Background: Secretory production of recombinant protein in bacterial hosts fulfills
several advantages. Selecting an appropriate secretory signal peptide is a critical step in secretory
production of different protein. Several patents report the usage of signal peptides for secretory
production of recombinant proteins in E. coli. In silico identification of suitable signal peptides is
a reliable and cost-effective alternative to experimental approaches.
Objective: This study was aimed to predict best signal peptides for the secretory production of recombinant
arginine deiminase in E. coli.
Methods: In this study, 30 different signal peptide sequences were retrieved from database. The
signal peptide probability, location of cleavage sites, and n, h and c regions were predicted by
SignalP 4.1 and Phobius servers. After purging the 30 predicted secretory signal peptides, TorT,
bla, NrfA, TolB, PapC, PldA, Lpp were removed. Several physicochemical properties of the remaining
potential SPs were determined by ProtParam, PROSO II, and SOLpro servers for theoretically
selecting the best candidates.
Results and Conclusion: Based on physicochemical properties, the signal peptides of OmpC,
OmpF, and DsbA were identified respectively as the promising candidates for efficient secretory
production of arginine deiminase in E. coli. Although the computational approach has established
itself as a basis of modern biotechnology, the experimental study is necessary to validate its results.
The criteria used in this study could be applied to other targets for recombination processes.