Antibacterial potential of a new glucosaminidase from

Introduction: Methods: Through differential extraction of protein fractions associated with the membrane of this bacterial strain and in silico analysis, we report the compositional, physicochemical, and biochemical characterization of an enzyme with N-acetylglucosaminidase (NAGase) activity. Additionally, we determined the bactericidal activity of this enzymatic extract against two Gram-positive and two Gram-negative pathogens. We also evaluated ultrastructural changes in sensitive bacteria using scanning electron microscopy (SEM). Results: This NAGase activity shows a high specificity against Micrococcus lysodeikticus ATCC 4698 cell walls. The active protein has a molecular mass close to 110 kDa, a sequence of 935 residues, a possible transmembrane fragment close to the N-terminal end, and a profile of high intrinsic flexibility with high hydrophilicity, consistent with a possible topology for a peripheral membrane protein. The enzyme induces significant autolytic activity in Discussion: This NAGase has great potential as an enzybiotic, as an alternative to the use of conventional antibiotics. Showing little hemolytic activity, this protein has pharmacological potential against multidrug-resistant bacteria. We propose a mechanism of action in which this enzyme hydrolyzes GlcNAc units present in the cell wall of diverse pathogens.