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The nutrition-versatility of  Burkholderia  sp. strain USM (JCM 15050) has initiated the studies on the use of this bacterium for polyhydroxyalkanoate (PHA) production. To date, the  Burkholderia  sp. has been reported to synthesize 3-hydroxybutyrate, 3-hydroxyvalerate and 3-hydroxy-4-methylvalerate monomers. In this study, the PHA biosynthetic genes of this strain were successfully cloned and characterized. The PHA biosynthetic cluster of this strain consisted of a PHA synthase ( phaC ), β-ketothiolase ( phaA ), acetoacetyl-CoA reductase ( phaB ) and PHA synthesis regulator ( phaR ). The translated products of these genes revealed identities to corresponding proteins of  Burkholderia vietnamiensis  (99–100 %) and  Cupriavidus necator  H16 (63–89%). Heterologous expression of  phaC   Bs   conferred PHA synthesis to the PHA-negative  Cupriavidus necator  PHB¯4, confirming that  phaC   Bs   encoded functionally active protein. PHA synthase activity measurements revealed that the crude extracts of  C. necator  PHB¯4 transformant showed higher synthase activity (243 U/g) compared to that of wild-types  Burkholderia  sp. (151 U/g) and  C. necator  H16 (180 U/g). Interestingly, the transformant  C .  necator  PHB¯4 harbouring  Burkholderia  sp. PHA synthase gene accumulated poly(3-hydroxybutyrate- co -4-hydroxybutyrate) with 4-hydroxybutyrate monomer as high as up to 87 mol% from sodium 4-hydroxybutyrate. The wild type  Burkholderia  sp. did not have the ability to produce this copolymer.

Revelation of the ability of Burkholderia sp. USM (JCM 15050) PHA synthase to polymerize 4-hydroxybutyrate monomer