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N Sauvageot

Publications and source records attributed to N Sauvageot.

2 recordsLinked to original sources
PubMed2005

Maltose utilization in Enterococcus faecalis.

AIMS: The aim of this research was to characterize the metabolic pathway for maltose utilization in Enterococcus faecalis. METHODS AND RESULTS: Screening a library of Enterococcus faecalis insertional mutants allowed the isolation of mutants affected in maltose utilization. Genetic analysis of the insertion loci revealed insertions in neighbour genes encoding an EII component of a phosphotransferase system (PTS) transporter (malT) and a maltose phosphorylase homologue (malP). The malP gene forms part of an operon which also includes genes encoding a phosphoglucomutase (malB), a mutarotase (aldose 1-epimerase) (malM) and a transcriptional regulator (malR). Analysis of (14)C-labelled carbohydrates uptake revealed that more than 97% of maltose enters the cells by the PTS transporter MalT. CONCLUSIONS: Both experimental data and genetic organization of the malPBMR operon strongly suggest that in Enterococcus faecalis, maltose enters using a PTS, leaving maltose-6-phosphate inside the cells which is hydrolysed by a maltose phosphate phosphorylase (MalP). SIGNIFICANCE AND IMPACT OF THE STUDY: This study describes a new pathway for maltose utilization in lactic acid bacteria.

Base Sequence↗
PubMed2000

Glycerol metabolism in Lactobacillus collinoides: production of 3-hydroxypropionaldehyde, a precursor of acrolein.

Lactobacillus collinoides is a lactic acid bacterium commonly found in fermenting apple juice. Although this bacterium is not particularly involved in malolactic conversion, the presence of L. collinoides in cider may have serious consequences on the product. L. collinoides is indeed considered to be responsible for the transformation of glycerol to 3-hydroxypropionaldehyde (3-HPA), a precursor of acrolein that spoils the product quality by generating bitter tastes. The purpose of our work was to evaluate the influence of environmental and culture conditions on the conversion of glycerol to 3-HPA in L. collinoides, and to obtain a DNA probe of the gene coding for glycerol dehydratase, the enzyme responsible for this conversion.

Acrolein↗