Source:http://linkedlifedata.com/resource/pubmed/id/20420682
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2010-5-18
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pubmed:abstractText |
Trigonopsis variabilis D-amino acid oxidase (TvDAO) is a well characterized enzyme used for cephalosporin C conversion on industrial scale. However, the demands on the enzyme with respect to activity, operational stability and costs also vary with the field of application. Processes that use the soluble enzyme suffer from fast inactivation of TvDAO while immobilized oxidase preparations raise issues related to expensive carriers and catalyst efficiency. Therefore, oxidase preparations that are more robust and active than those currently available would enable a much broader range of economically viable applications of this enzyme in fine chemical syntheses. A multi-step engineering approach was chosen here to develop a robust and highly active Pichia pastoris TvDAO whole-cell biocatalyst.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1475-2859
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pubmed:author | |
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 |
24
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pubmed:meshHeading |
pubmed-meshheading:20420682-Bioreactors,
pubmed-meshheading:20420682-Catalysis,
pubmed-meshheading:20420682-D-Amino-Acid Oxidase,
pubmed-meshheading:20420682-Enzyme Stability,
pubmed-meshheading:20420682-Gene Dosage,
pubmed-meshheading:20420682-Peroxisomes,
pubmed-meshheading:20420682-Pichia,
pubmed-meshheading:20420682-Protein Engineering,
pubmed-meshheading:20420682-Technology, Pharmaceutical
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pubmed:year |
2010
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pubmed:articleTitle |
Stepwise engineering of a Pichia pastoris D-amino acid oxidase whole cell catalyst.
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pubmed:affiliation |
Austrian Centre of Industrial Biotechnology, Graz University of Technology, Petersgasse 14, 8010 Graz, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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