Kaminishi H, Hagihara Y, Hayashi S, Cho T
Infect Immun. 1986 Aug;53(2):312-6. doi: 10.1128/iai.53.2.312-316.1986.
In media containing collagen as the nitrogen source, the pathogenic yeast Candida albicans secreted a collagenolytic enzyme. Purification of the enzyme from a culture filtrate was achieved by DEAE-Sephacel chromatography at pH 6.7. The molecular weight was found to be 46,000 by 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the isoelectric point was at pH 4.2. The pH optimum lay between 3.5 and 4.0, and above pH 6.0, the enzyme underwent alkaline denaturation. The enzyme was heat labile, and a decrease in activity was found above 55 degrees C. The enzyme activity was inhibited by the addition of urea, cysteine, and pepstatin. No other inhibitor among those tested had any effect. The C. albicans enzyme degraded both the native acid-soluble collagen and the insoluble dentinal collagen.
在以胶原蛋白作为氮源的培养基中，致病性酵母白色念珠菌分泌出一种胶原酶。通过在pH 6.7条件下进行DEAE-葡聚糖凝胶层析，从培养滤液中纯化得到了该酶。经10%十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定，其分子量为46,000，等电点为pH 4.2。该酶的最适pH值在3.5至4.0之间，pH值高于6.0时，酶会发生碱性变性。该酶对热不稳定，温度高于55℃时活性会降低。添加尿素、半胱氨酸和胃蛋白酶抑制剂会抑制酶的活性。在所测试的其他抑制剂中，没有任何一种有作用。白色念珠菌酶可降解天然酸溶性胶原蛋白和不溶性牙本质胶原蛋白。
