Development of a secretion system for the production of heterologous proteins in Corynebacterium glutamicum using the Porin B signal peptide

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Corynebacterium glutamicum is one of the useful hosts for the secretory production of heterologous proteins because of intrinsic attributes such as the presence of few endogenous proteins and proteases in culture medium. Here, we report the development of a new secretory system for the production of heterologous proteins by using the porin B (PorB) signal peptide in C glutamicum. We examined two different endoxylanases and an antibody fragment (scFv) as model proteins for secretory production. In the flask cultivations, all the examined proteins were successfully produced as active forms into the culture medium with high efficiency. For the high-level production of endoxylanase, fed-batch cultivation was also performed in a lab-scale (5 L) bioreactor, and the endoxylanases were efficiently secreted in the culture medium at levels as high as 615 mg/L. From the culture supernatant, the secreted endoxylanases could be purified with high purity via one-step affinity column chromatography. (C) 2013 Elsevier Inc. All rights reserved.
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Issue Date
2013-06
Language
English
Article Type
Article
Citation

PROTEIN EXPRESSION AND PURIFICATION, v.89, no.2, pp.251 - 257

ISSN
1046-5928
DOI
10.1016/j.pep.2013.04.003
URI
http://hdl.handle.net/10203/174020
Appears in Collection
BS-Journal Papers(저널논문)CBE-Journal Papers(저널논문)
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