Open AccessCo‐expression of polyhydroxyalkanoate synthase and ( R )‐enoyl‐CoA hydratase genes of Aeromonas caviae establishes copolyester biosynthesis pathway in Escherichia coli
Author(s) -
Fukui Toshiaki,
Yokomizo Satoru,
Kobayashi Genta,
Doi Yoshiharu
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13356.x
Subject(s) - polyhydroxyalkanoates , aeromonas caviae , escherichia coli , biochemistry , biosynthesis , copolyester , biology , chemistry , microbiology and biotechnology , enzyme , gene , bacteria , organic chemistry , genetics , vibrionaceae , polyester
Polyhydroxyalkanoate biosynthesis genes of Aeromonas caviae were expressed in Escherichia coli LS5218 ( fadR atoC (Con)), and the polyhydroxyalkanoate‐producing ability of the recombinants was investigated. A LS5218 strain harboring only phaC Ac (polyhydroxyalkanoate synthase gene) did not accumulate any polyhydroxyalkanoate from dodecanoate in spite of the existence of translated polyhydroxyalkanoate synthase protein, whereas co‐expression phaC Ac and phaJ Ac (( R )‐specific enoyl‐CoA hydratase gene) resulted in the accumulation of P(3‐hydroxybutyrate‐ co ‐3‐hydroxyhexanoate) copolymer up to 7–11 wt% of dry cell weight from octanoate and dodecanoate. These results indicated that both phaC Ac and phaJ Ac are essential for E . coli LS5218 to establish the polyhydroxyalkanoate biosynthesis pathway from alkanoic acids. The copolyester content in the strain expressing both the genes under the lac promoter control reached to 38 wt% from dodecanoate. Enzyme assays suggest that efficient monomer formation via β‐oxidation by a high level expression of phaJ Ac was important to achieve a high polyhydroxyalkanoate content in the recombinant E . coli .