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Title 

Production of soluble human interleukin-6 in cytoplasm by fed-batch culture of recombinant E. coli

Authors 

Tae Wan KimBong Hyun ChungY K Chang

Publisher 

American Chemical Society

Issue Date 

2005

Citation 

Biotechnology Progress, vol. 21, no. 2, pp. 524-531

Keywords 

bioreactorsbiotechnologycell culturecellsescherichia colimaltosepH effectsproteinsflask cultureshuman interleukin-6 (hIL-6)

Abstract 

The major objective of this study is to identify fed-batch culture conditions optimal for the production of human interleukin-6 (hIL-6) in a soluble form. Five different expression vectors were constructed for the expression of hIL-6 and hIL-6s fused with NusA, maltose binding protein (MBP), thioredoxin (Trx) or ubiquitin (Ubi). A series of flask cultures were conducted in LB medium at 37°C. The intact hIL-6 was expressed mostly in the form of inclusion body. More than 95% of the hIL-6 fused with NusA (NusA/hIL-6) and about 90% of MBP/hIL-6 were expressed in a soluble form, whereas Trx/hIL-6 and Ubi/hIL-6 were expressed mostly in the form of inclusion body. Based on this result, NusA was selected as the fusion partner for the production of hIL-6 in the subsequent experiments. A series of pH-stat fed-batch cultures of an E. coli BL21(DE3) transformed with a NusA/hIL-6 expression vector were conducted in a bioreactor with a working volume of about 3 L. As the amount of nitrogen source was increased in the feeding medium, more soluble NusA/hIL-6 was produced, while the total amount was not significantly changed. Under the best conditions 1 ested, about 90% of NusA/hIL-6 was produced in the soluble form. In this case, the concentration of soluble NusA/hIL-6 was 7.5 g/L with a volumetric productivity of 0.43 g/L-h.

ISSN 

8756-7938

Link 

http://dx.doi.org/10.1021/bp049645j

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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