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Citrate determination with aconitase immobilized on solid support.

E Cortes, S Viniegra, M S Aguilar

    The International Journal of Biochemistry
    |January 1, 1985
    PubMed
    Summary
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    Immobilized pig heart aconitase on Enzacryl AA offers enhanced stability and reusability for citrate quantification. This enzyme immobilization method provides a sensitive, reproducible, and economical alternative to traditional citrate analysis techniques.

    Area of Science:

    • Biochemistry
    • Enzyme Immobilization
    • Analytical Chemistry

    Background:

    • Aconitase is a key enzyme in the citric acid cycle.
    • Traditional citrate analysis methods can be time-consuming and costly.
    • Enzyme immobilization offers potential for improved enzyme stability and reusability.

    Purpose of the Study:

    • To immobilize pig heart aconitase onto Enzacryl AA.
    • To investigate the kinetic behavior, stability, and effectiveness of immobilized aconitase.
    • To develop a sensitive and reproducible method for citrate quantification using immobilized aconitase.

    Main Methods:

    • Enzyme immobilization of pig heart aconitase on Enzacryl AA.
    • Kinetic studies using a stirred bath reactor with continuous recycling.

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  • Assessment of enzyme stability under various conditions (pH, temperature, storage, repeated use).
  • Development of a spectrophotometric assay for citrate quantification.

    • Main Results:

    • Optimized flow rate in the reactor to mitigate diffusional limitations.
    • Immobilized aconitase exhibited comparable kinetic constants to soluble form.
    • Immobilized aconitase demonstrated superior stability, retaining full activity after repeated use and long-term storage, unlike the soluble form.
    • A linear relationship between absorbance increase and citrate concentration (0.2–3.2 mM) was established.

    Conclusions:

    • Immobilized pig heart aconitase on Enzacryl AA is a stable and reusable biocatalyst.
    • The developed system allows for sensitive and reproducible citrate determination.
    • This immobilized enzyme approach offers a cost-effective and simplified alternative for quantitative citrate analysis.