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
Galletti, Paola
Emer, Enrico
Paradisi, Francesca
Giacomini, Daria
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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