Well-defined particles of varying hydrophobicity will be model ingredients to investigate how bubble stability is challenged by food components. Anticipated outcomes are: 1) Definition of the conformational changes in proteins that improve their functionality in aerated foods2) A thorough characterization of the capacity of plant proteins to stabilize aerated structures, providing a roadmap for developing valuable functional ingredients3) Quantification of the extent to which the properties of commercial plant proteins depend on process history4) Quantification of the critical limits of particle loading on bubble stability to provide insights on optimized nutrient loading strategies5) Curiosity-inspired professionals trained in critical thinking and advanced laboratory techniques to drive innovation in the food industry and in academic investigations of soft materials.