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Background  Microbial polyhydroxyalkanoates (PHA) are biopolyesters consisting of diverse monomers. PHA synthase PhaC2 Ps  cloned from  Pseudomonas stutzeri  1317 is able to polymerize short-chain-length (scl) 3-hydroxybutyrate (3HB) monomers and medium-chain-length (mcl) 3-hydroxyalkanoates (3HA) with carbon chain lengths ranging from C6 to C12. However, the scl and mcl PHA production in  Escherichia coli  expressing PhaC2 Ps  is limited with very low PHA yield.    Results  To improve the production of PHA with a wide range of monomer compositions in  E. coli , a series of optimization strategies were applied on the PHA synthase PhaC2 Ps . Codon optimization of the gene and mRNA stabilization with a hairpin structure were conducted and the function of the optimized PHA synthase was tested in  E. coli . The transcript was more stable after the hairpin structure was introduced, and western blot analysis showed that both codon optimization and hairpin introduction increased the protein expression level. Compared with the wild type PhaC2 Ps , the optimized PhaC2 Ps  increased poly-3-hydroxybutyrate (PHB) production by approximately 16-fold to 30% of the cell dry weight. When grown on dodecanoate, the recombinant  E. coli  harboring the optimized gene  phaC2   Ps   O  with a hairpin structure in the 5’ untranslated region was able to synthesize 4-fold more PHA consisting of 3HB and medium-chain-length 3HA compared to the recombinant harboring the wild type  phaC2   Ps  .    Conclusions  The levels of both PHB and scl-mcl PHA in  E. coli  were significantly increased by series of optimization strategies applied on PHA synthase PhaC2 Ps . These results indicate that strategies including codon optimization and mRNA stabilization are useful for heterologous PHA synthase expression and therefore enhance PHA production.

Production of copolyesters of 3-hydroxybutyrate and medium-chain-length 3-hydroxyalkanoates by E. coli containing an optimized PHA synthase gene