Synergistic Tannic Acid-Fluoride Inhibition of Ammonia Emissions and Simultaneous Reduction of Methane and Odor Emissions from Livestock Waste.
Dalby Frederik R,Svane Simon,Sigurdarson Jens Jakob,Sørensen Morten K,Hansen Michael J,Karring Henrik,Feilberg Anders
Environmental science & technology
Gaseous emissions from livestock production are complex mixtures including ammonia, methane, volatile organic compounds (VOC), and HS. These contribute to eutrophication, reduced air quality, global warming, and odor nuisance. It is imperative that these gases are mitigated in an environmentally sustainable manner. We present the discovery of a microbial inhibitor combo consisting of tannic acid and sodium fluoride (TA-NaF), which exhibits clear synergistic inhibition of ammonia production in pure bacteria culture and in pig manure while simultaneously inhibiting methane and odorant (HS and VOC) emissions. In laboratory headspace experiments on pig manure, we used proton-transfer-reaction mass spectrometry and cavity ring-down spectroscopy to measure the effect of TA-NaF on gaseous emissions. Ammonia emission was reduced by more than 95%, methane by up to ∼99%, and odor activity value by more than 50%. Microbial community analysis and gas emission data suggest that TA-NaF acts as an efficient generic microbial inhibitor, and we hypothesize that the synergistic inhibitory effect on ammonia production is related to tannic acid causing cell membrane leakage allowing fluoride ions easy access to urease.
10.1021/acs.est.0c01231
Inactivation of urease by catechol: Kinetics and structure.
Mazzei Luca,Cianci Michele,Musiani Francesco,Lente Gábor,Palombo Marta,Ciurli Stefano
Journal of inorganic biochemistry
Urease is a Ni(II)-containing enzyme that catalyzes the hydrolysis of urea to yield ammonia and carbamate at a rate 10 times higher than the uncatalyzed reaction. Urease is a virulence factor of several human pathogens, in addition to decreasing the efficiency of soil organic nitrogen fertilization. Therefore, efficient urease inhibitors are actively sought. In this study, we describe a molecular characterization of the interaction between urease from Sporosarcina pasteurii (SPU) and Canavalia ensiformis (jack bean, JBU) with catechol, a model polyphenol. In particular, catechol irreversibly inactivates both SPU and JBU with a complex radical-based autocatalytic multistep mechanism. The crystal structure of the SPU-catechol complex, determined at 1.50Å resolution, reveals the structural details of the enzyme inhibition.
10.1016/j.jinorgbio.2016.11.016
Inhibitory effect of polyphenols from sumac, pomegranate and Indian almond on urease producing bacteria and jack bean urease activity.
International journal of biological macromolecules
Urinary tract infection caused by Klebsiella, Proteus and Streptococcus is a urease dependent process, hence treatment of these infections by antibacterial compounds lies in inhibition of their virulence factors. The crude methanolic extracts derived from sumac fruit, pomegranate peel and Indian almond leaves were separated into anthocyanin and non-anthocyanin fractions using solid phase cartridges. The inhibitory effect of these fractions was determined on the growth of urease producing species and jack bean urease activity. Known compounds in the fractions were also docked with ureases of different biological origins viz. K. pneumoniae (PDB ID: 8HCN), K. aerogenes (PDB ID: 2KAU), Helicobacter pylori (PDB ID:8HC1)and Canavalia ensiformis (jack bean) (PDB ID: 3LA4) to determine their binding affinities and interaction with the enzyme. All the fractions showed significant inhibition growth for P. mirabilis, S. epidermidis and K.pneumoniae. Among the samples, sumac showed greatest inhibition against all (MIC 6-25 mg.mL) while among the fractions, anthocyanin was found to be most active (MIC 6-12 mg/mL). Likewise, all fractions inhibited urease with lowest ICs shown by sumac fractions (21-116 μg.mL). Out of 39 compounds docked, 27 showed interaction with movable flaps and/or active site of ureases which explains their mode of inhibition.
10.1016/j.ijbiomac.2024.133735
Evaluation of Geranium spp., Helleborus spp. and Hyssopus spp. polyphenolic extracts inhibitory activity against urease and α-chymotrypsin.
Paun Gabriela,Litescu Simona Carmen,Neagu Elena,Tache Andreia,Lucian Radu Gabriel
Journal of enzyme inhibition and medicinal chemistry
This study was meant to determine the inhibitory activity of tannins and flavonoid compounds from Geranium robertianum, Helleborus purpurascens and Hyssopus officinale plant polyphenol rich extracts against urease and α-chymotrypsin. The G. robertianum, H. purpurascens and H. officinale extracts were purified and concentrated by microfiltration and ultrafiltration. Phenolic compounds including flavonoids and tannins have been linked to many pharmacological activities. Thus, the polyphenolic content of the extracts was assessed by UV-Vis spectroscopy and HPLC. The concentrated extracts enriched in polyphenolic compounds (flavonoids, tannins and phenolic acids) showed a significant inhibition against urease from jack bean (over 90%), whereas in case of the α-chymotrypsin, they proved to have an inhibition below 54%. The results of this support the use of G. robertianum, H. purpurascens and H. officinale polyphenolic extracts as potential sources of urease inhibitors. Among the three plant extracts tested, H. officinale polyphenolic extracts exhibited a high inhibitory activity (92.67%) against urease and low inhibition (19.6%) against α-chymotrypsin and could be considered as possible remedy in ulcer treatment.
