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Artificial cell-microencapsulated phenylalanine ammonia-lyase.

L Bourget, T M Chang

    Applied Biochemistry and Biotechnology
    |January 1, 1984
    PubMed
    Summary
    This summary is machine-generated.

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    Immobilizing phenylalanine ammonia-lyase (PAL) in artificial cells reduced its activity but maintained its Michaelis constant. This enzyme immobilization technique offers insights into enzyme kinetics for biocatalysis applications.

    Area of Science:

    • Biochemistry
    • Enzyme Engineering
    • Biocatalysis

    Background:

    • Phenylalanine ammonia-lyase (PAL) is a crucial enzyme in plant biochemistry and has potential biotechnological applications.
    • Enzyme immobilization is a key strategy to enhance enzyme stability and reusability.
    • Previous technical challenges existed in encapsulating enzymes like PAL within artificial cell structures.

    Purpose of the Study:

    • To investigate the kinetic properties of phenylalanine ammonia-lyase (PAL) after immobilization in collodion artificial cells.
    • To compare the performance of microencapsulated PAL with PAL in free solution.

    Main Methods:

    • Immobilization of phenylalanine ammonia-lyase (PAL) within collodion artificial cells.
    • Enzyme kinetic assays were performed on both immobilized and free PAL.

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  • Determination of kinetic parameters, including Km and Vm.

    • Main Results:

    • Microencapsulated PAL exhibited approximately 20% of the activity of PAL in free solution.
    • The Michaelis constant (Km) for both free and immobilized PAL remained consistent at 475 µM.
    • The maximum velocity (Vm) for microencapsulated PAL was 9 µM/min, significantly lower than 55 µM/min for free PAL.

    Conclusions:

    • Enzyme immobilization in collodion artificial cells significantly reduces PAL's Vm while maintaining its Km.
    • This study provides valuable kinetic data for immobilized PAL, informing future biocatalyst design.
    • Further research may optimize immobilization techniques to improve the activity of encapsulated enzymes.