Source:http://linkedlifedata.com/resource/pubmed/id/19937726
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2009-11-30
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pubmed:abstractText |
For the synthesis of polylactic acid (PLA) and its copolymers by one-step fermentation process, heterologous pathways involving Clostridium propionicum propionate CoA transferase (Pct(Cp)) and Pseudomonas sp. MBEL 6-19 polyhydroxyalkanoate (PHA) synthase 1 (PhaC1(Ps6-19)) were introduced into Escherichia coli for the generation of lactyl-CoA endogenously and incorporation of lactyl-CoA into the polymer, respectively. Since the wild-type PhaC1(Ps6-19) did not efficiently accept lactyl-CoA as a substrate, site directed mutagenesis as well as saturation mutagenesis were performed to improve the enzyme. The wild-type Pct(Cp) was not able to efficiently convert lactate to lactyl-CoA and was found to exert inhibitory effect on cell growth, random mutagenesis by error-prone PCR was carried out. By employing engineered PhaC1(Ps6-19) and Pct(Cp), poly(3-hydroxybutyrate-co-lactate), P(3HB-co-LA), containing 20-49 mol% lactate could be produced up to 62 wt% from glucose and 3HB. By controlling the 3HB concentration in the medium, PLA homopolymer and P(3HB-co-LA) containing lactate as a major monomer unit could be synthesized. Also, P(3HB-co-LA) copolymers containing various lactate fractions could be produced from glucose alone by introducing the Cupriavidus necator beta-ketothiolase and acetoacetyl-CoA reductase genes. Fed-batch cultures were performed to produce P(3HB-co-LA) copolymers having 9-64 mol% of lactate, and their molecular weights, thermal properties, and melt flow properties were determined.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Coenzyme A-Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/Lactic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Polymers,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/poly(3-hydroxyalkanoic acid)...,
http://linkedlifedata.com/resource/pubmed/chemical/poly(lactic acid)
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1097-0290
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
150-60
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pubmed:meshHeading |
pubmed-meshheading:19937726-Acyltransferases,
pubmed-meshheading:19937726-Blotting, Western,
pubmed-meshheading:19937726-Clostridium,
pubmed-meshheading:19937726-Coenzyme A-Transferases,
pubmed-meshheading:19937726-Escherichia coli,
pubmed-meshheading:19937726-Lactic Acid,
pubmed-meshheading:19937726-Molecular Structure,
pubmed-meshheading:19937726-Mutation,
pubmed-meshheading:19937726-Polymers,
pubmed-meshheading:19937726-Recombinant Proteins,
pubmed-meshheading:19937726-Signal Transduction
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pubmed:year |
2010
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pubmed:articleTitle |
Biosynthesis of polylactic acid and its copolymers using evolved propionate CoA transferase and PHA synthase.
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pubmed:affiliation |
Corporate R&D, LG Chem Research Park, 104-1 Moonji-dong, Yuseong-gu, Daejeon 305-380, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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