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A Novel Fungal Endo-β-N-acetylglucosaminidase that Specifically Acts on Plant Glycoproteins
- Source :
- Bioscience, Biotechnology, and Biochemistry. 62:1344-1350
- Publication Year :
- 1998
- Publisher :
- Informa UK Limited, 1998.
-
Abstract
- An endo-beta-N-acetylglucosaminidase specific for plant glycoprotein oligosaccharides was purified from the culture fluid of a fungus. The Mr of the purified enzyme was 89,000. This enzyme was stable at pH 5.5-7.0, up to 30 degrees C, and showed the highest activity at pH 6.0. Among sugar chains tested, xylose-containing sugar chains (M3X, M3FX, and M2FX) were the most favored substrates. Oligomannose type (M3, M5, and M9) and hybrid type (GNM3) sugar chains were hydrolyzed much more slowly than xylose-containing sugar chains, and a complex type sugar chain (GN2M3) was not hydrolyzed at all by the enzyme. Moreover, the enzyme released sugar chains from native horseradish peroxidase and stem bromelain, which were not hydrolyzed by other endo-beta-N-acetylglucosaminidases (Endo H, D, and F). The enzyme could transfer the xylose-containing sugar chain from bromelain to DNS-Asn-GlcNAc-Fuc.
- Subjects :
- Glycan
Stereochemistry
Molecular Sequence Data
Xylose
Applied Microbiology and Biotechnology
Biochemistry
Horseradish peroxidase
Substrate Specificity
Analytical Chemistry
chemistry.chemical_compound
Hydrolysis
Enzyme Stability
Sugar
Molecular Biology
Chromatography, High Pressure Liquid
Horseradish Peroxidase
Glycoproteins
Plant Proteins
chemistry.chemical_classification
biology
Organic Chemistry
Fungi
General Medicine
Hydrogen-Ion Concentration
Bromelains
Culture Media
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
Enzyme
Carbohydrate Sequence
chemistry
biology.protein
Stem bromelain
Electrophoresis, Polyacrylamide Gel
Glycoprotein
Biotechnology
Subjects
Details
- ISSN :
- 13476947 and 09168451
- Volume :
- 62
- Database :
- OpenAIRE
- Journal :
- Bioscience, Biotechnology, and Biochemistry
- Accession number :
- edsair.doi.dedup.....b0e35979f8cba11018c9c6ff07da1243