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  5. Horse Liver Alcohol Dehydrogenase: new perspectives for an old enzyme
 
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Horse Liver Alcohol Dehydrogenase: new perspectives for an old enzyme

Author(s)
Quaglia, Daniela  
Irwin, Jane A.  
Paradisi, Francesca  
Uri
http://hdl.handle.net/10197/3941
Date Issued
2012-11
Date Available
2013-11-01T04:00:08Z
Abstract
The EE subunit of horse liver alcohol dehydrogenase
(HLADH-EE) has been subcloned in pRSETb vector
to generate a fusion His-tag protein. The migration from a
multistep purification protocol for this well-known enzyme
to a single-step has been successfully achieved. Several
adjustments to the traditional purification procedure for Histag
proteins have been made to retain protein activity. A full
characterization of the fusion enzyme has been carried out
and compared with the native one. The Km for EtOH, NAD
and NADH in the His-tag version of HLADH are in line
with the ones reported in literature for the native enzyme. A
shift in optimal pH activity is also observed. The enzyme
retains the same stability and quaternary structure as the
wild type and can therefore be easily used instead of the
native HLADH for biotechnological applications.
Type of Material
Journal Article
Publisher
Springer Science+Business Media
Journal
Molecular Biotechnology
Volume
52
Issue
3
Start Page
244
End Page
250
Copyright (Published Version)
2012 Springer Science+Business Media, LLC
Subjects

DAC

Enzyme characterisati...

IMAC

Horse liver alcohol d...

Subject – LCSH
Chromatographic analysis
Alcohol dehydrogenase
Enzymes--Analysis
DOI
10.1007/s12033-012-9542-7
Language
English
Status of Item
Not peer reviewed
This item is made available under a Creative Commons License
https://creativecommons.org/licenses/by-nc-nd/3.0/ie/
File(s)
No Thumbnail Available
Name

Quaglia_J_Biotech_2012.doc

Size

304 KB

Format

Microsoft Word

Checksum (MD5)

0862e6f55cfb03a8c040633254e82b1f

Owning collection
Chemistry Research Collection

Item descriptive metadata is released under a CC-0 (public domain) license: https://creativecommons.org/public-domain/cc0/.
All other content is subject to copyright.

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