[Bacteriolytic enzymes produced by actinomycetes. I. The physicochemical properties of the enzymes and the spectrum of their lytic action].

This review is devoted to the bacteriolytic enzymes produced by many actinomycetes, mainly by Streptomyces genus. The bacteriolytic enzymes hydrolyse the specific bonds in bacterial peptidoglycans and cause the solubilization of the cellular walls and the disintegration of the bacterial cells. Many of the enzymes are purified to the electrophoretic homogeneity. The actinomycetes form the endo-N-acetylmuramidases more often, then the endopeptidases follow according to the frequency of occurrence, while the amidases and endo-N-acetylglucosaminidases are met rather seldom among the streptomycete-producers. The known amidases and exo-enzymes which are also produced by some species of actinomycetes are not related to the lytic enzymes proper. Almost all known endopeptidases from streptomyces hydrolyse the bridge peptide bonds in which the carboxyl group of terminal D-alanyl of peptide chain is involved. The bacteriolytic spectra of the different muramidases differ from each other and essentially differ from the spectrum of the egg-white lysozyme. Some endomuramidases from streptomyces are able to hydrolyse streptococci and some other important from the practical point of view microorganisms resistant to the action of lysozyme.