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alpha,alpha-Trehalase of Trichoderma reesei.

P Vijayakumar, W Ross, E T Reese

    Canadian Journal of Microbiology
    |October 1, 1978
    PubMed
    Summary

    Researchers purified the Trichoderma reesei trehalase enzyme using bentonite adsorption. This simple method significantly boosted enzyme activity and recovery, making it a promising technique for enzyme purification.

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    Area of Science:

    • Biochemistry
    • Enzyme Technology
    • Protein Purification

    Background:

    • Trehalase enzymes are crucial in various biological processes.
    • Efficient purification of Trichoderma reesei trehalase is important for its applications.
    • Bentonite is a clay mineral with adsorbent properties.

    Purpose of the Study:

    • To develop a simple and effective method for purifying Trichoderma reesei trehalase.
    • To characterize the purified alpha,alpha-trehalase.

    Main Methods:

    • Adsorption and elution of trehalase from Trichoderma reesei on bentonite.
    • Determination of enzyme activity, optimum pH, isoelectric point (pI), and Michaelis constant (Km).

    Main Results:

    • A 70-80 fold increase in specific activity was achieved.
    • 90% recovery of the trehalase enzyme was obtained.
    • The purified alpha,alpha-trehalase exhibited an optimum pH of 4.4, pI of 5.7, Km of 3.1 x 10(-3) M, and specific activity of 50 µmol/mg·min⁻¹.

    Conclusions:

    • Simple bentonite adsorption and elution is a highly effective method for purifying Trichoderma reesei trehalase.
    • The characterized enzyme properties provide valuable data for potential biotechnological applications.

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