Purification and characterization of glycerol dehydratase from Lactobacillus reuteri

Abstract

A coenzyme B12-dependent glycerol dehydratase from Lactobacillus reuteri has been purified and characterized. The dehydratase has a molecular weight of approximately 200,000, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis yielded a single major band with a molecular weight of 52,000. K(m) values for substrates and coenzyme B12 were in the millimolar and the submicromolar range, respectively.