Molecular identification of Lactobacillus hilgardii and genetic relatedness with Lactobacillus brevis
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منابع مشابه
Molecular identification of Lactobacillus hilgardii and genetic relatedness with Lactobacillus brevis.
Conventional phenotypic methods lead to misidentification of the lactic acid bacteria Lactobacillus hilgardii and Lactobacillus brevis. Random amplified polymorphic DNA (RAPD) and repetitive element PCR (REP-PCR) techniques were developed for a molecular study of these two species. The taxonomic relationships were confirmed by analysis of the ribosomal operon. Amplified DNA fragments were chose...
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In the cofermentation of glycerol with a sugar by Lactobacillus brevis and Lactobacillus buchneri, a 1,3-propanediol:NAD+ oxidoreductase provides an additional method of NADH disposal. The enzyme has been purified from both L. brevis B22 and L. buchneri B190 and found to have properties very similar to those reported for the enzyme from Klebsiella pneumoniae. The enzymes required Mn2+ and are p...
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The pyruvate metabolism of LactobaciUus plantarum and Latobacillus arabino8su, which according to Bergey (1948) are identical organisms, has been studied by Rowatt (1951) and Nossal (1952). Both these homofermentative lactobacilli were shown to form 3-hydroxybutan-2-one (acetoin) as the main product of their pyruvate metabolism. No one appears to have studied the metabolism of pyruvate by any o...
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Certain heterofermentative lactic acid bacteria often encountered in food and beverage fermentations are able to utilize the uronic acids as a sole carbon source for energy (J. R. Stamer and B. O. Stoyla, Bacteriol. Proc., p. 1, 1967). Although the mechanisms of uronic acid degradation by gram-negative or phytopathogenic microorganisms have been extensively studied (W. J. Payne and R. A. McRori...
متن کاملMolecular cloning and functional expression in lactobacillus plantarum 80 of xylT, encoding the D-xylose-H+ symporter of Lactobacillus brevis.
A 3-kb region, located downstream of the Lactobacillus brevis xylA gene (encoding D-xylose isomerase), was cloned in Escherichia coli TG1. The sequence revealed two open reading frames which could code for the D-xylulose kinase gene (xylB) and another gene (xylT) encoding a protein of 457 amino acids with significant similarity to the D-xylose-H+ symporters of E. coli, XylE (57%), and Bacillus ...
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ژورنال
عنوان ژورنال: International Journal of Systematic and Evolutionary Microbiology
سال: 1999
ISSN: 1466-5026,1466-5034
DOI: 10.1099/00207713-49-3-1075