[Carbohydrate component of Penicillium funiculosum dextranase].

The carbohydrate composition of dextranase from Penicillium funiculosum 15, as well as the composition of products of dextran deep hydrolysis by the enzyme were studied. The products are normally used to stabilize the enzyme during its purification. Using the methods available, it was possible to identify only part of strongly bound (adsorbed) carbohydrates.

[Stabilization of dextranase from Penicillium funiculosum and Fusarium solani during heating and freeze-drying].

Freeze-drying of highly purified dextranse from Penicillium funiculosum and Fusarium solani was accompanied by 90% losses of enzyme activity and solubility. Many carbohydrates were tested as stabilizers, e.g.

[Characteristics of asparaginase from Escherichia coli at different stages of purification].

Asparaginase of Escherichia coli obtained according to the previously developed scheme (extraction, acidification, heating with ammonium sulphate, twice repeated precipitation with ethanol and DEAE-cellulose chromatography) was examined by the methods of polyacrylamide gel electrophoresis, isoelectric focusing and molecular weight assay. Asparaginase activity was measured by the Nessler method. With respect to the above characteristics, the asparaginase preparation was very similar to those described in the literature, e.

[Formation of dextranases by mycelial fungi and actinomycetes].

The dextranase activity of cultures of mycelial fungi of different genera and actinomycetes from the Chromogenes species of the Actinomyces genus was studied. About one third of the mycelial fungi and 8% of actinomycetes showed dextranase activity. The resulting extracellular dextranases demonstrated on endotypic pattern of action on the substrate.

[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.