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Biochemical and Computational Insights on a Novel Acid-Resistant and Thermal-Stable Glucose 1-Dehydrogenase

Key Laboratory for Polar Science of State Oceanic Administration, Polar Research Institute of China, Shanghai 200136, China
East China Sea Fisheries Research Institute, Shanghai 200090, China
Author to whom correspondence should be addressed.
Academic Editor: Quan Zou
Int. J. Mol. Sci. 2017, 18(6), 1198;
Received: 10 May 2017 / Revised: 30 May 2017 / Accepted: 30 May 2017 / Published: 5 June 2017
(This article belongs to the Special Issue Special Protein Molecules Computational Identification)
PDF [5790 KB, uploaded 5 June 2017]


Due to the dual cofactor specificity, glucose 1-dehydrogenase (GDH) has been considered as a promising alternative for coenzyme regeneration in biocatalysis. To mine for potential GDHs for practical applications, several genes encoding for GDH had been heterogeneously expressed in Escherichia coli BL21 (DE3) for primary screening. Of all the candidates, GDH from Bacillus sp. ZJ (BzGDH) was one of the most robust enzymes. BzGDH was then purified to homogeneity by immobilized metal affinity chromatography and characterized biochemically. It displayed maximum activity at 45 °C and pH 9.0, and was stable at temperatures below 50 °C. BzGDH also exhibited a broad pH stability, especially in the acidic region, which could maintain around 80% of its initial activity at the pH range of 4.0–8.5 after incubating for 1 hour. Molecular dynamics simulation was conducted for better understanding the stability feature of BzGDH against the structural context. The in-silico simulation shows that BzGDH is stable and can maintain its overall structure against heat during the simulation at 323 K, which is consistent with the biochemical studies. In brief, the robust stability of BzGDH made it an attractive participant for cofactor regeneration on practical applications, especially for the catalysis implemented in acidic pH and high temperature. View Full-Text
Keywords: Bacillus; glucose 1-dehydrogenase; acid-resistant; thermal-stable; molecular dynamics simulation Bacillus; glucose 1-dehydrogenase; acid-resistant; thermal-stable; molecular dynamics simulation

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Ding, H.; Gao, F.; Yu, Y.; Chen, B. Biochemical and Computational Insights on a Novel Acid-Resistant and Thermal-Stable Glucose 1-Dehydrogenase. Int. J. Mol. Sci. 2017, 18, 1198.

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