Source:http://linkedlifedata.com/resource/pubmed/id/18618472
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2009-1-27
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pubmed:abstractText |
Microstructured flow reactors are emerging tools for biocatalytic process development. A compelling design is that of the coated-wall reactor where enzyme is present as a surface layer attached to microchannel walls. However, preparation of a highly active wall biocatalyst remains a problem. Here, a stainless steel microreactor was developed where covalent immobilization of the enzyme in multiple linear flow channels of the reaction plate was supported by a macroporous wash-coat layer of gamma-aluminum oxide. Using surface functionalization with aminopropyl triethoxysilane followed by activation with glutardialdehyde, the thermophilic beta-glycosidase CelB from Pyrococcus furiosus was bound with retention of half of the specific activity of the free enzyme (800 U/mg), yielding a high catalyst loading of about 500 U/mL. This microreactor was employed for the continuous hydrolysis of lactose (100 mM) at 80 degrees C, providing a space-time yield of 500 mg glucose/(mL h) at a stable conversion of > or =70%. The immobilized enzyme displayed a half-life of 15 days under the operational conditions. Due to the absence of hydrophobic solute-material interactions, which limit the scope of microstructures fabricated from poly(dimethylsiloxane) for biocatalytic applications, the new microreactor was fully compatible with the alternate enzyme substrate 2-nitro-phenyl-beta-D-galactoside and the 2-nitro-phenol product resulting from its hydrolysis catalyzed by CelB.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CelB protein, Pyrococcus furiosus,
http://linkedlifedata.com/resource/pubmed/chemical/Enzymes, Immobilized,
http://linkedlifedata.com/resource/pubmed/chemical/Lactose,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Glucosidase
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1860-7314
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
98-107
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pubmed:meshHeading |
pubmed-meshheading:18618472-Bacterial Proteins,
pubmed-meshheading:18618472-Biocatalysis,
pubmed-meshheading:18618472-Bioreactors,
pubmed-meshheading:18618472-Enzyme Stability,
pubmed-meshheading:18618472-Enzymes, Immobilized,
pubmed-meshheading:18618472-Escherichia coli,
pubmed-meshheading:18618472-Kinetics,
pubmed-meshheading:18618472-Lactose,
pubmed-meshheading:18618472-Recombinant Proteins,
pubmed-meshheading:18618472-Surface Properties,
pubmed-meshheading:18618472-Temperature,
pubmed-meshheading:18618472-beta-Glucosidase
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pubmed:year |
2009
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pubmed:articleTitle |
Coated-wall microreactor for continuous biocatalytic transformations using immobilized enzymes.
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pubmed:affiliation |
Research Center Applied Biocatalysis, Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Graz, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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