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Molecules 2015, 20(1), 846-862; doi:10.3390/molecules20010846

2-Keto-D-Gluconate-Yielding Membrane-Bound D-Glucose Dehydrogenase from Arthrobacter globiformis C224: Purification and Characterization

1,2,†
,
3,4,5,†
,
1,3,4,* , 1,3,4,* , 3,4
,
3,4
and
2
1
School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China
2
College of Life Science, Hebei Normal University, Shijiazhuang 050016, China
3
Parchn Sodium Isovitamin C Co. Ltd, Dexing 334221, China
4
Jiangxi Provincial Engineering and Technology Center for Food Additives Bio-production, Dexing 334221, China
5
Department of Pharmaceutical, Hebei Chemical and Pharmaceutical College, Shijiazhuang 050026, China
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Received: 14 November 2014 / Accepted: 4 January 2015 / Published: 8 January 2015
(This article belongs to the Section Natural Products)
View Full-Text   |   Download PDF [1022 KB, uploaded 8 January 2015]   |  

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. View Full-Text
Keywords: Arthrobacter globiformis; 2-ketogluconic acid (2KGlcA); D-glucose dehydrogenase (GlcDH); purification; enzymatic properties Arthrobacter globiformis; 2-ketogluconic acid (2KGlcA); D-glucose dehydrogenase (GlcDH); purification; enzymatic properties
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Xue, Q.; Wei, Z.; Sun, W.; Cui, F.; Yu, S.; Zhou, Q.; Liu, J. 2-Keto-D-Gluconate-Yielding Membrane-Bound D-Glucose Dehydrogenase from Arthrobacter globiformis C224: Purification and Characterization. Molecules 2015, 20, 846-862.

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