The functionality of caseins in food systems depends on their solubili
ty. The solubilities of whole casein, alphas1-casein, beta-casein, and
dephosphorylated whole casein were measured as the pH was adjusted fr
om 7 to 2 with HCl. When NaCl was added before PH adjustment, solubili
ties of whole casein at pH 2.5 decreased by 25, 40, 85, and 98% at NaC
l concentrations of .01, .05, .1 and .2 M, respectively. Likewise, sol
ubilities of dephosphorylated whole casein decreased by 50%, alpha(s)1
-casein by 30%, and beta-casein by 90% in . 1 M NaCl. When .01 and .05
M NaCl were added to whole casein solutions after pH adjustment, effe
cts on solubility were slight; however, . 1 and .2 M NaCl decreased so
lubility by 30 and 95%, respectively. When NaCl was added to casein so
lutions, pH decreased if the original solution was above the isoionic
point, indicating Na ion binding; however, at pH between 5 and 3, the
pH of the solution increased when NaCl was added. The pH shift upon ad
dition of NaCl to dephosphorylated casein was less than with native ca
seins, suggesting that Na ion binding by phosphate and acid groups occ
urred in casein. Although NaCl is commonly used in food processing, th
ese unusual solubility effects should be considered when NaCl is used
with casein.