Plant-based meat analogues: their protein structure and digestibility

Plant proteins have gained attention as a more sustainable protein and thus, used in food products such as plant-based meat analogues (PBMAs). Food processing methods can alter the native structure of proteins and improve techno-functional properties of plant proteins. Resulting structural change can affect protein digestibility and bioactive properties of the peptides produced. In this study, we investigated how food processing alters the native structure of plant proteins in plant-based meat analogues on the Canadian market. We also evaluated the effect of protein structural changes on plant protein digestibility. Two commercial traditional and novo PBMAs on the Canadian market were obtained. Samples were freeze-dried and subjected to alkaline solubilization and dialysis to extract the proteins. Pea and soy proteins were used as controls. The particle size distribution, surface hydrophobicity, and protein structure were evaluated. The digestibility of the proteins in the PBMAs and the peptides released after digestion will also be evaluated. The particle size distribution of novo products was more heterogenous, ranging from 100—2000 nm. Surface hydrophobicity of the novo products was about three-fold lower than the traditional products and the control. This study shows that PBMA processing conditions alter the surface properties of the plant proteins used.