High-Level Production of Bacillus subtilis Glycine Oxidase by Fed-Batch Cultivation of Recombinant Escherichia coli Rosetta (DE3)

2008 ◽  
Vol 23 (3) ◽  
pp. 645-651 ◽  
Author(s):  
Irene Martínez-Martínez ◽  
Christian Kaiser ◽  
Alexander Rohde ◽  
Andree Ellert ◽  
Francisco García-Carmona ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Batch Cultivation ◽  
Recombinant Escherichia Coli ◽  
Fed Batch ◽  
High Level ◽  
Level Production ◽  
Glycine Oxidase ◽  
Fed Batch Cultivation

High-level production of trans-cinnamic acid by fed-batch cultivation of Escherichia coli

2018 ◽  
Vol 68 ◽  
pp. 30-36 ◽  
Author(s):  
Hyun Bae Bang ◽  
Kyungsoo Lee ◽  
Yong Jae Lee ◽  
Ki Jun Jeong
Keyword(s):  
Escherichia Coli ◽  
Cinnamic Acid ◽  
Batch Cultivation ◽  
Fed Batch ◽  
High Level ◽  
Level Production ◽  
Fed Batch Cultivation

High level production of human proapo A-I by fed-batch culture of recombinant Escherichia coli

1993 ◽  
Vol 75 (2) ◽  
pp. 155-157 ◽  
Author(s):  
Kunihiko Ohta ◽  
Tatsuro Shibui ◽  
Yuuki Morimoto ◽  
Shinji Iijima ◽  
Takeshi Kobayashi
Keyword(s):  
Escherichia Coli ◽  
Batch Culture ◽  
Recombinant Escherichia Coli ◽  
Fed Batch ◽  
Fed Batch Culture ◽  
High Level ◽  
Level Production

scholarly journals High-Level Production of Human Leptin by Fed-Batch Cultivation of Recombinant Escherichia coli and Its Purification

1999 ◽  
Vol 65 (7) ◽  
pp. 3027-3032 ◽  
Author(s):  
Ki Jun Jeong ◽  
Sang Yup Lee
Keyword(s):  
Escherichia Coli ◽  
Total Protein ◽  
Anion Exchange Chromatography ◽  
Batch Cultivation ◽  
Exchange Chromatography ◽  
Total Protein Content ◽  
Fed Batch ◽  
T7 Promoter ◽  
High Level ◽  
Level Production

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%.

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