Up Scaling Strategies to Improve the Industrial Production of Bacitracin at Largescale.

Abstract

Bacitracin was discovered and named after a 7 year old American girl, Margaret Tracey in 1943 as Bacillus was isolated from her wounds. Bacillus licheniformis is usually present in soil and bird feathers. This bacterium is most commonly present around back plumage and chest of birds. There are different types of bacitracin but the one most potent is Bacitracin A. Bacitracin induced proteins are localized in bacterial membrane. Production of antibiotic initially stopped, resumed by induction of bacitracin induced protein but after few mitotic divisions microbes reverted to their vulnerable state. Induction of protein ceases after 4th hour of stationary phase. Immobilization is necessary for economic, process convenience and stability of the cell. Moreover, immobilization increases the ability of the cell to produce product in high quantity. Maximum production of antibiotic was noted at pH 8 after 4 hours of incubation at various glucose concentrations in shake flask fermentation at 30°C when immobilized in polyacrylamide gel. Increase in antibiotic activity was also found with increase in use of cells. Efforts have been made to alter heterocyclic metal binding subunit of bacitracin by synthesizing heterocyclic building blocks that can be coupled to linear decapeptide and consequently cyclization by PCPTE biodomain of bacitracin. Derivatives of bacitracin showed antimicrobial activities indicating the possibility of overcoming existing limitations just by altering their heterocyclic subunit. Bioactivity and stability can be increased by modifying peptide backbone of compounds.