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Issue
Korean Journal of Chemical Engineering,
Vol.30, No.4, 913-917, 2013
Production of cyclic adenosine-3',5'-monophosphate by whole cell catalysis using recombinant Escherichia coli overexpressing adenylate cyclase
Li N, He Y, Chen Y, Chen X, Bai J, Wu J, Xie J, Ying H
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 ℃ 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.
Keywords: cAMP; Adenylate Cyclase; Whole Cell Catalysis; Bioconversion
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