ArticleAMB Express2015
Kinetic properties and stability of glucose dehydrogenase from Bacillus amyloliquefaciens SB5 and its potential for cofactor regeneration.
Article in AMB Express, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 36 citations in OpenAlex.
- Enhanced Expression of Alcohol Dehydrogenase I inMicroorganisms · 2023Article
- Characterization and Application of a Novel Glucose Dehydrogenase with Excellent Organic Solvent Tolerance for Cofactor Regeneration in Carbonyl Reduction.Applied biochemistry and biotechnology · 2023Article
- Constitutive glucose dehydrogenase elevates intracellular NADPH levels and luciferase luminescence in Bacillus subtilis.Microbial cell factories · 2022Article
- Exploitation of Hetero- and Phototrophic Metabolic Modules for Redox-Intensive Whole-Cell Biocatalysis.Frontiers in bioengineering and biotechnology · 2022Review
- Directed evolution engineering to improve activity of glucose dehydrogenase by increasing pocket hydrophobicity.Frontiers in microbiology · 2022Article
- Enzymes of an alternative pathway of glucose metabolism in obligate methanotrophs.Scientific reports · 2021Article
- Characterization and Application of a Robust Glucose Dehydrogenase fromIndian journal of microbiology · 2020Article
- Unusual substrate and halide versatility of phenolic halogenase PltM.Nature communications · 2019Article
- Rational design of engineered microbial cell surface multi-enzyme co-display system for sustainable NADH regeneration from low-cost biomass.Journal of industrial microbiology & biotechnology · 2018Article
- Biochemical and Computational Insights on a Novel Acid-Resistant and Thermal-Stable Glucose 1-Dehydrogenase.International journal of molecular sciences · 2017Article
- Probing Steroidal Substrate Specificity of Cytochrome P450 BM3 Variants.Molecules (Basel, Switzerland) · 2016Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Glucose dehydrogenases (GluDH) from Bacillus species offer several advantages over other NAD(P)H regeneration systems including high stability, inexpensive substrate, thermodynamically favorable reaction and flexibility to regenerate both NADH and NADPH. In this research, characteristics of GluDH from Bacillus amyloliquefaciens SB5 (GluDH-BA) was reported for the first time. Despite a highly similar amino acid sequence when comparing with GluDH from Bacillus subtilis (GluDH-BS), GluDH-BA exhibited significantly higher specific activity (4.7-fold) and stability when pH was higher than 6. While an optimum activity of GluDH-BA was observed at a temperature of 50 °C, the enzyme was stable only up to 42 °C. GluDH-BA exhibited an extreme tolerance towards n-hexane and its respective alcohols. The productivity of GluDH obtained in this study (8.42 mg-GluDH/g-wet cells; 1035 U/g-wet cells) was among the highest productivity reported for recombinant E. coli. With its low K M-value towards glucose (5.5 mM) and NADP(+) (0.05 mM), GluDH-BA was highly suitable for in vivo applications. In this work, a recombinant solvent-tolerant B. subtilis BA overexpressing GluDH-BA was developed and evaluated by coupling with B. subtilis overexpressing an enzyme P450 BM3 F87V for a whole-cell hydroxylation of n-hexane. Significantly higher products obtained clearly proved that B. subtilis BA was an effective cofactor regenerator, a valuable asset for bioproduction of value-added chemicals.
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