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- W2022874937 abstract "Abstract 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 ϕ , 10 −6 m 3 mol −1 ) and intrinsic viscosities ([η], dL kg −1 ), respectively. Data are regressed and extrapolated to zero concentrations for ρ 0 , η 0 , and $$V_{phi}^{0} $$ 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 ϕ 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" @default.
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- W2022874937 date "2008-08-18" @default.
- W2022874937 modified "2023-09-30" @default.
- W2022874937 title "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" @default.
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- W2022874937 doi "https://doi.org/10.1002/app.26733" @default.
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