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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2010-3-19
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pubmed:abstractText |
The heterologous production of the industrially relevant fungal enzyme pyranose 2-oxidase in the prokaryotic host E. coli was investigated using 3 different expression systems, i.e. the well-studied T7 RNA polymerase based pET21d+, the L-arabinose inducible pBAD and the pCOLD system. Preliminary experiments were done in shaking flasks at 25 degrees C and optimized induction conditions to compare the productivity levels of the different expression systems. The pET21d+ and the pCOLD system gave 29 U/L x h and 14 U/L x h of active pyranose 2-oxidase, respectively, whereas the pBAD system only produced 6 U/L x h. Process conditions for batch fermentations were optimized for the pET21d+ and the pCOLD systems in order to reduce the formation of inactive inclusion bodies. The highest productivity rate with the pET21d+ expression system in batch fermentations was determined at 25 degrees C with 32 U/L x h. The pCOLD system showed the highest productivity rate (19 U/L x h) at 25 degrees C and induction from the start of the cultivation. Using the pCOLD system in a fed batch fermentation at 25 degrees C with a specific growth rate of mu = 0.15 h-1resulted in the highest productivity rate of active pyranose oxidase with 206 U/L x h.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20214772-11152063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20214772-12323357,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20214772-9821278
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1475-2859
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14
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pubmed:dateRevised |
2011-4-6
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pubmed:meshHeading |
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pubmed:year |
2010
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pubmed:articleTitle |
Evaluation of different expression systems for the heterologous expression of pyranose 2-oxidase from Trametes multicolor in E. coli.
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pubmed:affiliation |
Food Biotechnology Lab, Department of Food Sciences and Technology, BOKU - University of Natural Resources and Applied Life Sciences Vienna, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Evaluation Studies
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