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Inactivation of isocitrate lyase leads to increased production of medium-chain-length poly(3-hydroxyalkanoates) in Pseudomonas putida

Article Abstract:

Researchers increased the production of poly(3-hydroxyalkanoates) (PHAs) in Pseudomonas putida by inactivating the glyoxylate pathway and reducing the activity of isocitrate dehydrogenase. This shunted carbon flow toward fatty acid synthesis, leading to increased accumulation of PHAs. PHAs are biodegradable biopolymers that can be made from renewable resources.

Author: Klinke, Stefan, Dauner, Michael, Scott, George, Kessler, Birgit, Witholt, Bernard
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
Pseudomonas putida, Biopolymers

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Role of phaD in accumulation of medium-chain-length poly(3-hydroxyalkanoates) in pseudomonas oleovorans

Article Abstract:

Results show that a protein encoded by the phaD gene has an indirect role in the biosynthesis of medium-chain-length poly(3-hydroxyalkanoates)granule as revealed by mutant analysis. Data indicate that the PhaD protein mainly stabilizes the granules in concert with the PhaI protein.

Author: Klinke, Stefan, Kessler, Birgit, Witholt, Bernard, Roo, Guy de
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
United States, Switzerland, Statistical Data Included, Analysis, Physiological aspects, Polymers, Pseudomonas, Mutation (Biology), Mutation, Bacterial proteins

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Production of medium-chain-length poly(3-hydroxyalkanoates) from gluconate by recombinant Escherichia coli

Article Abstract:

Research was conducted to examine the production of medium-chain-length (MCL) poly(3-hydroxyalkanoates) (PHA) polymerase-encoding gene of Pseudomonas from gluconate by recombinant Escherichia coli. A pathway for the synthesis of MCL PHA from gluconate was developed by introducing genes coding for an MCLL PHA polymerase and the cytosolic thioesterase I into E. coli JMU193. Results provide evidence for an MCL PHA biosynthesis pathway scheme that involves both beta-oxidation and de novo fatty acid synthesis.

Author: Klinke, Stefan, Kessler, Birgit, Witholt, Bernard, Ren, Qun
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
Escherichia coli, Fatty acids, Recombinant proteins, Fatty acid synthesis, Polyesters

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Subjects list: Research, Genetic aspects
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