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

Authors

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

DOI:

https://doi.org/10.14232/abs.2018.1.61-66

Keywords:

cationic antimicrobial peptide, drug resistance, indolicidin, optimization

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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Published

2018-08-23

How to Cite

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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