A New Dehydrogenase Specific Towards Aromatic Aldehydes From A Halophilic Bacterium

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.

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