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[Serine proteases from Bac. subtilis].

V I Palubinskas, V S Vesa, A A Glemzha

    Biokhimiia (Moscow, Russia)
    |December 1, 1976
    PubMed
    Summary
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    Three distinct serine proteases were isolated from Bacillus subtilis using biospecific adsorption and gel filtration. These enzymes exhibit varied molecular weights and pH optima, indicating diverse functional properties.

    Area of Science:

    • Biochemistry
    • Enzymology

    Context:

    • Bacillus subtilis is a common soil bacterium known for producing various enzymes.
    • Proteases are crucial enzymes involved in protein hydrolysis.
    • Characterizing microbial enzymes is essential for biotechnological applications.

    Purpose:

    • To isolate and characterize serine proteases from Bacillus subtilis.
    • To determine the physicochemical properties of the isolated serine proteases, including molecular weight and pH optima.

    Summary:

    • Biospecific adsorption and Sephadex G-75 gel filtration were employed to isolate three serine protease fractions (I-III) from Bacillus subtilis.
    • Protease I: MW 23,000-24,000, pH optimum 6.5, activation energy 16.6 kcal/mol.
    • Protease II: MW 29,000, pH optimum 11.0, activation energy 14.4 kcal/mol.

    Related Experiment Videos

  • Protease III: Mixture with average MW 26,000 and pH optima at 7.0, 8.5, and 11.0.

    • Impact:

    • The study provides a detailed characterization of serine proteases from Bacillus subtilis.
    • The identified enzymes with distinct properties could have potential applications in various industrial processes.
    • This research contributes to the understanding of microbial enzyme diversity and function.