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

被引：6

作者：

Li, Nan ^{[1
]}

He, Ying ^{[1
]}

Chen, Yong ^{[1
]}

Chen, Xiaochun ^{[1
]}

Bai, Jianxin ^{[1
]}

Wu, Jinglan ^{[1
]}

Xie, Jingjing ^{[1
]}

Ying, Hanjie ^{[1
]}

机构：

[1] Nanjing Univ Technol, Coll Life Sci & Pharmaceut Engn, State Key Lab Mat Oriented Chem Engn, Nanjing 210009, Peoples R China

来源：

KOREAN JOURNAL OF CHEMICAL ENGINEERING | 2013年 / 30卷 / 04期

基金：

高等学校博士学科点专项科研基金;

关键词：

cAMP; Adenylate Cyclase; Whole Cell Catalysis; Bioconversion; RESPONSE-SURFACE METHODOLOGY; AMP; MONOPHOSPHATE; BIOCATALYSIS; OPTIMIZATION; MEMBRANE; MUSCLE;

D O I：

10.1007/s11814-012-0202-1

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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 degrees C 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.

引用

页码：913 / 917

页数：5

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