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

• Published in: The Korean journal of chemical engineering Vol. 30; no. 4; pp. 913 - 917
• Main Authors: Li, Nan, He, Ying, Chen, Yong, Chen, Xiaochun, Bai, Jianxin, Wu, Jinglan, Xie, Jingjing, Ying, Hanjie
• Format: Journal Article
• Language: English
• Published: Boston Springer US 01-04-2013; 한국화학공학회
• Subjects: Biotechnology; Catalysis; Chemistry; Chemistry and Materials Science; Industrial Chemistry/Chemical Engineering; Materials Science; 화학공학; Adenylate Cyclase; Bioconversion; Whole Cell Catalysis; cAMP
• ISSN: 0256-1115; 1975-7220
• DOI: 10.1007/s11814-012-0202-1

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 Mg
2+
were found to influence cAMP production significantly. Optimum conditions were pH 8.52 and 30 °C with 77.2 mM Mg
2+
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.