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[Fibrinolytic activity of natural variants of Bacillus mesentericus]

A A Imshenetskiĭ, G V Cherkesova, I D Kasatkina

    Mikrobiologiia
    |November 1, 1987
    PubMed

    Insights

    Bacillus mesentericus 64 exhibits natural variability in proteinase synthesis. A highly active M variant demonstrated significantly increased caseinolytic and fibrinolytic activities, crucial for thrombolysis.

    Area of Science:

    • Microbiology
    • Enzymology
    • Biochemistry

    Background:

    • Bacillus mesentericus 64 is known to produce proteinases.
    • The natural variability in proteinase synthesis within bacterial strains can impact their biotechnological applications.
    • Understanding strain heterogeneity is key to optimizing enzyme production.

    Purpose of the Study:

    • To investigate the natural variability in proteinase synthesis by Bacillus mesentericus 64.
    • To characterize different variants of Bacillus mesentericus 64 based on colony morphology and enzymatic activity.
    • To assess the potential of specific variants for applications requiring high proteolytic and fibrinolytic activity.

    Main Methods:

    • Cultivation of Bacillus mesentericus 64 and isolation of distinct colony variants (S, M, P).
    • Microscopic examination and analysis of colony morphology and culture characteristics.
    • Assay of caseinolytic activity.
    • Measurement of fibrinolytic activity and thrombolysis rate in vitro.

    Main Results:

    • The Bacillus mesentericus 64 population was found to be heterogeneous, with three distinct variants (S, M, P) identified.
    • The M variant exhibited significantly higher caseinolytic activity (threefold increase) compared to the parent strain.
    • The M variant also showed enhanced fibrinolytic activity and a high rate of blood thrombolysis in vitro.
    • A correlation was observed between the rate of proteinase synthesis and the morphological types of the sporogenic bacteria.

    Conclusions:

    • Bacillus mesentericus 64 displays significant natural variability in proteinase production.
    • The M variant represents a promising strain for applications requiring potent proteolytic and fibrinolytic enzymes.
    • Morphological characteristics can serve as indicators for proteinase synthesis rates in this bacterium.

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