ISSN:
1432-072X
Keywords:
Lactic acid bacteria
;
Lactobacillus brevis
;
Propanediol-1,2-dehydratase
;
Propanediol-1,2
;
Glycerol
;
Ethanediol-1,2
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract 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 4.2.1.28). 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 m=0.6 mM, glycerol K m=4 mM, ethanediol-1,2 K m=5.3 mM coenzyme B12 (substrate glycerol) K 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-1,2 dehydratase was determined as Mr=180,000.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00408381
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