Nomenclature Abstract for Clostridium paraputrificum (Bienstock 1906) Snyder 1936 (Approved Lists 1980).

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Sarah Wigley ◽  
George M Garrity ◽  
Dorothea Taylor
Keyword(s):  
Clostridium Paraputrificum

scholarly journals Preterm Infant-Associated Clostridium tertium, Clostridium cadaveris, and Clostridium paraputrificum Strains: Genomic and Evolutionary Insights

2017 ◽  
Vol 9 (10) ◽  
pp. 2707-2714 ◽  
Author(s):  
Raymond Kiu ◽  
Shabhonam Caim ◽  
Cristina Alcon-Giner ◽  
Gusztav Belteki ◽  
Paul Clarke ◽  
...  
Keyword(s):  
Preterm Infant ◽  
Clostridium Paraputrificum

scholarly journals Chitinase Chit62J4 Essential for Chitin Processing by Human Microbiome Bacterium Clostridium paraputrificum J4

Molecules ◽  
2021 ◽  
Vol 26 (19) ◽  
pp. 5978
Author(s):  
Jan Dohnálek ◽  
Jarmila Dušková ◽  
Galina Tishchenko ◽  
Petr Kolenko ◽  
Tereza Skálová ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Glycosyl Hydrolase ◽  
Bacterial Genome ◽  
Human Microbiome ◽  
Culture Fluid ◽  
Carbohydrate Binding ◽  
Ph Optimum ◽  
Catalytic Sites ◽  
Tim Barrel ◽  
Clostridium Paraputrificum

Commensal bacterium Clostridium paraputrificum J4 produces several extracellular chitinolytic enzymes including a 62 kDa chitinase Chit62J4 active toward 4-nitrophenyl N,N′-diacetyl-β-d-chitobioside (pNGG). We characterized the crude enzyme from bacterial culture fluid, recombinant enzyme rChit62J4, and its catalytic domain rChit62J4cat. This major chitinase, securing nutrition of the bacterium in the human intestinal tract when supplied with chitin, has a pH optimum of 5.5 and processes pNGG with Km = 0.24 mM and kcat = 30.0 s−1. Sequence comparison of the amino acid sequence of Chit62J4, determined during bacterial genome sequencing, characterizes the enzyme as a family 18 glycosyl hydrolase with a four-domain structure. The catalytic domain has the typical TIM barrel structure and the accessory domains—2x Fn3/Big3 and a carbohydrate binding module—that likely supports enzyme activity on chitin fibers. The catalytic domain is highly homologous to a single-domain chitinase of Bacillus cereus NCTU2. However, the catalytic profiles significantly differ between the two enzymes despite almost identical catalytic sites. The shift of pI and pH optimum of the commensal enzyme toward acidic values compared to the soil bacterium is the likely environmental adaptation that provides C. paraputrificum J4 a competitive advantage over other commensal bacteria.

Electrotransformation of Clostridium paraputrificum M-21 with some plasmids

2003 ◽  
Vol 96 (3) ◽  
pp. 304-306 ◽  
Author(s):  
Kazuo Sakka ◽  
Mamiko Kawase ◽  
Daisuke Baba ◽  
Kenji Morimoto ◽  
Shuichi Karita ◽  
...  
Keyword(s):  
Clostridium Paraputrificum

scholarly journals Clostridium paraputrificumBacteremia Associated with Colonic Necrosis in a Patient with AIDS

2015 ◽  
Vol 2015 ◽  
pp. 1-3 ◽  
Author(s):  
Takashi Shinha ◽  
Christiane Hadi
Keyword(s):  
Septic Shock ◽  
Clinical Significance ◽  
Clinical Disease ◽  
Morbidity And Mortality ◽  
Gram Positive ◽  
Disease Spectrum ◽  
Colonic Malignancy ◽  
Invasive Infections ◽  
Colonic Necrosis ◽  
Clostridium Paraputrificum

