Physicochemical studies of globular proteins—Bovine serum albumin,egg albumin,and lysozyme—In some aqueous iodide salts solutions of IA group and cetyltrimethyl ammonium bromide systems

Densities (ρ, kg m^?3), and viscosities (η, 0.1 kg m^?1 s^?1) of Bovine Serum Albumin (BSA), Egg Albumin, and Lysozyme in aqueous iodide salts of lithium, sodium, and potassium, along with cationic surfactant‐cetyltrimethyl ammonium bromide (CTAB) were measured at a temperature of 303.15 K. The 0.0010–0.0018 g %, w/v of each protein at an interval of 0.0002 mol L^?1 in 0.2, 0.4, and 0.8 millimol L^?1 of salt and CTAB are studied. Data are used for apparent molar volumes (V_?, 10^?6 m³ mol^?1) and intrinsic viscosities (η], dL kg^?1), respectively. Data are regressed and extrapolated to zero concentrations for ρ⁰, η⁰, and limiting values and S_d, S_η and S_V corresponding slopes for protein–salt structural interactions. With size of cations, the densities decrease as CTAB > LiI > NaI > KI and increase with salts concentrations, with salts the densities are as Lysozyme > BSA > Egg Albumin, viscosities and V_? as BSA > Egg–Albumin > Lysozyme. The ρ and η values with CTAB higher and η] are lower and converse at around 0.4 mmol L^?1 salt and is effective for greater stability of proteins. The η] in CTAB are higher than other salts and decreases with size of cations with stronger intermolecular forces. © 2008 Wiley Periodicals, Inc. J Appl Polym Sci, 2008