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[Substrate specificity of enzymes from Bacillus mesentericus]

N G Nesterova, G V Cherkesova, N F Kirillova

    Mikrobiologiia
    |July 1, 1989
    PubMed

    Insights

    Proteolytic enzymes from Bacillus mesentericus strains 64 and 8 were isolated and analyzed. Strain 64

    Area of Science:

    • Enzymology
    • Microbiology
    • Biochemistry

    Background:

    • Bacillus mesentericus strains are known producers of proteolytic enzymes.
    • Understanding the specific activities of these enzymes is crucial for potential biotechnological applications.

    Purpose of the Study:

    • To isolate and characterize proteolytic enzymes from Bacillus mesentericus strains 64 and 8.
    • To compare the substrate specificity and activity of these enzymes with a commercial preparation, terrilytin.

    Main Methods:

    • Proteolytic enzymes were isolated using affinity chromatography on bacillichine-silochrome.
    • Enzyme activity was assessed using various protein substrates (casein, hemoglobin, elastin, albumin) and synthetic peptides.
    • Esterase activity was measured via indophenyl acetate cleavage.

    Main Results:

    • The proteinase from strain 64 showed activity against casein, hemoglobin, and elastin, with specificity similar to terrilytin.
    • The proteinase from strain 8 exhibited higher thrombolytic and fibrinolytic activity, along with significant esterase activity.

    Conclusions:

    • Bacillus mesentericus strains 64 and 8 produce distinct proteolytic enzymes with unique substrate specificities and activities.
    • The enzyme from strain 8 demonstrates potential for applications requiring thrombolytic, fibrinolytic, and esterase functions.

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