Effect of non-classical secreted proteins on LipaseA secretion

Abstract:

Abstract:［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 (50amino acids) could guide LipaseA protein secretion．