초록
<P><B>Abstract</B></P><P>Conversion of 3-hydroxypropionate (3HP) from 1,3-propanediol (PDO) was improved by expressing dehydratase gene (<I>dhaT</I>) and aldehyde dehydrogenase gene (<I>aldD</I>) of <I>Pseudomonas putida</I> KT2442 under the promoter of <I>phaCAB</I> operon from <I>Ralstonia eutropha</I> H16. Expression of these genes in <I>Aeromonas hydrophila</I> 4AK4 produced up to 21g/L 3HP in a fermentation process. To synthesize homopolymer poly(3-hydroxypropionate) (P3HP), and copolymer poly(3-hydroxypropionate-co-3-hydroxybutyrate) (P3HP4HB), <I>dhaT</I> and <I>aldD</I> were expressed in <I>E. coli</I> together with the <I>phaC1</I> gene encoding polyhydroxyalkanoate (PHA) synthase gene of <I>Ralstonia eutropha</I>, and <I>pcs</I>' gene encoding the ACS domain of the tri-functional propionyl-CoA ligase (PCS) of <I>Chloroflexus aurantiacus</I>. Up to 92wt% P3HP and 42wt% P3HP4HB were produced by the recombinant <I>Escherichia coli</I> grown on PDO and a mixture of PDO+1,4-butanediol (BD), respectively.</P> <P><B>Highlights</B></P><P>► <I>E. coli</I> expressed <I>dhaT</I>, <I>aldD</I>, <I>phaC1</I> & ACS domain of the propionyl-CoA ligase (<I>pcs</I>'). ► The recombinant produced up to 92wt% P3HP and 42wt% P3HP4HB, respectively. ► Fermentative production of high intracellular P3HP content is expected.</P>