Domain shuffling and module engineering of Listeria phage endolysins for enhanced lytic activity and binding affinity

Abstract excerpt

Bacteriophage endolysins are peptidoglycan hydrolases employed by the virus to lyse the host at the end of its multiplication phase. They have found many uses in biotechnology; not only as antimicrobials, but also for the development of novel diagnostic tools for rapid detection of pathogenic bacteria. These enzymes generally show a modular organization, consisting of N-terminal enzymatically active domains...

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