Abstract
A new enzyme showing a dehydrogenase activity towards aromatic aldehydes was isolated, purified and characterized from a halophilic strain isolated from saline environment. The enzyme is a monomer of 54 kDa; it is rather thermostable (optimal temperature: 50°C) showing a broad spectrum of activity in a large pH range with the maximum at pH 9.5. The substrate specificity and the effect of ions were evaluated and compared with analogous described proteins.
Keywords: extremophiles, halophilic bacterium, dependent aldehyde dehydrogenase, enzyme purification
Protein & Peptide Letters
Title: A New Dehydrogenase Specific Towards Aromatic Aldehydes From A Halophilic Bacterium
Volume: 10 Issue: 5
Author(s): F. La Cara, L. Alves, F. Girio, A. Di Salle, A. Capasso and M. Rossi
Affiliation:
Keywords: extremophiles, halophilic bacterium, dependent aldehyde dehydrogenase, enzyme purification
Abstract: A new enzyme showing a dehydrogenase activity towards aromatic aldehydes was isolated, purified and characterized from a halophilic strain isolated from saline environment. The enzyme is a monomer of 54 kDa; it is rather thermostable (optimal temperature: 50°C) showing a broad spectrum of activity in a large pH range with the maximum at pH 9.5. The substrate specificity and the effect of ions were evaluated and compared with analogous described proteins.
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Cite this article as:
Cara La F., Alves L., Girio F., Salle Di A., Capasso A. and Rossi M., A New Dehydrogenase Specific Towards Aromatic Aldehydes From A Halophilic Bacterium, Protein & Peptide Letters 2003; 10 (5) . https://dx.doi.org/10.2174/0929866033478645
DOI https://dx.doi.org/10.2174/0929866033478645 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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