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The molecular non-covalent interaction often originates from the electrostatic attraction and accords with the Langmuir isothermal adsorption. The sodium dodecyl benzene sulfonate (SDBS)-polychrome blue B (PCB)-protein [bovine serum albumin (BSA), ovalbumin (OVA) and myoglobin (MB)] ternary reaction has been investigated at pH 3.88. Protein to replace PCB from the PCB-SDBS binding product was used to characterize the assembly of an invisible-spectral compound, SDBS, on proteins by measuring the variation of PCB light-absorption by the micro- surface adsorption-spectral correction (MSASC) technique. The effect of ionic strength and temperature on the ag- gregation was studied. Results showed that the aggregates SDBS92?BSA, SDBS58?OVA and SDBS15?MB at 30 ℃ and SDBS83?BSA, SDBS39?OVA and SDBS10?MB at 50 ℃ are formed.
The molecular non-covalent interaction often originates from the electrostatic attraction and accords with the Langmuir isothermal adsorption. The sodium dodecyl benzene sulfonate (SDBS) -polychrome blue B (PCB) -protein [bovine serum albumin (BSA), ovalbumin (OVA) and myoglobin (MB)] ternary reaction has been investigated at pH 3.88. Protein to replace PCB from the PCB-SDBS binding product was used to characterize the assembly of an invisible-spectral compound, SDBS, on proteins by measuring the variation of PCB light- absorption by the micro-surface adsorption-spectral correction (MSASC) technique. The effect of ionic strength and temperature on the ag- greation was studied. Results showed that the aggregates SDBS92® BSA, SDBS58® OVA and SDBS15® MB at 30 ° C and SDBS83? BSA, SDBS39? OVA and SDBS10? MB at 50C are formed.