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Related Experiment Video

Updated: Jan 29, 2026

Synthesis of Hydrogels with Antifouling Properties As Membranes for Water Purification
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[PURIFICATION AND PHYSICO-CHEMICAL PROPERTIES OF PENICILLIUM TARDUM a-L- RHAMNOSIDASE].

O V Gudsenko, L D Varbanets

    Mikrobiolohichnyi Zhurnal (Kiev, Ukraine : 1993)
    |February 14, 2019
    PubMed
    Summary
    This summary is machine-generated.

    Researchers isolated and purified a novel enzyme, alpha-L-rhamnosidase, from Penicillium tardum. This enzyme exhibits high stability and activity, making it a promising candidate for various biotechnological applications.

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    Area of Science:

    • Enzymology
    • Microbial Biotechnology
    • Biochemistry

    Background:

    • Enzymes with alpha-L-rhamnosidase activity are crucial for various industrial processes.
    • Identifying and characterizing novel enzymes from microbial sources is essential for expanding biocatalytic tools.
    • Penicillium tardum is a fungal species with potential for producing valuable enzymes.

    Purpose of the Study:

    • To isolate and purify the enzyme alpha-L-rhamnosidase from Penicillium tardum.
    • To characterize the biochemical and optimal activity parameters of the purified enzyme.
    • To assess the stability and potential applications of the enzyme.

    Main Methods:

    • Enzyme isolation and purification using ammonium sulfate fractionation and TSK-gel chromatography (Toyopearl HW-60, Fractogel TSK DEAE-650-s).
    • Determination of enzyme specific activity, molecular mass, and optimal temperature and pH.
    • Assessment of enzyme stability under various pH and temperature conditions.

    Main Results:

    • An enzyme with alpha-L-rhamnosidase activity was successfully isolated and purified 23-fold from Penicillium tardum.
    • The purified enzyme exhibited a specific activity of 27.7 U/mg protein, with a molecular mass of 67 kDa.
    • Optimal activity was observed at 60 °C and pH 5.0, with significant pH and thermostability attributed to a 12% carbohydrate component.

    Conclusions:

    • A highly stable and active alpha-L-rhamnosidase was purified from Penicillium tardum.
    • The enzyme's robust properties suggest its potential utility in industrial applications requiring enzymatic hydrolysis of rhamnose-containing substrates.
    • Further research into the enzyme's structure and mechanism could unlock broader biotechnological applications.