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.