Emulsifying salts cause protein quaternary structures to dissociate, promoting stability and functionality in protein-fortified beverages. As the plant-based alternative industry’s $22.6 billion value will double by 2040, improving protein functionality becomes essential. A Continuous Monitoring Prototype was designed to monitor the effects of ranging salt concentrations and temperatures on turbidity and rheological properties of almond-protein dispersions. Higher salt concentrations disrupted quaternary protein structure, as fluorescence increased, turbidity decreased, and increasing monomeric units appeared via electrophoresis.