Chitinolytic activities of <Emphasis Type="Italic">Clostridium</Emphasis> sp. JM2 isolated from stool of human administered per orally by chitosan |
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Authors: | J Šimůnek G Tishchenko I Koppová |
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Institution: | (1) Institute of Animal Physiology and Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czechia;(2) Institute of Macromolecular Chemistry, Academy of Sciences of the Czech Republic, 162 06 Prague, Czechia |
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Abstract: | 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/μg protein, respectively). The high cellular activity
of N-acetyl-β-glucosaminidase (NAGase) and chitosanase were detected (732.4 and 154 nkat/μg protein, respectively). NAGase activity
represented the main activity associated with the cellular fraction. The activities of both enzymes tested increased from
20 to 50 °C; the optimum reaction temperature estimated being 50 °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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