Production and Optimization of L-Asparaginase from Pseudomonas Aeruginosa by Strain Improvement.

Enzymes are biomolecules or proteins materials that catalyze chemical reactions. In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, called the products. Almost all processes in a biological cell need enzymes to occur at significant rates. Since enzymes are selective for their substrates and speed up only a few reactions from among many possibilities, the set of enzymes made in a cell determines which metabolic pathways occur in that cell. The discovery of the fact that L-Asparaginase is responsible for the action of the guineapig serum against the acute lymphoblastic leukemia has set a milestone in the field of medicine. After this discovery detailed information about the enzyme has been dug out. It has been proved that L-Asparaginase from Escherichia coli and Erwinia carotovora has anti-neoplastic activity against cancer and is being used as anti-cancer drug. Microbial L-Asparaginase has been widely used as a therapeutic agent in the treatment of certain human cancers. With the development of its new functions a great demand for Lasparaginase is expected in the coming years molecular weight using SDS-PAGE. the result showed that the M wt of L-asparaginase was 160 kDa when compared with standard molecular weight protein marker. To conclude that this study showed by mutation of the strain by UV irradiation, Immobilization of the whole cell and optimization of the basic fermentation media the production of L-asparaginase from Pseudomonas aeruginosa was increased up to 1.55 folds that gives hope to increase the productivity of L-asparaginase which will meet the demand of patients around the worl