<i>In silico</i> analysis of suitable signal peptides for secretion of a recombinant alcohol dehydrogenase with a key role in atorvastatin enzymatic synthesis.

Abstract

using signal peptides (SPs) might result in easy production and purification. To achieve this objective, we used some online bioinformatics web servers to evaluate the suitable SPs for translocation of LKADH into extracellular spaces. "Signal Peptide Website" and "UniProt" were utilized to retrieve the SPs and LKADH sequences. "SignalP 4.1" was used to determine SPs and their cleavage site location and the results were rechecked by "Philius". Physicochemical features of SPs were evaluated by "ProtParam", then solubility of their fusion with LKADH was assessed by "Protein-sol". Finally, secretion pathway and sub-cellular localization of the selected stable and soluble LKADH fusions were predicted by "PRED-TAT" and "ProtCompB". Amongst the 41 evaluated SPs, only LPTA_ECOLI, SUBF_BACSU, CHIS_BACSU, SACB_BACAM, CDGT_BACST and AMY_BACLI could translocate LKADH out of cytoplasm. The six selected SPs in the result section were suitable to design a soluble secretory LKADH that accelerate its scale-up production and might be useful in future experimental researches.