Thermal Unfolding of Mutant Forms C509G and C509S of Starch Binding Domain-Fragment of Aspergillus niger Glucoamylase.
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概要
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Thermal unfolding of the starch binding domain-fragment (SBDF; Thr507-Arg616) of Aspergillus niger glucoamylase and its mutant forms, Cys509→Gly (C509G) and Cys509→Ser (C509S), were investigated by adiabatic differential scanning calorimetry (DSC) to analyze the effect of the disulfide bridge (Cys509-Cys604) on thermal stability of SBDF. All the proteins, the wild type SBDF (WT), C509G, and C509S, showed single endothermic peak, and the peak temperature of the mutant proteins was lower than that of WT by about 9 degree. The apparent destabilization in the standard Gibbs free energy change caused by these mutations was 8-9 J mol-1 at the temperature of half-denaturation of the WT protein (52°C). It was suggested that a part of each protein forms dimer in the native state.
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