Nomenclature Abstract for Comamonas testosteroni (Marcus and Talalay 1956) Tamaoka et al. 1987 emend. Willems et al. 1991.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Sarah Wigley ◽  
George M Garrity
Keyword(s):  
Comamonas Testosteroni

Use of a dynamic gassing-out method for activity and oxygen diffusion coefficient estimation in biofilms

1998 ◽  
Vol 37 (4-5) ◽  
pp. 171-175
Author(s):  
Artem Khlebnikov ◽  
Falilou Samb ◽  
Paul Péringer
Keyword(s):  
Diffusion Coefficient ◽  
Oxygen Uptake ◽  
Oxygen Diffusion ◽  
Fixed Bed ◽  
Biofilm Reactor ◽  
Strictly Aerobic ◽  
Comamonas Testosteroni ◽  
Respiration Activity ◽  
Oxygen Diffusion Coefficient ◽  
Biofilm Development

p-toluenesulphonic acid degradation by Comamonas testosteroni T-2 in multi-species biofilms was studied in a fixed bed biofilm reactor. The polypropylene static mixer elements (Sulzer Chemtech Ltd., Switzerland) were used as a support matrix for biofilm formation. Biofilm respiration was estimated using the dynamic gassing-out oxygen uptake method. A strong relation between oxygen uptake and reactor degradation efficiency was observed, because p-toluenesulphonate degradation is a strictly aerobic process. This technique also allowed us to estimate the thickness of the active layer in the studied system. The mean active thickness was in order of 200 μm, which is close to maximum oxygen penetration depth in biofilms. A transient mathematical model was established to evaluate oxygen diffusitivity in non-steady-state biofilms. Based on the DO concentration profiles, the oxygen diffusion coefficient and the maximum respiration activity were calculated. The oxygen diffusion coefficient obtained (2 10−10-1.2 10−9 m2 s−1) is in good agreement with published values. The DO diffusion coefficient varied with biofilm development. This may be, most likely, due to the biofilm density changes during the experiments. The knowledge of diffusivity changes in biofilms is particularly important for removal capacity estimation and appropriate reactor design.

scholarly journals Bacterial Culture Filtrates Antinematode Activity of Abomasum Bacterial Culture Filtrates against Haemonchus contortus in Small Ruminants

Animals ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 1843
Author(s):  
Asfa Nazish ◽  
Fozia ◽  
Baharullah Khattak ◽  
Taj Ali Khan ◽  
Ijaz Ahmad ◽  
...  
Keyword(s):  
Haemonchus Contortus ◽  
Bacterial Culture ◽  
Small Ruminants ◽  
Adult Mortality ◽  
Comamonas Testosteroni ◽  
Bacterial Isolates ◽  
Egg Hatch ◽  
Nematode Parasites ◽  
Culture Filtrates ◽  
Nematode Mortality

Haemonchosis is a parasitic disease of small ruminants that adversely affects livestock production. Haemonchus contortus is one of the most prevalent nematode parasites that infect the abomasum of small ruminants. This parasite reduces milk production, overall growth and sometimes causes the death of the infected animals. The evaluation of the biocontrol potential of some abomasum bacterial isolates against H. contortus is investigated in this study. Out of which, three isolates—Comamonas testosteroni, Comamonas jiangduensis, Pseudomonas weihenstephanesis—show significant effect against the nematode L3, adult, and egg hatch inhibition assays. Various concentrations of metabolites from these bacteria are prepared and applied in different treatments compared with control. In the case of adult mortality assay, 50% metabolites of C. testosteroni and P. weihenstephanesis show 46% adult mortality, whereas C. jiangduensis shows 40% mortality. It is observed that decreasing the concentration of bacterial metabolite, lowers nematode mortality. The minimum nematode mortality rate is recorded at the lowest filtrates concentration of all the bacterial isolates. The same trend is observed in egg hatch inhibition assay, where the higher concentration of bacterial culture filtrates shows 100% inhibition of H. contortus egg. It is concluded that the effect of bacterial culture filtrates against H. contortus is dose-dependent for their activity against nematode L3, adult, and inhibition of egg hatchment.

