Abstract:

Diol dehydratase of Lactobacillus diolivorans was purified by ammonium sulfate precipitation and gel filtration chromatography.The molecular mass of the native complex was estimated to be 200×10³ by nondenaturing polyacrylamide gel electrophoresis.Three main bands were present after SDS-PAGE with molecular masses of 62×10³, 35×10³ and 22×10³, respectively. K_m for the three main substrates were 1.3 mmol·L^-1 for 1,2-propanediol，5.8 mmol·L^-1 for glycerol and 10.3 mmol·L^-1 for 1,2-ethanediol.K_m for adenosylcobalamin coenzyme was 1.5 μmol·L^-1, which was required for the enzyme catalysis.The optimal reaction conditions of the enzyme were pH 8.6 and 37℃.