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Related Experiment Videos

Aminoacylase pellets.

K I Hirano, I Karube, S Suzuki

    Biotechnology and Bioengineering
    |March 1, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Immobilizing aminoacylase on Aspergillus ochraceus mycelium enhanced its stability against heavy metals and inhibitors. However, cobalt ion activation decreased post-immobilization, suggesting covalent coupling via glutaraldehyde.

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    Area of Science:

    • Biotechnology
    • Enzyme Immobilization
    • Biocatalysis

    Background:

    • Aminoacylase is a crucial enzyme in various industrial processes.
    • Enzyme immobilization is a key strategy to improve enzyme stability and reusability.
    • Aspergillus ochraceus offers a potential platform for microbial enzyme production and immobilization.

    Purpose of the Study:

    • To immobilize aminoacylase onto Aspergillus ochraceus mycelium pellets.
    • To characterize the properties of the immobilized aminoacylase.
    • To compare the stability and activity of immobilized aminoacylase with its native form.

    Main Methods:

    • Enzyme immobilization using albumin and glutaraldehyde on Aspergillus ochraceus mycelium pellets.
    • Determination of optimal pH for both native and immobilized aminoacylase.

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  • Stability assays against varying pH, heavy metal ions, and inhibitors.
  • Enzyme activity measurements, including cobalt ion activation.

    • Main Results:

    • Immobilized aminoacylase exhibited optimal pH similar to the native enzyme.
    • Aminoacylase pellets demonstrated stability in the pH range of 4-8, with instability in alkaline conditions.
    • Immobilized aminoacylase showed increased stability against heavy metal ions and inhibitors compared to the native enzyme.
    • A decrease in cobalt ion activation was observed for the immobilized aminoacylase.

    Conclusions:

    • Immobilization of aminoacylase on Aspergillus ochraceus mycelium enhances its operational stability.
    • Glutaraldehyde likely mediates covalent coupling of aminoacylase to the mycelium.
    • Further optimization may be needed to fully retain cofactor-dependent activation properties.