title: A simple method for the isolation and purification of L-asparaginase from Enterobacter aerogenes.
abstract: L-Asparaginase from Enterobacter aerogenes was purified by a simple method involving sonication of the crude cell mass, gel filtration with Sephacryl S-100 as the separating material, followed by ultrafiltration. Recent methods involve complex purification procedures of 5-6 steps. The isolation process resulted in 10-fold purification of the enzyme with a specific activity of 55 IU/mg protein and recovery of 54%. The purity was tested by capillary electrophoresis, used for the first time for documenting the purification of L-asparaginase. The choice of the column material was critical in the purification process.
authors.affiliation: Institut für Technische Chemie der Universität Hannover, Germany.
authors.forename: J
authors.initials: J
authors.lastname: Mukherjee
authors.forename: K
authors.initials: K
authors.lastname: Joeris
authors.forename: P
authors.initials: P
authors.lastname: Riechel
authors.forename: T
authors.initials: T
authors.lastname: Scheper
mesh_terms: D001215:Asparaginase / Q000302:isolation & purification*; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002850:Chromatography, Gel; D004754:Enterobacter / Q000737:chemistry*; D013010:Sonication; D014462:Ultrafiltration
chemical_list: D001426:Bacterial Proteins; D001215:Asparaginase