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

Nan Li; Ying He; Yong Chen; Xiaochun Chen; Jianxin Bai; Jinglan Wu; Jingjing Xie; Hanjie Ying

Korean Journal of Chemical Engineering, Vol.30, No.4, 913-917, April, 2013

DOI10.1007/s11814-012-0202-1 Export Citation

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

Nan Li, Ying He, Yong Chen, Xiaochun Chen, Jianxin Bai, Jinglan Wu, Jingjing Xie^†, and Hanjie Ying^†

State Key Laboratory of Materials-Oriented Chemical Engineering, College of Life Science and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 210009, P. R. China

E-mail:,

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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[2] Buettner MJ, Spitz E, Rickenberg HV, J. Bacteriol., 14, 1068 (1973)

[3] Adelstein RS, Hathaway DR, Am. J. Cardiol., 44, 783 (1979)

[4] Ando S, Kametani H, Osada H, Iwamoto M, Kimura N, Brain Res., 405, 371 (1987)

[5] Antoni FA, Front. Neuroendocrin., 21, 103 (2000)

[6] Sands WA, Palmer TM, Cell Signal., 20, 460 (2008)

[7] Hoonekamp PM, Bone., 6, 37 (1985)

[8] Tsai SF, Yang C, Wang SC, Wang JS, Hwang JS, Ho SP, Toxicol. Appl. Pharm., 194, 34 (2004)

[9] Kawada T, Yoshida Y, Imai S, Br. J. Pharmacol., 97, 371 (1989)

[10] Hong D, Peng XR, Chin. Pharmacol. Bull., 19, 940 (2003)

[11] Mcphee I, Gibson LCD, Kewney J, Darroch C, Stevens PA, Spinks D, Biochem. Soc. Trans., 33, 1330 (2005)

[12] Hirata M, Hayaishi O, Biochim. Biophys. Acta., 149, 1 (1976)

[13] Ishiyama J, Appl. Microbiol. Biotechnol., 34, 359 (1990)

[14] Chen XC, Song H, Fang T, Cao JM, Ren HJ, Bai JX, Xiong J, Ouyang PK, Ying HJ, Bioresour. Technol., 101(9), 3159 (2010)

[15] Ishige T, Honda K, Shimizu S, Curr. Opin. Chem. Biol., 9, 174 (2005)

[16] Wang X, Ma CQ, Wang XW, Xu P, J. Bacteriol., 189, 9030 (2007)

[17] Iyer PV, Ananthanarayan L, Process Biochem., 43, 1019 (2008)

[18] Chakraborty AA , Phadke RP, Chaudhary FA, Shete PS, Rao BS, Jasani KD, World J. Microbiol. Biotechnol., 21, 221 (2005)

[19] Zhou JW, Huang L, Lian JZ, Sheng JY, Cai J, Xu ZN, Biotechnol. Lett., 32(10), 1481 (2010)

[20] Gough S, Dostal L, Howe A, Deshpande M, Scher M, Rosazza JNP, Process Biochem., 40, 2597 (2005)

[21] Goldberg K, Schroer K, Lutz S, Liese A, Appl. Microbiol. Biotechnol., 76(2), 237 (2007)

[22] He Y, Li N, Chen Y, Chen XC, Bai JX, Wu JL, Xie JJ, Ying HJ, Appl. Microbiol. Biotechnol., DOI: 10.1007/s00253-012-3890-x. PMID:22290647 (2012 Jan. 31).

[23] Chen RRZ, Appl. Microbiol. Biotechnol., 74(4), 730 (2007)

[24] de Carvalho CCCR, Biotechnol. Adv., 29, 75 (2011)

[25] Bellalou J, Sarfati RS, Predeleanu R, Enzyme Microb. Technol., 10, 293 (1988)

[26] Bradford MM, Anal. Biochem., 72, 248 (1976)

[27] Chen XC, Bai JX, Cao JM, Li ZJ, Xiong J, Zhang L, Hong Y, Ying HJ, Bioresour. Technol., 100(2), 919 (2009)

[28] Li Y, Lu J, J. Am. Soc. Brew. Chem., 63, 171 (2005)

[29] Schnaitman CA, J. Bacteriol., 108, 545 (1971)