Cloning and expression in E. coli of an organic solvent-tolerant and alkali-resistant glucose 1-dehydrogenase from Lysinibacillus sphaericus G10

Ding, Haitao; Du, Yiqing; Liu, Danfeng; Li, Zeli; XueJiao, Chen; Zhao, Yong

doi:10.1016/j.biortech.2010.08.018

Cited by 31 publications

(26 citation statements)

References 31 publications

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“…strain S-1 [81] and Nesterentonia sp. strain F [71], proteases from Pseudomonas aeruginosa [82] and B. licheniformis [83], and glucose 1-dehydrogenase from Lysinibacillus sphaericus [84].…”

Section: Discussionmentioning

confidence: 99%

Molecular characterization of a novel trehalose-6-phosphate hydrolase, TreA, from Bacillus licheniformis

Chuang

Ong

Wang

et al. 2012

International Journal of Biological Macromolecules

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“…strain S-1 [81] and Nesterentonia sp. strain F [71], proteases from Pseudomonas aeruginosa [82] and B. licheniformis [83], and glucose 1-dehydrogenase from Lysinibacillus sphaericus [84].…”

Section: Discussionmentioning

confidence: 99%

Molecular characterization of a novel trehalose-6-phosphate hydrolase, TreA, from Bacillus licheniformis

Chuang

Ong

Wang

et al. 2012

International Journal of Biological Macromolecules

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“…In contrast, PTDH-WM88 activity is not influenced by the presence of EDTA [8]. The significant activation of PTDH-K activity by EDTA may be due to a cooperative effect between EDTA and Na + , similar to that found for LsGDH [27].…”

Section: Surface Electrostatic Potential Analysis Of Ptdh-k and Ptdh-mentioning

confidence: 55%

Cloning, Expression, and Characterization of a Wide-pH-Range Stable Phosphite Dehydrogenase from Pseudomonas sp. K in Escherichia coli

Liu

Ding

et al. 2012

Appl Biochem Biotechnol

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A phosphite dehydrogenase gene (ptdhK) consisting of 1,011-bp nucleotides which encoding a peptide of 336 amino acid residues was cloned from Pseudomonas sp. K. gene ptdhK was expressed in Escherichia coli BL21 (DE3) and the corresponding recombinant enzyme was purified by metal affinity chromatography. The recombinant protein is a homodimer with a monomeric molecular mass of 37.2 kDa. The specific activity of PTDH-K was 3.49 U mg(-1) at 25 °C. The recombinant PTDH-K exhibited maximum activity at pH 3.0 and at 40 °C and displayed high stability within a wide range of pHs (5.0 to 10.5). PTDH-K had a high affinity to its natural substrates, with K (m) values for sodium phosphite and NAD of 0.475 ± 0.073 and 0.022 ± 0.007 mM, respectively. The activity of PTDH-K was enhanced by Na(+), NH (4) (+) , Mg(2+), Fe(2+), Fe(3+), Co(2+), and EDTA, and PTDH-K exhibited different tolerance to various organic solvents.

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“…By using gel filtration chromatography through a Zorbax Bio-series GF-450 column, the molecular weight of the native BzGDH was estimated to be 120 kDa. These results indicated that BzGDH was a homo-tetramer composed of four identical subunits, as well as other NAD-dependent GDHs derived from Bacillus [1,2,3,4,5,6,23,24,26,27]. …”

Section: Resultsmentioning

confidence: 82%

“…GDHs from Bacillus sp. ZJ (this study), Bacillus megaterium IWG3 [5], Lysinibacillus sphaericus G10 [2], Bacillus cereus var. mycoides [24], Bacillus sp.…”

Section: Figurementioning

confidence: 99%

“…NAD(P)-dependent glucose 1-dehydrogenase (GDH, EC 1.1.1.47) is an oxidoreductase present in various organisms and involved in glucose metabolic pathways, catalyzing the oxidation of d -glucose to d -glucono-1,5-lactone while simultaneously reducing NAD(P) to NAD(P)H [1,2,3,4,5,6]. As a member of the short-chain dehydrogenases/reductases family (SDRs), GDH is a tetrameric protein consisting of four identical subunits, which shares similar overall folding and oligomeric architecture with those of its homologous counterparts [7,8].…”

Section: Introductionmentioning

confidence: 99%

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

Ding

Gao

et al. 2017

IJMS

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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.

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Cloning and expression in E. coli of an organic solvent-tolerant and alkali-resistant glucose 1-dehydrogenase from Lysinibacillus sphaericus G10

Cited by 31 publications

References 31 publications

Molecular characterization of a novel trehalose-6-phosphate hydrolase, TreA, from Bacillus licheniformis

Molecular characterization of a novel trehalose-6-phosphate hydrolase, TreA, from Bacillus licheniformis

Cloning, Expression, and Characterization of a Wide-pH-Range Stable Phosphite Dehydrogenase from Pseudomonas sp. K in Escherichia coli

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

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