Abstract
The enthalpies of interaction between Aspergillus niger catalase and sodium n-dodecyl sulphate (SDS) in aqueous solutions of pH 3.2, 6.4 and 10.0 have been measured over a range of SDS concentrations by microcalorimetry at 25°C. Binding isotherms have been obtained by equilibrium dialysis and interpreted in terms of theoretical models (Hill equation and Wyman binding potential). The data are compared with corresponding data for bovine catalase. The enthalpies of interaction of Aspergillus niger and bovine catalase are similar at pH 3.2 and 10.0 but significantly different at pH 6.4 where it has been shown that SDS activates Aspergillus niger catalase but denatures bovine catalase.
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