Department of Bioresource Science, Faculty of Agriculture, Kagawa University, Miki-cho, Kagawa 761-07, and Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Kyoto 606, Japan.
Appl Environ Microbiol. 1989 Dec;55(12):3107-12. doi: 10.1128/aem.55.12.3107-3112.1989.
Arthrobacter protophormiae produced a high level of extracellular endo-beta-N-acetylglucosaminidase when cells were grown in a medium containing ovalbumin. The enzyme was induced by the glycopeptide fraction of ovalbumin prepared by pronase digestion. Production of the enzyme was also induced by glycoproteins such as yeast invertase and bovine ribonuclease B but not by monosaccharides such as mannose, N-acetylglucosamine, and galactose. The enzyme was purified to homogeneity as demonstrated by polyacrylamide gel electrophoresis and has an apparent molecular weight of about 80,000. The enzyme showed a broad optimum pH in the range of pH 5.0 to 11.0. The enzyme hydrolyzed all heterogeneous ovalbumin glycopeptides, although the hydrolysis rates for hybrid type glycopeptides were very low. The substrate specificity of A. protophormiae endo-beta-N-acetylglucosaminidase was very similar to that of Endo-C(II) from Clostridium perfringens. Therefore, the enzyme induction by A. protophormiae seems to have a close relation to the substrate specificity of the enzyme.
当细胞在含有卵清蛋白的培养基中生长时，节杆菌属原变种会产生高水平的细胞外内切-β-N-乙酰氨基葡萄糖苷酶。该酶由用蛋白酶消化制备的卵清蛋白糖肽部分诱导。该酶也可被糖蛋白如酵母转化酶和牛核糖核酸酶 B 诱导，但不能被单糖如甘露糖、N-乙酰氨基葡萄糖和半乳糖诱导。该酶通过聚丙烯酰胺凝胶电泳显示为均一纯，具有约 80000 的表观分子量。该酶在 pH5.0 到 11.0 的范围内显示出广泛的最适 pH。该酶水解所有异质的卵清蛋白糖肽，尽管杂交型糖肽的水解速度非常低。A. protophormiae 内切-β-N-乙酰氨基葡萄糖苷酶的底物特异性与来自产气荚膜梭菌的 Endo-C(II)非常相似。因此，A. protophormiae 的酶诱导似乎与酶的底物特异性密切相关。
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