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Purification and characterisation of a 4-hydroxy benzaldehyde dehydrogenase cloned from Acinetobacter baylyi

Paper ID Volume ID Publish Year Pages File Format Full-Text
17817 42698 2008 6 PDF Available
Title
Purification and characterisation of a 4-hydroxy benzaldehyde dehydrogenase cloned from Acinetobacter baylyi
Abstract

4-Hydroxy benzaldehyde dehydrogenase catalyses a step in a well-studied pathway for the catabolism of 4-hydroxy-substituted cinnamates in Acinetobacter baylyi, oxidising a benzaldehyde group to the corresponding benzoic acid, with the concomitant reduction of NAD+ to NADH. Although much genetic and in vivo data for the enzyme have been presented, there have been no reports of the purification and in vitro characterisation of this enzyme. In this work, 4-hydroxy benzaldehyde dehydrogenase from A. baylyi was cloned to incorporate a hexahistidine affinity tag, heterologously expressed in Escherichia coli, purified and characterised. The enzyme was found to be stable up to 45 °C, losing only 25% of its activity over 9 h at this temperature. NAD+ was the preferred cofactor. The enzyme was found to act on a number of benzaldehyde substrates, and steady-state kinetics suggested that 4-hydroxy and 3,4-dihydroxy benzaldehydes were preferred substrates to benzaldehyde, or 4-hydroxy 3-methoxy benzaldehyde (vanillin).

Keywords
4-Hydroxy benzaldehyde dehydrogenase; Acinetobacter baylyi; Aromatic metabolism; Biocatalytic oxidation
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Purification and characterisation of a 4-hydroxy benzaldehyde dehydrogenase cloned from Acinetobacter baylyi
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 43, Issue 6, 6 November 2008, Pages 417–422
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us