The use of antimicrobial peptides (AMPs) as biopreservative to replace chemical preservatives has become of interest among consumers. Current approaches of production and purification of AMPs are time-consumingand costly and may kill the producing host cells. In this study a recombinant peptide was patterned from Lasioglossin LL ΙΙΙ which is found naturally in the venom of eusocial bee, this recombinant peptide was produced to inhibit food microbial degradation with the least possible costs. The synthesis of this peptide in the periplasmic space of Escherichia coli, has facilitated the production and purification of this additive. The pET based expression system for production of a recombinant form of Lasioglossin LL ΙΙΙ using E. coli as a host was developed. The antibacterial and antioxidant activities of recombinant peptide were determined. A C-terminal poly histidine tag was used to facilitate purification by standard methods using Ni2+ affinity chromatography. The average yield of the recombinant peptide was 0.7g/L. The findings showed great antimicrobial function of the peptide. The antioxidant activity of the peptide was lower than Butylated hydroxytoluene (BHT) synthesized antioxidant as a common antioxidant but the antioxidant potential of the peptide along with the antimicrobial activity against foodborne pathogens have shown promising benefits of the peptide. These results demonstrated that pET expression system is appropriate for the rapid and simple isolation of recombinant lasioglossin LL ΙΙΙ from E. coli and the recombinant peptide could be used as a natural preservative source. However, further studies need to be carried out to check the effect of this peptide on more microorganisms.

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