Purification and Characterization of Glycerol Dehydratase from Lactobacillus reuteri

Author:

Talarico Todd L.1,Dobrogosz Walter J.1

Affiliation:

1. Department of Microbiology, North Carolina State University, Raleigh, North Carolina 27695

Abstract

A coenzyme B 12 -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 B 12 were in the millimolar and the submicromolar range, respectively.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Reference16 articles.

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5. Dobrogosz W. J. I. A. Casas G. A. Pagano T. L. Talarico B.-M. Sjoberg and K. Karlsson. 1989. Lactobacillus reuteri and the enteric microbiota. In R. Grub T. Midtvedt and E. Norin (ed.) The regulatory and protective role of the normal flora. A Wenner-Gren International Symposium. The Macmillan Press Ltd. London.

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