Partial purification and characterization of a novel histidine decarboxylase from Enterobacter aerogenes DL-1.
Prep Biochem Biotechnol
; 45(6): 605-15, 2015 Aug 18.
Article
em En
| MEDLINE
| ID: mdl-25036745
ABSTRACT
Histidine decarboxylase (HDC) from Enterobacter aerogenes DL-1 was purified in a three-step procedure involving ammonium sulfate precipitation, Sephadex G-100, and DEAE-Sepharose column chromatography. The partially purified enzyme showed a single protein band of 52.4 kD on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH for HDC activity was 6.5, and the enzyme was stable between pH 4 and 8. Enterobacter aerogenes HDC had optimal activity at 40°C and retained most of its activity between 4 and 50°C. HDC activity was reduced in the presence of numerous tested compounds. Particularly with SDS, it significantly (p < 0.01) inhibited enzyme activity. Conversely, Ca(2+) and Mn(2+) showed prominent activation effects (p < 0.01) with activity increasing to 117.20% and 123.42%, respectively. The Lineweaver-Burk plot showed that K m and V max values of the enzyme for L-histidine were 0.21 mM and 71.39 µmol/min, respectively. In comparison with most HDCs from other microorganisms and animals, HDC from E. aerogenes DL-1 displayed higher affinity and greater reaction velocity toward L-histidine.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Contexto em Saúde:
3_ND
Base de dados:
MEDLINE
Assunto principal:
Perciformes
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Cromatografia DEAE-Celulose
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Enterobacter aerogenes
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Precipitação Fracionada
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Histidina Descarboxilase
Limite:
Animals
Idioma:
En
Revista:
Prep Biochem Biotechnol
Ano de publicação:
2015
Tipo de documento:
Article