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Received August 16, 2012
Accepted November 16, 2012
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Production of cyclic adenosine-3',5'-monophosphate by whole cell catalysis using recombinant Escherichia coli overexpressing adenylate cyclase
State Key Laboratory of Materials-Oriented Chemical Engineering, College of Life Science and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 210009, P. R. China
xiej@njut.edu.cn
Korean Journal of Chemical Engineering, April 2013, 30(4), 913-917(5), 10.1007/s11814-012-0202-1
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Abstract
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.
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Bellalou J, Sarfati RS, Predeleanu R, Enzyme Microb. Technol., 10, 293 (1988)
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