Characterization of chitinases of polycentric anaerobic rumen fungi
Language English Country United States Media print-electronic
Document type Journal Article
- MeSH
- Anaerobiosis MeSH
- Rumen metabolism microbiology MeSH
- Chitin metabolism MeSH
- Chitinases * chemistry metabolism MeSH
- Chytridiomycota classification enzymology growth & development MeSH
- Fungal Proteins genetics MeSH
- Hydrogen-Ion Concentration MeSH
- Neocallimastigales classification enzymology growth & development MeSH
- Enzyme Stability MeSH
- Temperature MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Chitin MeSH
- Chitinases * MeSH
- Fungal Proteins MeSH
Chitinolytic systems of anaerobic polycentric rumen fungi of genera Orpinomyces and Anaeromyces were investigated in three crude enzyme fractions - extracellular, cytosolic and cell-wall. Endochitinase was found as a dominant enzyme with highest activity in the cytosolic fraction. Endochitinases of both genera were stable at pH 4.5-7.0 with optimum at 6.5. The Orpinomyces endochitinase was stable up to 50 degrees C with an optimum for enzyme activity at 50 degrees C; similarly, Anaeromyces endochitinase was stable up to 40 degrees C with optimum at 40 degrees C. The most suitable substrate for both endochitinases was fungal cell-wall chitin. Enzyme activities were inhibited by Hg(2+) and Mn(2+), and activated by Mg(2+) and Fe(3+). Both endochitinases were inhibited by 10 mmol/L SDS and activated by iodoacetamide.
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