Subsite Affinity of a Glucoamylase from Aspergillus saitoi

概要

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In order to investigate the subsite structure of the glucoamylase from Asp. saitoi, kinetic parameters (K_m and k_o 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 k_<int> value for the glucoamylase from Asp. saitoi was about half of that for the enzyme from Rhizopus sp.
社団法人日本薬学会の論文
1984-02-25