Utilize este identificador para referenciar este registo:
https://hdl.handle.net/1822/1947
Título: | A new alkali-thermostable azoreductase from bacillus sp. strain SF |
Autor(es): | Maier, Jurgen Kandelbauer, A. Erlacher, Angelika Paulo, Artur Cavaco Gübitz, Georg M. |
Data: | 2004 |
Editora: | American Society for Microbiology (ASM) |
Revista: | Applied and Environmental Microbiology |
Citação: | "Applied and environmental microbiology". ISSN 0099-2240. 70:2 (Feb. 2004) 837–844. |
Resumo(s): | A screening for dye-decolorizing alkali-thermophilic microorganisms resulted in a Bacillus sp. strain isolated out of the wastewater drain of a textile finishing company. An NADH-dependent azoreductase of this strain, Bacillus sp. strain SF, was found to be responsible for the decolorization of azo dyes. This enzyme was purified by a combination of ammonium sulfate precipitation and anion-exchange and affinity chromatography and had a molecular mass of 61.6 kDa and an isoelectric point at pH 5.3. The pH optimum of the azoreductase depended on the substrate and was within the range of pHs 8 to 9, while the temperature maximum was reached at 80°C. Decolorization only took place in the absence of oxygen and was enhanced by FAD, which was not consumed during the reaction. A 26% similarity of this azoreductase to chaperonin Cpn60 from a Bacillus sp. was found by peptide mass mapping experiments. Substrate specificities of the azoreductase were studied by using synthesized model substrates based on di-sodium-(R)-benzyl-azo-2,7-dihydroxy-3,6-disulfonyl-naphthaline. Those dyes with NO2 substituents, especially in the ortho position, were degraded fastest, while analogues with a methyl substitution showed the lowest degradation rates. |
Tipo: | Artigo |
URI: | https://hdl.handle.net/1822/1947 |
DOI: | 10.1128/AEM.70.2.837-844.2004 |
ISSN: | 0099-2240 |
Arbitragem científica: | yes |
Acesso: | Acesso aberto |
Aparece nas coleções: | DET/2C2T - Artigos em revistas internacionais com arbitragem científica |