title: [Peptidases of preparations of proteolytic enzymes from several species of bacteria, molds and actinomycetes].
abstract: The activity of carboxy- and aminopeptidases of enzymic preparations obtained from bacteria Bacillus subtilis 1 M, 17, Bacillus mesentericus 100/26, 100/56, 16; Pseudomonas aeruginosa 1/7a, 1/4; Bacillus thermophilicus S. sp. nov B-22, moulds Aspergillus oryzae 1-746, Aspergillus flavus 716 and actinomycete Streptomyces griseus 32-13 was studied. In the bacterial preparations the proteolytic activity was 1.5-2.5 times lower than in the fungal and actinomycete preparations. The carboxypeptidase activity of bacterial preparations was comparable with that of the moulds and by one order of magnitude lower than that of the actinomycete. The aminopeptidase activity of the bacterial preparations was different; however, it was comparable with that of the moulds and was higher than that in some cases. In the Streptomyces preparation the aminopeptidase activity was significantly higher than in the bacterial and fungal preparations. In most preparations Co2+ and Mn2+ influenced the activity of carboxy- and amino-peptidases. This suggests that these proteins can be referred to metal enzymes.
mesh_terms: D001231:Aspergillus flavus / Q000201:enzymology; D001236:Aspergillus oryzae / Q000201:enzymology; D001407:Bacillus / Q000201:enzymology; D001412:Bacillus subtilis / Q000201:enzymology; D003035:Cobalt; D004789:Enzyme Activation; D008345:Manganese; D010447:Peptide Hydrolases / Q000032:analysis*; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D013305:Streptomyces griseus / Q000201:enzymology
chemical_list: D003035:Cobalt; D008345:Manganese; D010447:Peptide Hydrolases
vernacular_title: Peptidazy preparatov proteoliticheskikh fermentov nekotorykh vidov bakteriĭ, plesnevykh gribov i aktinomitsetov