Abstract—This 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 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 13 993 Da, the absorption coefficient at 280 nm is 3.94 \(\varepsilon \frac{{{\text{mg}}}}{{{\text{mL}}}}\), and the isoelectric point is 10.35. The specific activity of the enzyme in relation to S. aureus FDA 209P cell suspension is 1518 U/mg with pH optimum of 7.7 and a temperature of 40°C.

摘要—本文提供了从猪葡萄球菌B-8870培养液中鉴定出一种新型葡萄球菌分解酶的数据。该酶的一级序列与松鼠葡萄球菌DD 4747的 N-乙酰胞壁酰基-L-丙氨酸酰胺酶的 CHAP 结构域具有最大的相似性。该酶对葡萄球菌属的多种微生物（包括 MRSA 菌株）具有活性。该酶的分子量为13 993 Da，280 nm处的吸收系数为3.94 \(\varepsilon \frac{{{\text{mg}}}}{{{\text{mL}}}}\)，等电点为10.35。与金黄色葡萄球菌相关的酶的比活性FDA 209P 细胞悬浮液为 1518 U/mg，最佳 pH 值为 7.7，温度为 40°C。