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The thermodynamic effects of the disulfide bond of the fragment protein of the starch-binding domain of Aspergillus niger glucoamylase was investigated by measuring the thermal unfolding of the wild-type protein and its two mutant forms, Cys3Gly/Cys98Gly and Cys-3Ser/Cys98Ser. The circular dichroism spectra and the thermodynamic parameters of binding with -cyclodextrin at 25 C suggested that the native structures of the three proteins are essentially the same. Differential scanning calorimetrydoi:10.1271/bbb.70098 pmid:17587686 fatcat:hvxok5myqvcl5lcfdrniadi7dy