| Abstract: | Using the pH-jump (neutral to above 11) for Tyr-OH ionization as a probe, two glucoamylases from Rhizopus niveus and Rhizopus delemar were found to be caused the change in conformation, which is in a kinetically single step. The pH titration at pHs below 12 was carried out on a multidimensional correlation spectrophotometer. Correlations among the spectrophotometric properties: fluorescence, absorption and circular dichroism are almost identical for the two enzymes. These results suggest that conformational characteristics of the niveus enzyme is almost the same as that of the delemar one. |