Clostridiumspecies are anaerobic Gram-positive rods that can cause a broad range of invasive infections in humans, including myonecrosis and bacteremia. Importantly, clostridial bacteremia is frequently associated with underlying medical conditions, such as colonic malignancy. CharacterizingClostridiumspp. and understanding their associated clinical disease spectrum are paramount to provide optimal treatment, thereby decreasing morbidity and mortality especially in those with underlying debilitating comorbidities.Clostridium paraputrificumis an infrequently isolatedClostridiumspecies and its clinical significance has not been well described. We herein report a case of bacteremia due toC. paraputrificumin a 65-year-old man with AIDS who developed acute colonic necrosis complicated by septic shock. We then review other cases of bacteremia associated withC. paraputrificumin the literature in addition to discussing the clinical significance of anaerobic bacteremia in general. To our knowledge, our report is the second case ofC. paraputrificumbacteremia in a patient with AIDS.

Conversion of Chitinous Wastes to Hydrogen Gas by Clostridium paraputrificum M-21.

2001 ◽  
Vol 91 (4) ◽  
pp. 339-343 ◽  
Author(s):  
DWIERRA EVVYERNIE ◽  
KENJI MORIMOTO ◽  
SHUICHI KARITA ◽  
TETSUYA KIMURA ◽  
KAZUO SAKKA ◽  
...  
Keyword(s):  
Hydrogen Gas ◽  
Clostridium Paraputrificum

The Coupling of Anaerobic Steroid Dehydrogenation to Nitrate Reduction in Pseudomonas N.C.I.B. 10590 and Clostridium paraputrificum

1975 ◽  
Vol 3 (2) ◽  
pp. 299-301 ◽  
Author(s):  
PETER J. BARNES ◽  
RODNEY F. BILTON ◽  
ARTHUR N. MASON ◽  
FRESIA FERNANDEZ ◽  
MICHAEL J. HILL
Keyword(s):  
Nitrate Reduction ◽  
Clostridium Paraputrificum

scholarly journals Clostridium paraputrificum as rare causative of lifethreatening spontaneous necrotizing cellulitis of the abdominal wall

2016 ◽  
Vol 4 (1) ◽  
pp. 3 ◽  
Author(s):  
Joerg Lindenmann ◽  
Nicole Fink-Neuboeck ◽  
Eva Leitner ◽  
Andrea Grisold ◽  
Peter Kohek ◽  
...  
Keyword(s):  
Abdominal Wall ◽  
Clostridium Paraputrificum

scholarly journals Chitinolytic enzymes from bacterium inhabiting human gastrointestinal tract -- critical parameters of protein isolation from anaerobic culture.

2011 ◽  
Vol 58 (2) ◽  
Author(s):  
Jarmila Dušková ◽  
Galina Tishchenko ◽  
Evgenia Ponomareva ◽  
Jiří Šimůnek ◽  
Ingrid Koppová ◽  
...  
Keyword(s):  
Gastrointestinal Tract ◽  
Size Exclusion ◽  
Critical Parameters ◽  
Protein Isolation ◽  
Chromatographic Separations ◽  
Healthy Human ◽  
Chitinolytic Enzymes ◽  
Sds Page ◽  
Clostridium Paraputrificum

The object of this study are chitinolytic enzymes produced by bacterium Clostridium paraputrificum J4 isolated from the gastrointestinal tract of a healthy human. In particular, we focus on the development of purification protocols, determination of properties of the enzymes and their activity profiles. The process of bacteria cultivation and isolation of chitinolytic complex of enzymes showing specific activities of endo-, exo-chitinase and N-acetyl-β-glucosaminidase was optimized. A range of various purification procedures were used such as ultrafiltration, precipitation, chromatographic separations (ion-exchange, size exclusion, chromatofocusing) in altered combinations. The optimal purification protocol comprises two or three steps. Individual samples were analyzed by SDS/PAGE electrophoresis and after renaturation their activity could be detected using zymograms. Mass spectroscopy peptide fragment analysis and MALDI analysis of the purest samples indicate presence of endochitinase B (molecular mass about 85 kDa) and of 60-kDa endo- and exochitinases.

Sign in / Sign up

Export Citation Format

Share Document