Berete Y J, Schaeg W, Brückler J, Blobel H
Zentralbl Bakteriol A. 1980 Nov;248(2):229-33.
Lipase and phospholipase C from Staphylococcus aureus of different origin were demonstrated qualitatively by agar diffusion on tributyrin- and lecithin agar. On test media with either 0,3% Na-azide or 0,3% KCN lipase-activity was not inhibited, phospholipase C, on the other hand, completely blocked (Table 1, Fig. 2). In this manner a tentative differentiation was possible between lipase and phospholipase C. For the quantitative determination of lipase the hydrolysis of p-nitrophenyl palmitate proved to be most useful (Fig. 1). S. aureus-cultures of human origin produced more often and more actively lipase and phospholipase C than those from cattle (Table 2).
通过在三丁酸甘油酯琼脂和卵磷脂琼脂上进行琼脂扩散法,定性检测了不同来源金黄色葡萄球菌的脂肪酶和磷脂酶C。在含有0.3%叠氮化钠或0.3%氰化钾的测试培养基上,脂肪酶活性未受抑制,而磷脂酶C则被完全阻断(表1,图2)。通过这种方式,可以初步区分脂肪酶和磷脂酶C。对于脂肪酶的定量测定,对硝基苯基棕榈酸酯的水解被证明是最有用的(图1)。与来自牛的金黄色葡萄球菌培养物相比,人类来源的金黄色葡萄球菌培养物更频繁、更活跃地产生脂肪酶和磷脂酶C(表2)。