High pressure homogenization shapes the techno-functionalities and digestibility of pea proteins

• High pressure homogenization (HPH) induces structural modifications of pea proteins. • Pea proteins unfold with HPH intensity up to 70 MPa for 3 passes. • Pea proteins aggregate with HPH intensity above 100 MPa. • Solubility and oil holding capacity increase with HPH-induced unfolding. • Protein aggregation upon more severe HPH conditions reduces functionality. • HPH does not impair pea protein gastrointestinal fate. This work aimed to design high-pressure homogenization process able to improve pea protein functionalities. To this purpose, pea protein concentrate suspensions (5% w/w) were homogenised at increasing pressures (up to 150 MPa) and number of passes (up to 3). Samples were analysed for protein structural and conformational modifications, technological functionalities, and in vitro digestibility. As HPH intensity increased, protein unfolding was favoured, leading to solubility and oil holding capacity increase and generating emulsions with rheological properties shifting from liquid-like pseudo-plastic behaviours to gel-like plastic characteristics. The best performing HPH treatment included 3 passes at 70 MPa and leaded to a novel plant-protein based ingredient with improved techno-functionalities and digestibility comparable to original pea proteins. A further increase in HPH intensity at 150 MPa for 3 passes caused protein aggregation with detrimental effects on technological functionalities and digestibility. Results demonstrate the remarkable effect of HPH in tailoring protein functionalities, highlighting the need of a process design step to define HPH process parameters allowing to generate novel high-added value.