Complex Coacervation and Precipitation Between Soluble Pea Proteins and Apple Pectin

Abstract Complex formation (leading to either coacervation or precipitation) offers a tool to generate plant-based novel food structures and textures. This study investigated the formation of complexes between soluble pea proteins and apple pectin upon varying the protein-to-pectin ratio (r = 2:1 to 10:1), pH (3–7), and temperature (25 and 85 °C) with a total biopolymer concentration set to 1% (w/w). The results showed that predominantly soluble biopolymer complexes were formed at pH 5, and at low ratio (r = 2:1), whereas lowering the pH to more acidic condition, and to higher ratios (r = 4:1–10:1) induced the formation of more insoluble biopolymer complexes. In general, the mean particle sizes of the biopolymer complexes ranged between approximately 20 and 100 μm. Upon heating to 85 °C, the amount of insoluble biopolymer complexes increased at pH 3–5 at all ratios, except at r = 2:1. In addition, the complex sizes became somewhat larger at r = 2:1 to 6:1 upon heat treatment, whereas only trivial size changes were observed at higher ratios (r = 8:1 to 10:1). Overall, electrostatic and hydrophobic interactions played a major role in the complex formation between the soluble pea proteins and apple pectin. These findings are important for designing solely plant-based food structures.