Expression and production optimization of the cationic antimicrobial peptide - indolicidin by the recombinant E. coli C41 (DE3) clones

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Kanesan Panneer Selvam
Guruvu Nambirajan
Balasubramaniam Annamalai
Mohammed Alaidarous
Bader Mohammed Alshehri
Abdul Aziz A. Bin Dukhyil
Coimbatore Subramanian Shobana
Palanisamy Manikandan

Abstract

The cytoplasmic granules of bovine neutrophils naturally possess indolicidin - a promising cationic antimicrobial peptide as it displays inherent inhibitory activities against a broad type of microbial pathogens. In this study, a shake flask level production and expression optimizations of the indolicidin by the recombinant Escherichia coli C41 (DE3) clones (transformed with pET21a(+) plasmid carrying indolicidin gene) were carried out under standard conditions, as to determine the conditions required for maximal production. It was determined that a concentration of 1 mM of IPTG was effective, the 2×YT with salts and LB media at pH 7.5 with 3-6 h of incubation were required for maximal indolicidin expression.

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Selvam, K. P., Nambirajan, G., Annamalai, B., Alaidarous, M., Alshehri, B. M., Bin Dukhyil, A. A. A., Shobana, C. S. and Manikandan, P. (2018) “Expression and production optimization of the cationic antimicrobial peptide - indolicidin by the recombinant E. coli C41 (DE3) clones”, Acta Biologica Szegediensis, 62(1), pp. 61–66. doi: 10.14232/abs.2018.1.61-66.
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