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Propanediol-1,2-hehydratase and metabolism of glycerol of Lactobacillus brevis

: Radler, F.; Schütz, H.

Archives of microbiology (1984), Nr.139, S.366-370
ISSN: 0302-8933
Fraunhofer IFU; 2002 in Helmholtz-Gesellschaft integriert
lactic acid bacteria; Lactobacillus brevis

While most strains of heterofermentative lactobacilli and strains of Leuconostoc species contained only traces of a dehydratase reacting with glycerol or propanediol-1,2, three strains of Lactobacillus brevis and one strain of L.buchneri that metabolized glycerol readily in the presence of glucose, contained propanediol-1,2 dehydratase (EC This cobamide requiring enzyme from L.brevis B 18 was partially purified. It reacts with the substrates propanediol-1,2, glycerol and ethanediol-1,2 with the relative activities of about 3:2:1. This ratio remained unchanged throughout the purification procedure. The substrate affinities were measured: propanediol-1,2 K sub m = 0.6 mM, glycerol K sub m = 4 mM, ethanediol-1,2 K sub m = 5.3 mM coenzyme B12 (substrate glycerol) K sub m = 0.007 mM. The activity of the dehydratase was promoted by potassium or ammonium ions and inhibited by sodium, lithium, magnesium or specially manganese. The apparent molecular weight of propanediol-1, dehydrat ase was determined as M sub r = 180,000. (IFU)