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Related Experiment Videos

Properties of cellulase from Trichoderma viride.

J K Gupta, Y P Gupta

    Folia Microbiologica
    |January 1, 1979
    PubMed
    Summary

    Trichoderma viride cellulase efficiently breaks down carboxymethyl cellulose at optimal pH 4.5 and 55°C. Heavy metal ions like silver and mercury inhibit its activity.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Microbial Biotechnology

    Background:

    • Cellulases are crucial enzymes for biomass degradation.
    • Trichoderma viride is a known producer of industrially relevant cellulases.
    • Understanding enzyme kinetics and optimal conditions is vital for industrial applications.

    Purpose of the Study:

    • To characterize the cellulase enzyme from Trichoderma viride.
    • To determine the kinetic parameters (Km) of the enzyme.
    • To identify optimal temperature and pH for cellulase activity and assess inhibitor effects.

    Main Methods:

    • Enzyme kinetic assays using carboxymethyl cellulose as substrate.
    • Determination of Michaelis constant (Km).
    • pH and temperature profile analysis.
    • Inhibition studies with various metal ions and anions.

    Main Results:

    • The cellulase exhibited a Michaelis constant (Km) of 4.9 g/L for carboxymethyl cellulose.
    • The optimal pH for enzyme activity was determined to be 4.5.
    • The optimal temperature for the enzyme was found to be 55°C.
    • Significant inhibition was observed in the presence of Ag+, Hg2+, Zn2+, Cu2+, and N3-.

    Conclusions:

    • Trichoderma viride cellulase demonstrates specific kinetic and activity profiles.
    • The enzyme functions optimally under acidic conditions and elevated temperatures.
    • The enzyme's activity is sensitive to specific heavy metal ions and anions, indicating potential limitations in certain industrial environments.

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