ArticleFolia microbiologica2008
Chitinolytic activities of Clostridium sp. JM2 isolated from stool of human administered per orally by chitosan.
Article in Folia microbiologica, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Chitinase Chit62J4 Essential for Chitin Processing by Human Microbiome BacteriumMolecules (Basel, Switzerland) · 2021Article
- Excretome of the chitinolytic bacterium Clostridium paraputrificum J4.Folia microbiologica · 2012Article
- Extracellular complex of chitinolytic enzymes of Clostridium paraputrificum strain J4 separated by membrane ultrafiltration.Folia microbiologica · 2010Article
- The antimicrobial action of low-molar-mass chitosan, chitosan derivatives and chitooligosaccharides on bifidobacteria.Folia microbiologica · 2010Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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/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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