Role of ionic strength in biochemical properties of soluble fish proteins isolated from cryoprotected Pacific whiting mince

Biochemical characteristics of Pacific whiting muscle proteins extracted at acidic, neutral and alkaline conditions were investigated as affected by various ionic strength levels. The protein solubility at pH 4 declined, as NaCl was added up to 200 mM, due to protein aggregation through hydrophobic interactions. In contrast, at pH 7 and 10, solubility increased as NaCl was added up to 400 mM after which it remained constant. Changes in total SH content and S(o)were highly related to the different molecular weight distributions of the soluble proteins. At pH 4, myosin heavy chain (MHC) was soluble as evidenced by the presence of MHC in the soluble fraction, even though degraded molecules were shown at IS 10-100 mM, and became completely insoluble at IS >= 150 mM. At pH 10, the density of the MHC band gradually increased as IS increased and the formation of high MW polymers was observed at IS >= 150 mM.