Molybdoprotein aldehyde dehydrogenases from comamonas testosteroni and amycolatopsis methanolica

1995 ◽  
Vol 59 (2-3) ◽  
pp. 741
Author(s):  
D.M.A.M. Luykx ◽  
S.W. Kim ◽  
S. de Vries ◽  
J.A. Duine
Keyword(s):  
Comamonas Testosteroni ◽  
Aldehyde Dehydrogenases

Interaction with Endogenous Microorganisms, Comamonas testosteroni Enhanced the Degradation of Polycyclic Aromatic Hydrocarbon in Soil

2021 ◽  
Author(s):  
Xueting Sun ◽  
Xin Li ◽  
Yue Cui ◽  
Ziwei Jiang ◽  
Qiao Wang ◽  
...  
Keyword(s):  
Contaminated Soil ◽  
Structural Equation ◽  
Functional Role ◽  
Degradation Rate ◽  
Structural Equation Models ◽  
Low Molecular Weight ◽  
Comamonas Testosteroni ◽  
Functional Bacteria ◽  
Polycyclic Aromatic

Abstract This study was to explore the functional role of Comamonas testosteroni (Ct) on soil indigenous microorganisms, and analyze the effect of Ct on PAHs degradation in PAH-contaminated soil. Results showed that inoculation of Ct could degrade naphthalene (Nap), phenanthrene (Phe), and benzo [α] pyrene (BaP) significantly. The degradation rate of Nap, Phe and BaP was 81.18%, 63.38% and 37.98% on day 25, respectively, suggesting that the low molecular weight of Nap and Phe were easier to be degraded by microorganisms than BaP. Network analysis showed that inoculation of Ct significantly increased the bacteria closely related to PAHs. Structural equation models confirmed Steroidobacter as functional bacteria could affect the degradation of Nap and BaP. Inoculated Ct could effectively enhance the synergy among indigenous bacteria to degrade PAHs. This would be helpful to understand the function of inoculated strains in PAH-contaminated soil and identify functional microorganisms of PAHs remediation.

Structural insights into dihydroxylation of terephthalate, a product of polyethylene terephthalate degradation

2022 ◽  
Author(s):  
Jai Krishna Mahto ◽  
Neetu Neetu ◽  
Monica Sharma ◽  
Monika Dubey ◽  
Bhanu Prakash Vellanki ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Polyethylene Terephthalate ◽  
Active Site ◽  
Catalytic Domain ◽  
Structural Features ◽  
Comamonas Testosteroni ◽  
Plastic Pollution ◽  
Microbial Utilization ◽  
Steady State Kinetics

Biodegradation of terephthalate (TPA) is a highly desired catabolic process for the bacterial utilization of this Polyethylene terephthalate (PET) depolymerization product, but to date, the structure of terephthalate dioxygenase (TPDO), a Rieske oxygenase (RO) that catalyzes the dihydroxylation of TPA to a cis -diol is unavailable. In this study, we characterized the steady-state kinetics and first crystal structure of TPDO from Comamonas testosteroni KF1 (TPDO KF1 ). The TPDO KF1 exhibited the substrate specificity for TPA ( k cat / K m = 57 ± 9 mM −1 s −1 ). The TPDO KF1 structure harbors characteristics RO features as well as a unique catalytic domain that rationalizes the enzyme’s function. The docking and mutagenesis studies reveal that its substrate specificity to TPA is mediated by Arg309 and Arg390 residues, two residues positioned on opposite faces of the active site. Additionally, residue Gln300 is also proven to be crucial for the activity, its substitution to alanine decreases the activity ( k cat ) by 80%. Together, this study delineates the structural features that dictate the substrate recognition and specificity of TPDO. Importance The global plastic pollution has become the most pressing environmental issue. Recent studies on enzymes depolymerizing polyethylene terephthalate plastic into terephthalate (TPA) show some potential in tackling this. Microbial utilization of this released product, TPA is an emerging and promising strategy for waste-to-value creation. Research from the last decade has discovered terephthalate dioxygenase (TPDO), as being responsible for initiating the enzymatic degradation of TPA in a few Gram-negative and Gram-positive bacteria. Here, we have determined the crystal structure of TPDO from Comamonas testosteroni KF1 and revealed that it possesses a unique catalytic domain featuring two basic residues in the active site to recognize TPA. Biochemical and mutagenesis studies demonstrated the crucial residues responsible for the substrate specificity of this enzyme.

scholarly journals Respirometry kinetics of phenol oxidation by Comamonas testosteroni Pb50 under various conditions of nutritional stress

2010 ◽  
Vol 53 (6) ◽  
pp. 1519-1528 ◽  
Author(s):  
Jan Paca ◽  
Alena Kosteckova ◽  
Leona Pacova ◽  
Ales Prell ◽  
Martin Halecky ◽  
...  
Keyword(s):  
Nutritional Stress ◽  
Phenol Oxidation ◽  
Comamonas Testosteroni ◽  
Kinetics Of
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