Species of bacterium
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Paucimonas lemoignei, formerly ["Pseudomonas lemoignei"], is a Gram-negative soil bacterium. It is aerobic, motile, and rod-shaped.
Taxonomy.
"P. lemoignei" is established by Delafield "et al." in 1965, and transferred by Jendrossek in 2001 after reevaluating its 16S rDNA sequence. This is a big shift from one class to another. "P. lemoignei" is so far the only species under the genus "Paucimonas."
""Paucus" means little or few. "Paucimonas"" refers to bacterium with restricted catabolic capacities. "P. lemoignei" is named after the French microbiologist Maurice Lemoigne who first described poly-3-hydroxybutyrate (PHB) as a constituent of bacterial cells.
Metabolic Properties.
"P. lemoignei" are originally isolated from soil rich in poly-3-hydroxybutyrate (PHB). There are only 10 known substrates, mostly organic acids, that can be used for "P. lemoignei" as a sole carbon source. Sugars, sugar acids, alcohols, polyalcohols, amino acids, polypeptides, and polyols do not support its growth. Preferred carbon sources include: acetate, pyruvate, succinate, butyrate, 3-hydroxybutyrate, valerate and 3-hydroxyvalerate.
Application.
Polyhydroxyalkanoates (PHA) are polyesters that can be used to make biodegradable and biocompatible thermoplastics, attracting commercial interests with the growing awareness of sustainability. PHA-degrading bacteria are mainly proteobacteria. 
"P. lemoignei" can encode five kinds of extracellular PHA depolymerase, all of which hydrolyze PHB at high specific activities. It hydrolyzes the 3-hydroxybutyrate dimer with the highest specific activity of any of the enzymes reported so far. In addition, the purified enzymes are remarkably stable and active at high temperature (60 °C), high pH (up to 12.0), low ionic strength (distilled water), and in solvents ("e.g. n"-propyl alcohol).
The PHA depolymerases of "P. lemoignei" demonstrate a stable expression and secretion in recombinant "Escherichia coli". The processing sites of the precursors in "E. coli" were the same as that in "P. lemoignei", and similar substrate specificities were determined for the wild-type and the recombinant proteins. This lays the foundation for streamlined production of extracellular PHA depolymerases.
References.
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