ArticleMolecules (Basel, Switzerland)2015
2-Keto-D-gluconate-yielding membrane-bound D-glucose dehydrogenase from Arthrobacter globiformis C224: purification and characterization.
Article in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Microgravity environment grown crystal structure information based engineering of direct electron transfer type glucose dehydrogenase.Communications biology · 2022Article
- Efficient biosynthesis of 2-keto-D-gluconic acid by fed-batch culture of metabolically engineeredSynthetic and systems biotechnology · 2019Article
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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.
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