Source:http://linkedlifedata.com/resource/pubmed/id/15046591
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 2
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pubmed:dateCreated |
2004-3-29
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pubmed:abstractText |
Biocatalysis is a useful tool in the provision of chiral technology and extremophilic enzymes are just one component in that toolbox. Their role is not always attributable to their extremophilic properties; as with any biocatalyst certain other criteria should be satisfied. Those requirements for a useful biocatalyst will be discussed including issues of selectivity, volume efficiency, security of supply, technology integration, intellectual property and regulatory compliance. Here we discuss the discovery and commercialization of an L-aminoacylase from Thermococcus litoralis, the product of a LINK project between Chirotech Technology and the University of Exeter. The enzyme was cloned into Escherichia coli to aid production via established mesophilic fermentation protocols. A simple downstream process was then developed to assist in the production of the enzyme as a genetically modified-organism-free reagent. The fermentation and downstream processes are operated at the 500 litre scale. Characterization of the enzyme demonstrated a substrate preference for N-benzoyl groups over N-acetyl groups. The operational parameters have been defined in part by substrate-concentration tolerances and also thermostability. Several examples of commercial biotransformations will be discussed including a process that is successful by virtue of the enzyme's thermotolerance.
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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:month |
Apr
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pubmed:issn |
0300-5127
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
290-2
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15046591-Amidohydrolases,
pubmed-meshheading:15046591-Biochemistry,
pubmed-meshheading:15046591-Bioreactors,
pubmed-meshheading:15046591-Biotechnology,
pubmed-meshheading:15046591-Biotransformation,
pubmed-meshheading:15046591-Catalysis,
pubmed-meshheading:15046591-Enzyme Stability,
pubmed-meshheading:15046591-Escherichia coli,
pubmed-meshheading:15046591-Fermentation,
pubmed-meshheading:15046591-Hot Temperature,
pubmed-meshheading:15046591-Models, Chemical,
pubmed-meshheading:15046591-Substrate Specificity,
pubmed-meshheading:15046591-Thermococcus
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pubmed:year |
2004
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pubmed:articleTitle |
Application of thermophilic enzymes in commercial biotransformation processes.
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pubmed:affiliation |
Dowpharma, Chirotech Technology Ltd, 321 Cambridge Science Park, Milton Road, Cambridge CB4 0WG, U.K. itaylor@dow.com
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pubmed:publicationType |
Journal Article
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