[Isolation and characterization of endo-N-acetylmuramidase produced by Actinomyces levoris]

Precipitation by ammonium sulfate and a subsequent purification of the culture fluid of Actinomyces levoris by gel-filtration through Sephadex G-25, ion-exchange chromatography on DEAE-cellulose and CM-cellulose resulted in an enzyme which activley lyzes the cell walls of a hemolytic streptococcus of group A. The molecular weight (12,500), isoelectric point (pI 10,6) and amino acid composition of the enzyme were determined. The enzyme specificity was assayed using peptidoglycane isolated rom the cell walls of streptococcus of group A used as a substrate. An analysis of the hydrolysis products of peptidoglycane showed that the enzyme under study is an endo-beta-N-acetylmuramidase (EC 3.2.1.17).