title: The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions.
abstract: The aggregation of proteins is of fundamental relevance in a number of daily phenomena, as important and diverse as blood coagulation, medical diseases, or cooking an egg in the kitchen. Colloidal food systems, in particular, are examples that have great significance for protein aggregation, not only for their importance and implications, which touches on everyday life, but also because they allow the limits of the colloidal science analogy to be tested in a much broader window of conditions, such as pH, ionic strength, concentration and temperature. Thus, studying the aggregation and self-assembly of proteins in foods challenges our understanding of these complex systems from both the molecular and statistical physics perspectives. Last but not least, food offers a unique playground to study the aggregation of proteins in three, two and one dimensions, that is to say, in the bulk, at air/water and oil/water interfaces and in protein fibrillation phenomena. In this review we will tackle this very ambitious task in order to discuss the current understanding of protein aggregation in the framework of foods, which is possibly one of the broadest contexts, yet is of tremendous daily relevance.
authors: ETH Zurich, Food and Soft Materials Science, Department of Health Science and Technology, Institute of Food, Nutrition and Health, Schmelzbergstrasse 9, LFO E23, 8092 Zürich, Switzerland. raffaele.mezzenga@hest.ethz.ch
authors: Raffaele
authors: R
authors: Mezzenga
authors: Peter
authors: P
authors: Fischer
mesh_terms: D000818:Animals; D004044:Dietary Proteins; D006801:Humans; D006868:Hydrolysis; D044367:Phase Transition; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D058767:Protein Unfolding
chemical_list: D004044:Dietary Proteins