Heteroprotein Complex Coacervate Based on β-Conglycinin and Lysozyme: Dynamic Protein Exchange, Thermodynamic Mechanism, and Lysozyme Activity

Abstract

Heteroprotein complex coacervate (HPCC) is a liquid-like protein concentrate produced by liquid-liquid phase separation. We revealed the protein dynamic exchange and thermodynamic mechanism of β-conglycinin/lysozyme coacervate, and clarified the effect of HPCC on protein structure and activity. β-conglycinin and lysozyme assembled into coacervate at pH 5.75-6.5 and assembled into amorphous precipitates at higher pH. As the pH dropped from 8 to 6, the number of binding sites of the complex decreased in half, and the desolvation degree corresponding to the entropy gain was greatly reduced, conducing to the formation of coacervates rather than precipitates. The coacervates achieved the unique dynamic exchange by exchanging proteins with the diluted phase, making the uniform distribution of proteins in coacervates. The lysozyme activity was completely retained in β-conglycinin/lysozyme coacervates. These results proved that β-conglycinin-based heteroprotein complex coacervate is a feasible method to encapsulate and enrich active proteins in a purely aqueous environment.