[Isolation of the proteolytic complex from industrial waste waters from streptomycin production].

Dynamics of industrial biosynthesis of polyenzymic Streptomyces griseus system proteases and changes in their activities are studied in the process of streptomycin production. The method to isolate protease preparations is developed with optimization of production cycles of the stabilization, vacuum-concentration, ballast protein salting-out and lyophilization stages. The preparation is low toxic, retains 98% of the proteolytic activity at the temperature of 60 degrees C, 30 and 80%--under the effect of EDTA and urea, the activity maximum is at pH 7.

[Physicochemical and enzymatic properties of Aspergillus oryzae aminopeptidase].

The paper deals with properties of Aspergillus oryzae (strain KC) purified aminopeptidase. The enzyme is homogeneous in electrophoresis in polyacrylamide gel and enzyme-electrophoresis with the synthetic substrate leucyl-beta-naphthylamide applied. The molecular mass is 60000-61000 Daltons.

[Effect of SH-reagents and thiol compounds on aminopeptidase from Aspergillus oryzae].

It is shown that iodacetate and iodacetamide produce an insignificant inhibition of the Asp. oryzae aminopeptidase activity, para-chloromercuribenzoate is a stronger inhibitor. Dithiotreitol, beta-mercaptoethanol, reduced glutathione also cause a considerable loss in the enzyme activity.

[Immobilization of aspergillus oryzae aminopeptidase on organic and inorganic carriers].

The process of Asp. oryzae aminopeptidase immobilization on organic (AE-cellulose, sepharose 4B, Sephadex G-200) and inorganic (SCh-2, SCh-3 sylochromes and KCK N 1 silicagel) carriers was studied. Aminopeptidase immobilized on Sephadex G-200 contains the largest amount of protein (80 mg per 1 g of carrier) and is the most active of all other preparations.

[Properties of immobilized complexes of Streptomyces griseus proteases on different carriers].

A complex of Str. griseus proteases was obtained. The proteases were immobilized on Sephadex G-200 and agarose by the bromo-cyanogen method and on the microcrystalline cellulose by means of TiCl3.

[Role of metal ions in the catalytic activity of Aspergillus oryzae aminopeptidase].

The paper deals with the role of metals in the catalytic action of Asp. oryzae aminopeptidase. Cobalt ions are more specific activators than Mn2+ and Mn2+ and evoke its maximal activity.