抄録
In order to investigate the subsite structure of the glucoamylase from Asp. saitoi, kinetic parameters (Km and ko values) of the enzyme for various sizes of maltooligosaccharide substrates were measured. The subsite affinities of this enzyme were calculated from the kinetic parameters and compared with those of the Rhizopus sp. glucoamylase, which differs from the Asp. saitoi glucoamylase in molecular weight, pI and of course, origin. The characteristic features of the subsite affinities of glucoamylase from Rhizopus, reported by Hiromi and his colleagues [Agric. Biol. Chem., 47, 573 (1983); Biochim. Biophys. Acta, 302, 362 (1973)], were retained in the glucoamylase from Asp. saitoi. However, the kint value for the glucoamylase from Asp. saitoi was about half of that for the enzyme from Rhizopus sp.
