[Effect of different pH values on the activity and quaternary structure of asparaginase in Escherichia coli extracts]

The effect of low pH values on the activity and stability of the quaternary structure of asparaginase from Escherichia coli was investigated at early stages of purification of the enzyme. Acidification of the E. coli extract was most effective before the biomass separation. This procedure helped to separate biomass together with coagulated ballast proteins and not to reduce the activity. Upon storage of the acidified solution at 5 degrees C reversible dissociation of the tetrametric structure into dimers and monomers occurred. Stability of L-asparaginase in the storage of acetone powders and during extraction was studied. It is suggested that asparaginase in bacterial cells in unlikely to have the quaternary structure which normally occurs in the solution at neutral pH.