For the first time, the process development research team at c-LEcta has succeeded in creating and screening a signal peptide bank directly in the company’s proprietary high-performance Bacillus production strain.
When we think of Bacillus as a production host, we think of its secretion power: the ability to export proteins across the membrane directly into the growth medium. The efficiency of the secretion depends, among many other factors, on an export signal, called signal peptide. The signal peptide is fused to the gene of interest and plays a key role in the translocation of the newly synthesized protein. However, there is no single signal peptide that acts equally efficiently on a variety of target enzymes. Therefore, the best combination of signal peptide and target enzyme needs to be screened by creating libraries of hundreds of different signal peptide / target protein combinations. So far, the generation of such libraries was performed in a so-called screening host and the selected signal peptide-enzyme combinations were then transferred to a production host. This process was limited by the transformability of the host strain.
The process development research team at c-LEcta have now elaborated a very efficient protocol for the transformation of the production strain, enabling the construction and screening of signal peptide libraries directly in the production strain. A transfer between Bacillus screening host and production host is no longer necessary. This is an important methodological achievement in improving c-LEcta's Bacillus Technology.
The new approach was established as part of the development of a new enzyme product. As a direct result of this new methodology, the secretion yield of the enzyme of interest was increased almost 30-fold. This is an important milestone in the expression of the new enzyme, which will most likely also be produced on an industrial scale in the near future.
Learn more about c-LEctas Technology platform ENESYZ.