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  • Polyhydroxybutyrate biosynthesis in Caulobacter crescentus: Molecular characterization of the polyhydroxybutyrate synthase

    Author(s)
    Qi, QS
    Rehm, BHA
    Griffith University Author(s)
    Rehm, Bernd
    Year published
    2001
    Metadata
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    Abstract
    Caulobacter crescentus was investigated with respect to polyhydroxybutyrate (PHB) biosynthesis. Polyhydroxyalkanoate (PHA) accumulation contributing to approximately 18% of the cell dry weight was obtained in the presence of glucose. Gas chromatography–mass spectrometry and gel permeation chromatography of the purified PHA showed that this polyester was solely composed of 3-hydroxybutyrate and had a weight average molar mass of 5·5×105 g mol−1 and a polydispersity of 1·6. An ORF encoding a conserved, hypothetical protein which shared approximately 47% identity with the PHB synthase from Azorhizobium caulinodans was identified ...
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    Caulobacter crescentus was investigated with respect to polyhydroxybutyrate (PHB) biosynthesis. Polyhydroxyalkanoate (PHA) accumulation contributing to approximately 18% of the cell dry weight was obtained in the presence of glucose. Gas chromatography–mass spectrometry and gel permeation chromatography of the purified PHA showed that this polyester was solely composed of 3-hydroxybutyrate and had a weight average molar mass of 5·5×105 g mol−1 and a polydispersity of 1·6. An ORF encoding a conserved, hypothetical protein which shared approximately 47% identity with the PHB synthase from Azorhizobium caulinodans was identified within the complete C. crescentus genomic sequence. This putative C. crescentus PHB synthase gene, phaC, consisted of a 2019 nt stretch of DNA (encoding 673 aa residues), which encoded a PHB synthase with a molecular mass of approximately 73 kDa. This is currently the largest PHA synthase identified. The phaC coding region was subcloned into vector pBBR1-JO2 under lac promoter control. The resulting plasmid, pQQ4, mediated PHB accumulation in the mutant Ralstonia eutropha PHB−4 and recombinant Escherichia coli JM109(pBHR69), which produced the β-ketothiolase and acetoacetyl-CoA reductase from R. eutropha, contributing to approximately 62% and 6% of cell dry weight, respectively. Functional expression of the coding region of phaC was confirmed by immunoblotting and in vitro PHB synthase activity.
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    Journal Title
    Microbiology
    Volume
    147
    Issue
    12
    DOI
    https://doi.org/10.1099/00221287-147-12-3353
    Subject
    Microbiology not elsewhere classified
    Publication URI
    http://hdl.handle.net/10072/373505
    Collection
    • Journal articles

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