Isolation and Characterization f a New L - SorboselL - Sorbosone Dehydrogenase
نویسنده
چکیده
two subumits with molecular weights of 64,500 and 62,500. As its prosthetic group, non-covalelltly bound PQQ was foHnd. The dye-linked spectrophotemetric enzyme assay showed that the optimum enzyme activity occurred in the pH range about 7.0-9.0, and the ellzyme activity was inhibited by EDTA er EGTA. The enzyme showed extremely broEd substrate specificity for primary and secondary alcohols, aldehydes, aldoses, ketoses, and other sugar alcohols, but not for methanol or formaldehyde. The cytochrome c obtained from the soluble fraction ef this strain was found te act as a physiological electron acceptor of the enzyme.
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