2-Keto-D-gluconate-yielding membrane-bound D-glucose dehydrogenase from Arthrobacter globiformis C224: purification and characterization.
Molecules
; 20(1): 846-62, 2015 Jan 08.
Article
em En
| MEDLINE
| ID: mdl-25580683
ABSTRACT
Glucose dehydrogenase (GlcDH) is the rate-limiting catalyst for microbial conversion of glucose to the important organic acid 2-ketogluconic acid (2KGlcA). In this study, a D-glucose dehydrogenase was purified from the industrial 2KGlcA producer Arthrobacter globiformis C224. After four purification steps, the GlcDH was successfully purified over 180 folds and specific activity of 88.1 U/mg. A single protein band of 87 kDa was detected by SDS-PAGE. The purified GlcDH had the broad substrate specificity with the Km values for D-glucose, D-xylose, D-galactose and maltose of 0.21 mM, 0.34 mM, 0.46 mM and 0.59 mM, respectively. The kinetic studies proved that A. globiformis GlcDH followed the ping-pong kinetic mechanism. The GlcDH showed an optimum catalytic activity at pH 5.0 and 45 °C with the stable activity at temperature of 20-40 °C and pH of 6.0-7.0. Organic solvents, metal ions or EDTA could significantly influence the GlcDH activity to different degrees.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Arthrobacter
/
Membrana Celular
/
Glucose 1-Desidrogenase
/
Gluconatos
Idioma:
En
Revista:
Molecules
Assunto da revista:
BIOLOGIA
Ano de publicação:
2015
Tipo de documento:
Article
País de afiliação:
China
País de publicação:
CH
/
SUIZA
/
SUÍÇA
/
SWITZERLAND