Purification and Characterization of an Endo-N-Acetyl-4-D-Glucosaminidase from the Culture Medium of Stigmatella aurantiaca DW4

Sylvain Bourgerie (1) , Yannis Karamanos (1) , Thierry Grard (2) , Raymond Julien (1)

1 UNILIM - Université de Limoges
2 ULCO - Université du Littoral Côte d'Opale

A novel endo-N-acetyl- ,-D-glucosaminidase (ENGase), acting on the diN -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.

Mots clés: glucosaminidase

Domaines: Bactériologie; Biochimie [q-bio.BM]

Sylvain Bourgerie, Yannis Karamanos, Thierry Grard, Raymond Julien. Purification and Characterization of an Endo-N-Acetyl-4-D-Glucosaminidase from the Culture Medium of Stigmatella aurantiaca DW4. Journal of Bacteriology, 1994, 176 (20), pp.6170-6174. ⟨10.1128/jb.176.20.6170-6174.1994⟩. ⟨hal-03697251⟩