Objective: We used 50-amino acid-long peptides from the N-terminus of 4 different non-classically secreted proteins to study the secretion efficiency of Bacillus subtilis LipaseA via non-classical secretion pathway.
Methods: We amplified the coding sequences (CDs) of LipaseA and N-terminus of non-classically secreted proteins, constructed 8 fusion protein expression vectors containing both LipaseA CD and different secretion signal peptide and transformed them into B. subtilis WB800. Secretion efficiency of these fusion proteins was analyzed by enzyme activity, SDS-PAGE and Western-Blot.
Results: Recombinant LipaseA containing coding sequences of PdhA or N-terminus of SodA and Eno as secretion signals was efficiently secreted.
Conclusion: Parts of non-classically secreted proteins or N-terminus (50 amino acids) could guide LipaseA protein secretion.