Purification and characterization of L-asparginase producing bacteria MNTG-7

Abstract

Several techniques have been described for recovery and purification of L-asparaginase from different sources. The present
study was undertaken to recover and purify L-asparaginase from mutated MNTG-7 cell line using three-step procedure
involving ammonium sulphate precipitation, ion exchange and gel filtration chromatography followed by the characterization
of the purified enzyme. Protein molecular mass markers, DEAE cellulose and Sephadex G-200 matrices, Agarose,
acrylamide, bis-acrylamide, sodium dodecyl sulfate (SDS), TEMED, ammonium persulphate and bovine serum albumin were
used in the purification process.