1. Phase partitioning nature, interaction forces and thermodynamic parameters of triton X-100 and bovine serum albumin mixture: impacts of the composition of Na-salt.
- Author
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Akbor, Aysha Bente, Islam, Md. Rafikul, Bahajjaj, Aboud Ahmed Awadh, Anis-Ul-Haque, K. M., Goni, Md Abdul, Hoque, Md. Anamul, and Islam, D. M. Shafiqul
- Subjects
TRITON X-100 ,SERUM albumin ,PHASE partition ,GIBBS' free energy ,GLOBULAR proteins - Abstract
Herein, the assessment of interactions between a non-ionic surfactant (NIS) triton X-100 (TNX-100) and a globular protein bovine serum albumin (BSA) was explored through the determination of clouding nature in aqueous solution of sodium salts (Na-salts). Sodium chloride (NaCl), sodium acetate (NaOAc), sodium carbonate (Na
2 CO3 ), sodium oxalate (Na2 Oxal), sodium sulphate (Na2 SO4 ), and sodium phosphate (Na3 PO4 ) have been chosen to assess their impacts on the clouding nature of TNX-100 + BSA mixture. The estimated cloud point (CP) values were noticed to be lowered with the enhancement of [Na-salts]. The lessening of CP values has been explained by the salting out effect of anions. The calculated standard Gibbs free energy change ( $ \Delta G_c^o $ Δ G c o ) was positive at all examined conditions which illustrates the nonspontaneity of phase change. The standard enthalpy ( $ \Delta H_c^o $ Δ H c o ) and entropy ( $ \Delta S_c^o $ Δ S c o ) changes exhibited negative values at low contents of aq. Na-salts and positive values at high aq. Na-salts content. These consequences illustrate the presence of electrostatic interactions at low Na-salts concentration and hydrophobic interactions at high Na-salts concentration. Furthermore, enthalpy-entropy parameters were successfully computed and explained with proper clarification. [ABSTRACT FROM AUTHOR]- Published
- 2024
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