There is a growing demand for drinks and shakes containing high dairy protein contents. The effect of ionic environments in complex protein quaternary structures (e.g., casein micelles), can only be transformed into technological applications using an empirical approach where a broad set of environmental conditions are tested (e.g., emulsifying salt, salt concentration, casein concentration, temperature, and pH). For this purpose, a prototype protein characterization unit (PCU) was designed and assembled to autonomously look thorough a wide range of sample conditions rapidly to generate a clear picture of how the parameters effect salt-protein interactions. The PCU was tested for environmental conditions including pH (6.0, 6.5 and 7.0), temperature (5, 15, 25, 35, 45 and 55°C), salt concentration (0–200 mM), exposure time (0–240 s), and measuring absorbance (400 nm), fluorescence (excitation: 380 nm; emission: 470 nm) and viscosity (gauge pressure) of the liquid systems containing milk proteins and salts. The absorbance values were then interpreted as micelle dissociation through the critical salt concentration (C*) using an exponential decay model [absorbance = absorbance(c = 0)×Exp(−C/C*); where C is the salt concentration]. Sodium and potassium citrates were effective in dissociating casein micelles with critical concentrations leading to micellar dissociation ~2 to 4 mM. An increase in temperature shortened the required exposure time for dissociation and decreased system viscosity by nearly 50%. Increase in pH however, increased the critical concentration values from nearly 5 mM at pH = 6.0 to 7 mM at pH = 7.0. Furthermore, tartrates were also able to deliver the similar effects but at higher concentrations (~15–50 mM). Effects of anions were significantly more profound compared with cations where the average initial critical concentration for citrates was ~3 to 4 mM and for tartrates was ~20 mM. In summary, the mapping of protein-salt interactions will allow for better understanding of protein functionality toward liquid system containing high protein contents.