Efficient production of cyclic adenosine monophosphate from adenosine triphosphate by the N-terminal half of adenylate cyclase from <i>Escherichia coli</i>

Chen Ma; Jing Wang; Xuelin Wang; Dandan Mai; Yuqi Jin; Kequan Chen; Xin Wang; Pingkai Ouyang

doi:10.1016/j.cjche.2020.01.003

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Efficient production of cyclic adenosine monophosphate from adenosine triphosphate by the N-terminal half of adenylate cyclase from Escherichia coli

Biotechnology and Bioengineering | Updated：2026-01-06

- Efficient production of cyclic adenosine monophosphate from adenosine triphosphate by the N-terminal half of adenylate cyclase from Escherichia coli
- Chinese Journal of Chemical Engineering Vol. 28, Issue 8, Pages: 2167-2172(2020)
- Affiliations：
  
  State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University,Nanjing,China,211816
- Author bio：
- Funds：
- DOI：10.1016/j.cjche.2020.01.003
  CLC：
- Published：2020
- Accepted：
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[J]. 中国化学工程学报, 2020, 28(8): 2167-2172.
DOI：

[J]. 中国化学工程学报, 2020, 28(8): 2167-2172. DOI： 10.1016/j.cjche.2020.01.003.

摘要

Abstract

In this study

we aimed at developing an efficient biocatalytic process for bio-production of cyclic adenosine monophosphate (cAMP) from adenosine triphosphate (ATP). First

adenylate cyclase from

Escherichia coli

MG1655 (

EAC

) and

Bordetella Pertussis

(

BAC

) were expressed in

E. coli

BL21 (DE3) and comparatively analyzed for their activities. As a result

EAC from

E. coli

MG1655 exhibited a higher activity. However

amount of EAC were obtained in an insoluble form. Therefore

we expressed the first 446 amino acids of

EAC

(

EAC446

) to avoid the inclusion body. The effects of induction temperature

incubation time

and incubation pH were further evaluated to improve the expression of

EAC

446. Subsequently

the reaction process for the production of cAMP with ATP as a starting material was investigated. As none of cAMP was detected in the whole-cell based biocatalytic process

the reaction catalyzed by the crude enzyme was determined for cAMP production. What's more

the reaction temperature

reaction pH

metal ion additives and substrate concentration was optimized

and the maximum

cAMP production of 18.45 g·L

-1

was achieved with a yield of 95.4% after bioconversion of 6 h.

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⁰

Efficient production of cyclic adenosine monophosphate from adenosine triphosphate by the N-terminal half of adenylate cyclase from Escherichia coli

DOI：10.1016/j.cjche.2020.01.003

摘要

Abstract

关键词

Keywords

references