PURIFICATION AND CHARACTERIZATION OF AN ENDO-N-ACETYL-BETA-D-GLUCOSAMINIDASE FROM THE CULTURE-MEDIUM OF STIGMATELLA-AURANTIACA DW4

被引：14

作者：

BOURGERIE, S

KARAMANOS, Y

GRARD, T

JULIEN, R

机构：

[1] UNIV LIMOGES, INST BIOTECHNOL, F-87060 LIMOGES, FRANCE

[2] UNIV SCI & TECH LILLE FLANDRES ARTOIS, CHIM BIOL LAB, F-59655 VILLENEUVE DASCQ, FRANCE

来源：

JOURNAL OF BACTERIOLOGY | 1994年 / 176卷 / 20期

关键词：

D O I：

10.1128/jb.176.20.6170-6174.1994

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

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收藏

页码：6170 / 6174

页数：5

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