Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-3-19
pubmed:abstractText
Heterogenous expression of (R)-3-hydroxydecanoyl-ACP:CoA transacylase gene (phaG) isolated from Pseudomonas putida in Escherichia coli HB101 led to the extracellular production of 3-hydroxydecanoic acid (3HD) in a growth medium consisting of carbon source non-related to 3HD structure, while no 3HD was detected in the growth media inoculated with wild type E. coli HB101 and recombinant E. coli HB101 harboring vector pBluescript SK- only. 3HD production by E. coli HB101 (pLZZGPp) harboring phaG from fructose was 587 mg/l, approximately three times that from cultivation in glucose under same culture conditions. 3HD production was affected by timing of fructose addition and fructose concentration in the culture. As an inhibitor of fatty acid de novo synthesis, the presence of triclosan in the culture could increase 3HD production by E. coli HB101 (pLZZGPp) by about 20-40%. The results further confirmed that (R)-3-hydroxydecanoyl-ACP:CoA transacylase (PhaG) provides 3HD precursors for medium-chain-length polyhydroxyalkanoate synthesis. At the same time, this phenomenon showed that recombinant organisms can be used for production of certain fine chemicals such as hydroxyalkanoic acids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0003-6072
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
93-101
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Production of 3-hydroxydecanoic acid by recombinant Escherichia coli HB101 harboring phaG gene.
pubmed:affiliation
Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't