Establishing the Mixing and Solubilization Behavior of Pork Meat and Potato Proteins at Acidic to Neutral pH

Technofunctional properties of plant proteins deviate from those of animal-derived proteins and make their combination in foods challenging. In this work, proteins from a soluble, low-molecular weight potato protein fraction (<24 kDa) and pork meat were salt-solubilized (1.8 wt % NaCl) and mixed in a 50:50 (v/v) ratio to assess their miscibility at three different pH values. The mixture maintained high solubility at pH 7.0 irrespective of the proximity to the pI of potato proteins (pH 6.7 +/- 0.1) and exhibited lower surface hydrophobicity (174) than individual potato (608) and meat (278) protein fractions. In contrast, mixtures were visible as large heteroprotein particles of dense, irregular shape at pH 5.0 and 3.0. These particles deviated from highly regular, anisotropic aggregates in pure meat dispersions or solutions of potato proteins that were aggregate-free and was related to modulations of electrostatic and hydrophobic meat-potato protein interactions. This study presents the first insights into and a basic understanding of the combinational effects of meat and plant proteins and is useful for further compatibility studies and the development of hybrid products.