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Lysozymes' esterase activity.

J Jollès, P Jollès

    FEBS Letters
    |October 3, 1983
    PubMed
    Summary
    This summary is machine-generated.

    Duck and goose lysozymes exhibit esterase activity, challenging previous assumptions about histidine's essential role. This finding expands our understanding of lysozyme enzyme function beyond its known antimicrobial properties.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Protein Science

    Background:

    • Hen lysozyme (c-type) exhibits non-specific esterase activity.
    • Histidine residues were previously implicated as crucial for this enzymatic function.

    Purpose of the Study:

    • To investigate the esterase activity of histidine-less duck lysozyme (c-type) and goose lysozyme (g-type).
    • To determine if histidine is essential for the non-specific esterase activity observed in lysozymes.

    Main Methods:

    • Enzyme activity assays were performed using p-nitrophenylacetate as a substrate.
    • Comparative analysis of esterase activity in different lysozyme types (hen, duck, goose).

    Main Results:

    • Histidine-less duck egg-white lysozyme (c-type) demonstrated significant esterase activity.

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  • Goose lysozyme (g-type) also exhibited comparable esterase activity.
  • These findings indicate that histidine is not essential for the non-specific esterase activity of these lysozymes.

    • Conclusions:

    • The non-specific esterase activity of c-type and g-type lysozymes is independent of histidine residues.
    • Lysozyme's functional repertoire extends beyond antimicrobial action to include esterase activity, mediated by mechanisms not reliant on histidine.