Purification and characterization of carbonyl enantioselective reductase from Morganella morganii J-8 / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 268-272, 2007.
Artigo
em Chinês
| WPRIM
| ID: wpr-325381
ABSTRACT
The purification and the characteristics of an enzyme from Morganella morganii J-8, which could produce d-pseudoephedrine from 1-phenyl-2-methylamine-acetone, were performed in this study. In this research, first, cells were disrupted by ultrasonic treatment at 4 degrees C. The carbonyl enantioselective reductase was purified with a combination of ammonium precipitation, Phenyl Superose hydrophobic chromatography, DEAE anion exchange, and native polyacrylamide gel electrophoresis. The molecular mass of the purified enzyme subunit was estimated to be 42.5kD on sodium dodecyl sulfate-polyacrylamide electrophoresis (SDS-PAGE). The native molecular mass of the enzyme that was analyzed by high-performance liquid chromatography was found out to be 84.1 kD, which indicated that the enzyme was a dimmer. The purified enzyme was analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, and the result showed that the purified enzyme had high homology with leucine dehydrogenase.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Oxirredutases
/
Farmacologia
/
Estereoisomerismo
/
Temperatura
/
Proteínas de Bactérias
/
Estabilidade Enzimática
/
Cinética
/
Química
/
Cromatografia Líquida de Alta Pressão
/
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Idioma:
Chinês
Revista:
Chinese Journal of Biotechnology
Ano de publicação:
2007
Tipo de documento:
Artigo
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