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A New Dehydrogenase Specific Towards Aromatic Aldehydes From A Halophilic Bacterium

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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: dependent aldehyde dehydrogenase; enzyme purification; extremophiles; halophilic bacterium

Document Type: Review Article


Affiliations: Institute of Protein Biochemistry - C.N.R., Via P. Castellino, 111, 80131, Naples, Italy.

Publication date: October 1, 2003

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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