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Aspergillus awamori catalytic (residues 1-470) and starch binding domains (residues 508-616) were prepared by directed mutagenesis and purified to homogeneity as judged by amino acid sequencing and composition anaJysis. Both sedimentation equilibrium experiments and MALDI-TOF spectra of GA470 and the SBD show molecular masses of 56.2 and 12.5 kDa, respectively, and carbohydrate contents of approximately 12% and 5%, respectively. GC/MS studies on the SBD and its 161-162 Da mass unit difference in MALDI-TOF spectra indicates presence of mannose residues. The thermal unfolding transition for GA470 is calorimetrically irreversible at pH 7.5, whereas that of SBD is completely reversible at pH 6.0-8.0, as measured by circular dichroism. At pH 7.5, GA470 unfolds with a high degree of cooperativity, producing a single sharp aisymmetric endotherm in DSC with Tm of 60.9°C and AH of 410 kcaJ/mol. In contrast, at the same

Biophysical studies of catalytic and starch binding domains of wild-type and mutant glucoamylases from Aspergillus awamori