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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.

Kinetic properties and stability of glucose dehydrogenase from Bacillus amyloliquefaciens SB5 and its potential for cofactor regeneration