Optimization of the secretion pathway for heterologous proteins in Bacillus subtilis

Abstract

Secretion of homologous proteins in large amounts has been accomplished for many proteins, but no efficient secretion system has been described so far which can be generally applied for heterologous proteins. The objective of this review article is to compare the three major secretion pathways in E. coli and in B. subtilis and review the stages of conversion of the secreted proteins from the unfolded polypeptide chains into the correctly folded and fully active protein. Furthermore, bottlenecks in the production of heterologous proteins and the ways to resolve them are briefly discussed.