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. 2012 May;78(9):3480-3.
doi: 10.1128/AEM.00058-12. Epub 2012 Feb 17.

Relative catalytic efficiency of ldhL- and ldhD-encoded products is crucial for optical purity of lactic acid produced by lactobacillus strains

Zhaojuan Zheng  1 , Binbin Sheng, Cuiqing Ma, Haiwei Zhang, Chao Gao, Fei Su, Ping Xu
Affiliations

Relative catalytic efficiency of ldhL- and ldhD-encoded products is crucial for optical purity of lactic acid produced by lactobacillus strains

Zhaojuan Zheng et al. Appl Environ Microbiol. 2012 May.

Abstract

NAD-dependent l- and d-lactate dehydrogenases coexist in Lactobacillus genomes and may convert pyruvic acid into l-lactic acid and d-lactic acid, respectively. Our findings suggest that the relative catalytic efficiencies of ldhL- and ldhD-encoded products are crucial for the optical purity of lactic acid produced by Lactobacillus strains.

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Figures

Fig 1
Fig 1
Determination of the relative transcriptional levels of ldhD and ldhL by using qPCR. Error bars represent the standard deviations of the means of three independent experiments.
Fig 2
Fig 2
NJ tree based on l-nLDH amino acid sequences from various Lactobacillus strains, rooted with Xylanimonas cellulosilytica. Numbers at nodes indicate the percentage of NJ bootstrap analyses with 1,000 replicates. The scale bar indicates the level of amino acid sequence divergence.
Fig 3
Fig 3
NJ tree based on d-nLDH amino acid sequences from various Lactobacillus strains, rooted with E. coli. Numbers at nodes indicate the percentage of NJ bootstrap analyses with 1,000 replicates. The scale bar indicates the level of amino acid sequence divergence.
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