His-tagged Horse Liver Alcohol Dehydrogenase: Immobilization and application in the bio-based enantioselective synthesis of (S)-arylpropanols
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|Title:||His-tagged Horse Liver Alcohol Dehydrogenase: Immobilization and application in the bio-based enantioselective synthesis of (S)-arylpropanols||Authors:||Quaglia, Daniela
|Permanent link:||http://hdl.handle.net/10197/4376||Date:||May-2013||Abstract:||The novel histidine-tagged Horse Liver Alcohol Dehydrogenase (His-HLADH-EE) was successfully purified and covalently immobilized onto a solid support in a one-step procedure through a metal-directed technique. A full characterization of the immobilized enzyme was carried out. Effects of pH, temperature and organic co-solvents were deeply investigated and they showed a shift in the optimum pH with respect to the free form as well as increased stability to temperature and solvents. The immobilized His-HLADH-EE proved to be effective as catalyst in the reduction of aliphatic and aromatic aldehydes. Application of the free and immobilized His-HLADH-EE to the chemo-enzymatic synthesis of (S)-Profenols demonstrated enhanced enantioselectivity and high reusability of the immobilized form. The achievement of a robust and effective immobilization of an alcohol dehydrogenase substantiated the use of biocatalytic reduction in the synthesis of primary alcohols and valuable chiral intermediates especially for pharmaceutical industries.||Funding Details:||Irish Research Council for Science, Engineering and Technology||Type of material:||Journal Article||Publisher:||Elsevier||Copyright (published version):||2013 Elsevier Ltd.||Keywords:||Alcohol dehydrogenases;Immobilization;Enantioselective reduction;Profenols;Dynamic kinetic resolution;Horse liver alcohol dehydrogenase||DOI:||10.1016/j.procbio.2013.03.016||Language:||en||Status of Item:||Peer reviewed|
|Appears in Collections:||Chemistry Research Collection|
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