| Understanding enzyme immobilisation. | |
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MedLine Citation:
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PMID: 19169460 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Enzymes are versatile catalysts in the laboratory and on an industrial scale. To broaden their applicability in the laboratory and to ensure their (re)use in manufacturing the stability of enzymes can often require improvement. Immobilisation can address the issue of enzymatic instability. Immobilisation can also help to enable the employment of enzymes in different solvents, at extremes of pH and temperature and exceptionally high substrate concentrations. At the same time substrate-specificity, enantioselectivity and reactivity can be modified. However, most often the molecular and physical-chemical bases of these phenomena have not been elucidated yet. This tutorial review focuses on the understanding of enzyme immobilisation. |
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Authors:
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Ulf Hanefeld; Lucia Gardossi; Edmond Magner |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review Date: 2008-12-09 |
Journal Detail:
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Title: Chemical Society reviews Volume: 38 ISSN: 0306-0012 ISO Abbreviation: Chem Soc Rev Publication Date: 2009 Feb |
Date Detail:
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Created Date: 2009-01-26 Completed Date: 2009-03-20 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0335405 Medline TA: Chem Soc Rev Country: England |
Other Details:
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Languages: eng Pagination: 453-68 Citation Subset: IM |
Affiliation:
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Gebouw voor Scheikunde, Afdeling Biotechnologie, Technische Universiteit Delft, Julianalaan 136, Delft, 2628 BL, The Netherlands. u.hanefeld@tudelft.nl |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adsorption Enzymes, Immobilized / chemistry*, metabolism Hydrogen Bonding Ions / chemistry Lipase / chemistry, metabolism Stereoisomerism |
| Chemical | |
Reg. No./Substance:
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0/Enzymes, Immobilized; 0/Ions; EC 3.1.1.3/Lipase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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