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Protein Expr Purif. 2013 Jun;89(2):251-7. doi: 10.1016/j.pep.2013.04.003. Epub 2013 Apr 15.

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

Author information

1
Department of Chemical and Biomolecular Engineering, KAIST, Yuseong-gu, Daejeon 305-701, Republic of Korea.

Abstract

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 (5L) bioreactor, and the endoxylanases were efficiently secreted in the culture medium at levels as high as 615mg/L. From the culture supernatant, the secreted endoxylanases could be purified with high purity via one-step affinity column chromatography.

PMID:
23597779
DOI:
10.1016/j.pep.2013.04.003
[Indexed for MEDLINE]

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