PURIFICATION AND CHARACTERIZATION OF AN ENDO-N-ACETYL-BETA-D-GLUCOSAMINIDASE FROM THE CULTURE-MEDIUM OF STIGMATELLA-AURANTIACA DW4
PURIFICATION AND CHARACTERIZATION OF AN ENDO-N-ACETYL-BETA-D-GLUCOSAMINIDASE FROM THE CULTURE-MEDIUM OF STIGMATELLA-AURANTIACA DW4
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DOI：
10.1128/jb.176.20.6170-6174.1994
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发表时间：
1994-10-01
影响因子：
3.2
通讯作者：
JULIEN, R
中科院分区：
文献类型：
--
作者：
BOURGERIE, S;KARAMANOS, Y;JULIEN, R
研究了一种新的内源性n -乙酰- β - d -氨基葡萄糖苷酶（ENGase），该酶作用于n -链聚糖的双n -乙酰壳生物基部分。经过硫酸铵沉淀、凝胶过滤和色谱聚焦纯化至均匀性，经十二烷基硫酸钠-聚丙烯酰胺凝胶电泳，该ENGase的分子量接近27 kDa。最适pH为4.0，最适pI为6.8。该酶被命名为ENGase St，对寡糖甘露苷型糖天冬酰胺和糖蛋白具有高活性，也可以水解杂交型和复合型糖天冬酰胺，但不作为小鼠水解酶。
A novel endo-N-acetyl-beta-D-glucosaminidase (ENGase), acting on the di-N-acetylchitobiosyl part of N-linked glycans, was characterized in the culture medium of Stigmatella aurantiaca DW4. Purified to homogeneity by ammonium sulfate precipitation, gel filtration, and chromatofocusing, this ENGase presents, upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, a molecular mass near 27 kDa. Optimal pH and pI were 4.0 and 6.8, respectively. The enzyme, named ENGase St, exhibits high activity on oligomannoside-type glycoasparagines and glycoproteins and could also hydrolyze hybrid- and complex-type glycoasparagines but does not acts as a murein hydrolase.