Chitinolytic activities of Clostridium sp. JM2 isolated from stool of human administered per orally by chitosan
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Acetylglucosaminidase metabolism MeSH
- Chitin metabolism MeSH
- Chitinases metabolism MeSH
- Chitosan administration & dosage MeSH
- Clostridium classification enzymology growth & development isolation & purification MeSH
- Feces microbiology MeSH
- Glycoside Hydrolases metabolism MeSH
- Hydrogen-Ion Concentration MeSH
- Humans MeSH
- Enzyme Stability MeSH
- Temperature MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Acetylglucosaminidase MeSH
- Chitin MeSH
- Chitinases MeSH
- Chitosan MeSH
- chitosanase MeSH Browser
- Glycoside Hydrolases MeSH
The novel chitinolytic bacterium Clostridium beijerinckii strain JM2 was isolated from the stool of healthy volunteers supplied daily per orally with 3 g of chitosan. The bacterium grown on colloidal chitin produced a complete array of chitinolytic enzymes. Significant activities of endochitinase, exochitinase and chitosanase were excreted into the medium (301, 282 and 268 nkat/microg protein, respectively). The high cellular activity of N-acetyl-beta-glucosaminidase (NAGase) and chitosanase were detected (732.4 and 154 nkat/microg protein, respectively). NAGase activity represented the main activity associated with the cellular fraction. The activities of both enzymes tested increased from 20 to 50 degrees C; the optimum reaction temperature estimated being 50 degrees C. Endochitinase as well as NAGase showed an activity in the pH interval of 4.0-8.0; the optimum pH values were 6.5 and 6.0, respectively. The extracellular endochitinase complex consisted of six isoenzymes with molar mass of 32-76 kDa; in the cellular fraction five bands with molar mass of 45-86 kDa were detected. Exochitinase activity was demonstrated in the form of three bands (with molar mass of 30-57 kDa), NAGase activity displayed one band of 45 kDa.
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