Production of cyclic adenosine-3′,5′-monophosphate by whole cell catalysis using recombinant Escherichia coli overexpressing adenylate cyclase

Adenylate cyclase (EC 4. 6. 1. 1) catalyzes the formation of cyclic adenosine-3′,5′-monophosphate (cAMP) from adenosine 5′-triphosphate (ATP). Recombinant Escherichia coli overexpressing adenylate cyclase was used to synthesize cAMP by whole cell catalysis. Some key parameters were examined during the catalytic process, while pH and Mg²⁺ were found to influence cAMP production significantly. Optimum conditions were pH 8. 52 and 30 °C with 77. 2 mM Mg²⁺ in 100 mM Tris-HCl buffer, including 0. 25% Triton-X 100 as detergent and 30 mM pyruvate sodium as enzyme activator for 6 h. 14. 93 g/L of cAMP was produced with a conversion rate of 91. 5%. The current work provided a potential way for the industrial production of cAMP.