Optimization of recombinant Analgesic peptides production in Bacterial Cultures by using Taguchi Method

Abstract

E.coli has several advantages over other higher organisms like yeast, plant, insects and other mammalian
cells in production of recombinant proteins and scale up of production process. E.coli has three
chambers for production of recombinant proteins that incorporates a periplasm, cytoplasm &
extracellular medium. Depending upon the chambers utilized for synthesis, various methods can be
developed for optimum levels production of functional analgesic opioid peptides. The reduction of
cytoplasm makes a desirable region for high leve production of analgesic opioid peptides, that do not
demand disulfide bond making for their poteintialities. E. coli is one of the favourite host for the
synthesis of various small peptides, however it is one of the toughest for production of full protein due to
of be deficient in glycosylation process and weak assemblage of peptide molecules. The full length
studies of protein in Eschrischia coli, although the productivity were not as desired (~149 mg in 72-h
cultivation soluble full length of IgG/L). However, in E. coli, up to 4g/l of high level volumetric
productivities can be obtained using high cell density cultivations (HCDC)