The Science of Alt Protein: Plant protein colloidal state and techno-functionality
Arno Wouters
Associate Professor
KU Leuven
Event description
Globular plant proteins generally lack in their techno-functionalities, such as foaming, gelling, and emulsifying, as compared to animal proteins. This relates to their inherent structural characteristics, but also to the fact that commercially available plant protein ingredients contain heavily aggregated proteins. In addition, it has recently become clear that globular plant proteins tend to self-assemble into specific colloidal states depending on the environmental conditions, such as changing pH and salt concentration. The implications of such supramolecular structural organization for the functionalities of the proteins in food systems remain unclear.
In this presentation from Dr. Arno Wouters, several examples will be given regarding the self-assembly of globular plant proteins into different aggregation states, depending on prior processing or altered environmental conditions. The link to protein techno-functionality will be made as well. In the end, Dr. Wouters will demonstrate the importance of considering protein colloidal state when utilizing globular plant proteins as functional food ingredients.
Meet the speaker
Arno Wouters, PhD
ASSOCIATE PROFESSOR
LABORATORY OF FOOD CHEMISTRY AND BIOCHEMISTRY, KU LEUVEN
Arno Wouters is an associate professor in Food Chemistry at the Laboratory of Food Chemistry and Biochemistry at KU Leuven, Belgium. Arno is particularly interested in exploiting the potential of various plant protein sources for structuring food. His research focuses on establishing structure-function relationships for cereal and legume proteins. An important focus point is the relationship between protein colloidal state, dictated by prior protein isolation, varying environmental conditions and targeted modification, and the implications thereof for protein functionality. Another focus point is mechanistically studying protein functionalities, with particular emphasis on protein foaming, at different length scales.
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