Ohmic heating as an innovative strategy to modulate protein fibrillation

Abstract

The integration of emerging technologies and innovative functionalization techniques presents a promising strategy to address contemporary challenges involving dietary shifts, environmental and ethical issues associated with traditional protein consumption. Amyloid fibrils (AFs) are on the spotlight since they can deliver innovative techno-functional properties in food systems. Conventional proteins such egg white proteins (EWP) have demonstrated to form AFs under food processing conditions. Vegetable proteins, such as pea protein (PP) are pointed as a potential alternative for EWP but have limited techno-functionality. In this sense, ohmic heating (OH) was used for the first time as an assisting technology in protein fibrillation of EWP and PP. OH treatment of EWP dispersions induced the formation of AFs with distinct aggregation patterns and shorter length (ca. 65 nm) than the ones obtained by conventional heating (ca. 134 nm). Regarding PP fibrillation, the results point towards to a structural rearrangement of the existing fibrils, particularly when OH is applied. These findings open a perspective for using OH for tailoring food protein fibril formation and innovative food protein applications. Ultimately, this work underlines that, as any other functionalization strategy, plant protein fibrillation is more challenging than animal protein fibrillation. Industrial relevanceResearch on food protein AFs formation has increased because of its potential to deliver specific techno-functionality (e.g., viscosity, gelling, emulsifying and foaming properties) in food systems. Recent reports show that animal and plant protein can fibrillate under food processing relevant conditions. In line with this, the use of emerging processing technologies such as OH to induce fibril formation is of high interest because of its ability to modulate protein structures. We here demonstrated that OH can be used under food processing relevant conditions for tailoring food protein fibril formation which can lead to novel food protein applications.