Abstract
The interaction between α ‐amylase from Bacillus subtilis and cetyltrimethylammonium bromide (CTAB) has been investigated at various temperature conditions using fluorescence and circular dichroism (CD) spectroscopic methods. Fluorescence data revealed that the fluorescence quenching of α ‐amylase by CTAB is the result of complex formation between CTAB and α ‐amylase. The thermodynamic analysis on the binding interaction data shows that the interactions are strongly exothermic (Δ H°=−17.92 kJ mol −1) accompanied with increase in entropy (Δ S° between 109 to 135 J mol −1 K −1). Thus the binding of CTAB to α-amylase is both enthalpic and entropic driven, which represent the predominate role of both electrostatic and hydrophobic interactions in complex formation process. The values of 2.17×10 −3 M −1 and 1.30 have been obtained from associative binding constant ( K a) and stoichiometry of binding number ( n), from analysis of fluorescence data, respectively. Circular dichroism spectra showed the substantial conformational changes in secondary structure of α ‐amylase due to binding of CTAB, which represents the complete destruction of both secondary and tertiary structure of α-amylase by CTAB.
Published Version
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