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Calf rennet lysozyme.

J J Pahud, F Widmer

    The Biochemical Journal
    |March 1, 1982
    PubMed
    Summary
    This summary is machine-generated.

    A novel glycosidase with endo-N-acetylmuramoylhydrolase specificity was isolated from calf rennet and abomasal secretions. This stable enzyme exhibits chitinase activity and competitive inhibition by specific sugars.

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    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Lysozymes are glycosidases crucial for bacterial cell wall degradation.
    • Calf rennet and abomasal secretions are potential sources of novel enzymes.

    Purpose of the Study:

    • To isolate and characterize a glycosidase from calf rennet with endo-N-acetylmuramoylhydrolase specificity.
    • To investigate the enzyme's properties, including stability, optimal conditions, and substrate inhibition.

    Main Methods:

    • Enzyme isolation from calf rennet and abomasal secretions.
    • Characterization using electrofocusing, molecular weight determination (Mr), pH optimum, and isoelectric point (pI) analysis.
    • Enzyme kinetics studied via competitive inhibition assays with N-acetylglucosamine and N-acetylmuramic acid.

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    Main Results:

    • Isolation of a glycosidase with endo-N-acetylmuramoylhydrolase specificity (EC 3.2.1.17).
    • The main enzyme form exhibited a molecular weight of approximately 15,000, pH optimum of 5.0, and pI of 7.5, with high conformational stability.
    • Competitive inhibition by N-acetylglucosamine (Ki = 29 mM) and N-acetylmuramic acid (Ki = 2.4 mM) was observed.
    • Significant chitinase activity was also detected.

    Conclusions:

    • A stable glycosidase with endo-N-acetylmuramoylhydrolase and chitinase activities was successfully isolated from calf sources.
    • The enzyme's characteristics suggest potential applications in biotechnology and microbial control.