High‐level production of d ‐pantothenic acid from glucose by fed‐batch cultivation of Escherichia coli

Author(s):  
Shu‐Ping Zou ◽  
Zhi‐Jian Wang ◽  
Kuo Zhao ◽  
Bo Zhang ◽  
Kun Niu ◽  
...  
2018 ◽  
Vol 68 ◽  
pp. 30-36 ◽  
Author(s):  
Hyun Bae Bang ◽  
Kyungsoo Lee ◽  
Yong Jae Lee ◽  
Ki Jun Jeong

2008 ◽  
Vol 23 (3) ◽  
pp. 645-651 ◽  
Author(s):  
Irene Martínez-Martínez ◽  
Christian Kaiser ◽  
Alexander Rohde ◽  
Andree Ellert ◽  
Francisco García-Carmona ◽  
...  

1999 ◽  
Vol 65 (7) ◽  
pp. 3027-3032 ◽  
Author(s):  
Ki Jun Jeong ◽  
Sang Yup Lee

ABSTRACT Human leptin is a 16-kDa (146-amino-acid) protein that is secreted from adipocytes and influences body weight homeostasis. In order to obtain high-level production of leptin, the human obesegene coding for leptin was expressed in Escherichia coliBL21(DE3) under the strong inducible T7 promoter. The recombinant leptin was produced as inclusion bodies in E. coli, and the recombinant leptin content was as high as 54% of the total protein content. For production of recombinant human leptin in large amounts, pH-stat fed-batch cultures were grown. Expression of leptin was induced at three different cell optical densities at 600 nm (OD600), 30, 90, and 140. When cells were induced at an OD600 of 90, the amount of leptin produced was 9.7 g/liter (37% of the total protein). After simple purification steps consisting of inclusion body isolation, denaturation and refolding, and anion-exchange chromatography, 144.9 mg of leptin that was more than 90% pure was obtained from a 50-ml culture, and the recovery yield was 41.1%.


PLoS ONE ◽  
2011 ◽  
Vol 6 (5) ◽  
pp. e20265 ◽  
Author(s):  
Yangkai Duan ◽  
Zhi Zhu ◽  
Ke Cai ◽  
Xiaoming Tan ◽  
Xuefeng Lu

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