A simple method for the isolation and purification of L-asparaginase from Enterobacter aerogenes.
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.
Mukherjee
J
J
Institut für Technische Chemie der Universität Hannover, Germany.
Joeris
K
K
Riechel
P
P
Scheper
T
T
D001215:Asparaginase / Q000302:isolation & purification*; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002850:Chromatography, Gel; D004754:Enterobacter / Q000737:chemistry*; D013010:Sonication; D014462:Ultrafiltration
D001426:Bacterial Proteins; D001215:Asparaginase