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The non‐enzymatic microbicidal activity of lysozymes
Author(s) -
Düring Klaus,
Porsch Petra,
Mahn Andreas,
Brinkmann Olaf,
Gieffers Werner
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00405-6
Subject(s) - chemistry , enzyme , biochemistry , microbiology and biotechnology , biology
T4 lysozyme was thought to destroy bacteria by its muramidase activity. However, we demonstrate here that amphipathic helix stretches in the C‐terminus of T4 lysozyme mediate its bactericidal and fungistatic activities. In heat‐denatured T4 lysozyme, the enzymatic activity is completely abolished but unexpectedly, the antimicrobial functions remain preserved. Small synthetic peptides corresponding to amphipathic C‐terminal domains of T4 lysozyme show a microbicidal activity. Its membrane disturbing activity was directly demonstrated for bacterial, fungal and plant cells but not in a hemolysis assay. Comparable results were obtained with hen egg white lysozyme. This opens up many new opportunities for optimization of lysozymes as antimicrobial agents in various applications by protein engineering.