Abstract
Secretory expression of valuable enzymes by Bacillus subtilis and its related species has attracted intensive work over the past three decades. Although many proteins have been expressed and secreted, the titers of some recombinant enzymes are still low to meet the needs of practical applications. Signal peptides that located at the N-terminal of nascent peptide chains play crucial roles in the secretion process. In this mini-review, we summarize recent progress in secretory expression of recombinant proteins in Bacillus species. In particular, we highlighted and discussed the advances in molecular engineering of secretory machinery components, construction of signal sequence libraries and identification of functional signal peptides with high-throughput screening strategy. The prospects of future research are also proposed.
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Acknowledgments
We appreciate Professor Byong Lee at Jiangnan University for his discussion and revision. This work was financially supported by the National High Technology Research and Development Program of China (863 Program, 2011AA100905), Program for Changjiang Scholars and Innovative Research Team in University (no. IRT1135), the Natural Science Foundation of Jiangsu Province (BK20141107), China Postdoctoral Science Foundation ((2013M540414), the 111 Project, and the Priority Academic Program Development of Jiangsu Higher Education Institutions.
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Kang, Z., Yang, S., Du, G. et al. Molecular engineering of secretory machinery components for high-level secretion of proteins in Bacillus species. J Ind Microbiol Biotechnol 41, 1599–1607 (2014). https://doi.org/10.1007/s10295-014-1506-4
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DOI: https://doi.org/10.1007/s10295-014-1506-4