Fungal beta-N-acetylhexosaminidases with high beta-N-acetylgalactosaminidase activity and their use for synthesis of beta-GalNAc-containing oligosaccharides
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12681926
DOI
10.1016/s0008-6215(03)00044-2
PII: S0008621503000442
Knihovny.cz E-resources
- MeSH
- beta-N-Acetyl-Galactosaminidase MeSH
- beta-N-Acetylhexosaminidases metabolism MeSH
- Hexosaminidases metabolism MeSH
- Hydrogen-Ion Concentration MeSH
- Molecular Structure MeSH
- Oligosaccharides chemical synthesis chemistry MeSH
- Penicillium enzymology MeSH
- Substrate Specificity MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- beta-N-Acetyl-Galactosaminidase MeSH
- beta-N-Acetylhexosaminidases MeSH
- Hexosaminidases MeSH
- Oligosaccharides MeSH
About 60 fungal strains were tested for production of extracellular beta-N-acetylhexosaminidases. A unique beta-N-acetylhexosaminidase with the beta-GalNAc-ase/beta-GlcNAc-ase ratio of 2.3-2.8 was found in the culture filtrates of some strains of Penicillium oxalicum. Addition of 20% (w/v) MgSO(4) increased the beta-GalNAc-ase/beta-GlcNAc-ase ratio to the value of 3.35. Cultivation conditions influence this ratio as well. beta-N-Acetylhexosaminidases from P. oxalicum CCF 2430 and Aspergillus oryzae CCF 1066 considerably differing in the GalNAc-ase activity were used for the synthesis of the following structures beta-D-GalpNAc-(1-->4)-D-GlcpNAc, beta-D-GalpNAc-(1-->6)-D-GlcpNAc, beta-D-GalpNAc-(1-->6)-D-GalpNAc, beta-D-GalpNAc-(1-->4)-alpha-D-GlcpNAcOAll and beta-D-GalpNAc-(1-->6)-beta-D-Galp-(1-->4)-alpha-D-GlcpNAcOAll to demonstrate the application of these new enzymes.
References provided by Crossref.org
Crystallization and diffraction analysis of β-N-acetylhexosaminidase from Aspergillus oryzae
