Isolation, Purification and some Properties of Staphylolytic Enzyme from <i>Staphylococcus hyicus</i>

Abstract

The paper presents data on the identification of a new staphylolytic enzyme from the cultural liquid of Staphylococcus hyicus B-8870. The primary sequence of the enzyme has the maximum similarity to the CHAP domain of N-acetylmuramoyl-L-alanine amidase from Staphylococcus sciuri DD 4747. The enzyme is active against a wide range of microorganisms of the Staphylococcus genus, including MRSA strains. The molecular weight of the enzyme is 13993 Da, the absorption coefficient at 280 nm is \(\varepsilon \frac{{{\text{mg}}}}{{{\text{ml}}}}\) 3.94, the value of the isoelectric point pI 10.35. The specific activity of the enzyme in relation to the cell suspension of S.aureus FDA 209P is 1518 U/mg with an optimum pH of 7.7 and a temperature of 40°C.