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Isolation and stability of ribitol dehydrogenase a possible new zinc enzyme from mycobacterium butyricum

, : Isolation and stability of ribitol dehydrogenase a possible new zinc enzyme from mycobacterium butyricum. Acta Microbiologica Polonica 40(1-2): 99-100

Various Mycobacterium species were tested for activity of polyhydric alcohol dehydrogenases (ribitol, sorbitol and mannitol dehydrogenases), and for their response to zinc content in the growth medium. Mycobacterium butyricum was chosen as a good source of well-responded ribitol dyhydrogenase. As the enzyme was suggested to be a new zinc enzyme, it was purified and its stability in various conditions was studied. The enzyme was purified about 90-times with 20% of recovery. It was near the homogeneity, as checked by polyacrylamide gel electrophoresis. Among compounds tested, glycerol and ammonium sulphate protected the enzyme best during the storage in the frozen state, or incubation at elevated temperature (


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