10.3109/14756366.2012.749399
In-silico design, synthesis, ADMET studies and biological evaluation of novel derivatives of Chlorogenic acid against Urease protein and bacterium.
BMC chemistry
BACKGROUND:Plants have always played important role in treating human and animal diseases as a therapeutic agent for traditional medicine. Through extensive research throughout the world, potential of natural products have been identified to control the over activity of many enzymes. - screening a library of chlorogenic acid derivatives highlighted some novel compounds which were found effective against urease enzyme and cancer causing bacterium. Selected top ligands possessing minimum binding energy and good docking score were synthesized in wet lab by suitable procedure and evaluated for urease enzyme inhibition and free radical scavenging property. Synthetic scheme includes three step reactions i. e protection of hydroxyl group of quinic acid part of chlorogenic acid with lactonisation process, anilide formation by reaction with substituted anilines followed by extraction with ethyl acetate under vacuum and deprotection of hydroxyl groups by treatment with hydrochloric acid. RESULTS:In-vitro results of the series concluded that compounds , and (IC 11.01 ± 0.013, 13.8 ± 0.041 and 15.86 ± 0.004 µM respectively in urease inhibition and 5.10 ± 0.018, 5.34 ± 0.007 and 6.01 ± 0.005 µM in antioxidant property against DPPH) were found to be significantly potent with excellent dock score - 10.091, - 10.603, - 9.833 and binding energy - 62.674, - 63.352, 56.267 kg/mol as compared to standard drugs thiourea and acetohydroxamic acid (- 3.459, - 3.049 and - 21.156 kJ/mol and - 17.454 kJ/mol) whereas compounds , (, ) exhibited moderate in vivo activity when compared to standard. CONCLUSIONS:Selected candidates from the outcome of in vitro urease inhibitory were further examined for anti- activity by well diffusion method against bacterium (DSM 4867). Compound showed significant anti- activity with zone of inhibition 10.00 ± 0.00 mm and MIC value 500 μg/mL as compared to standard drug acetohydroxamic acid having zone of inhibition 9.00 ± 0.50 mm and MIC 1000 μg/mL. Molecular docking studies also showed that compounds show strong inhibition by forming strong hydrogen bonding interactions with residues of pocket site in target protein. Hence, the present investigation studies will provide a new vision for the discovery of potent agents against and urease associated diseases.
10.1186/s13065-019-0556-0
Chlorogenic acid, caffeic acid and luteolin from dandelion as urease inhibitors: insights into the molecular interactions and inhibition mechanism.
Journal of the science of food and agriculture
BACKGROUND:Dandelion contains hundreds of active compounds capable of inhibiting urease activity, but the individual compounds have not yet been fully identified, and their effects and underlying mechanisms are not clear. The present study aimed to screen the urease inhibition active compounds of dandelion by urease inhibitory activity evaluation HPLC-tandem mass spectrometry analysis, their mechanism of urease inhibition by polyphenols was explored using enzyme kinetic studies via Lineweaver-Burk plots. Other investigations included isothermal titration calorimetry and surface plasmon resonance sensing, fluorescence quenching experiments, and single ligand molecular docking and two-ligand simultaneous docking techniques. RESULTS:The results indicated that the ethyl acetate fraction of dandelion flower exhibited the greatest inhibition (lowest IC 0.184 ± 0.007 mg mL). Chlorogenic acid, caffeic acid and luteolin could be effective urease inhibitors that acted in a non-competitive inhibition manner. Individually, chlorogenic acid could not only fast bind to urease, but also dissociate rapidly, whereas luteolin might interact with urease with the weakest affinity. The chlorogenic acid-caffeic acid combination exhibited an additive effect in urease inhibition. However, the chlorogenic acid-luteolin and caffeic acid-luteolin combinations exhibited antagonistic effects, with the caffeic acid-luteolin combination showing greater antagonism. CONCLUSION:The present study reveals that chlorogenic acid, caffeic acid and luteolin are major bioactive compounds for urease inhibition, indicating the molecular mechanisms. The antagonistic effects were observed between luteolin and chlorogenic acid/caffeic acid, and the interactions of the catalytic site and flap may account for the antagonistic effects. © 2024 Society of Chemical Industry.
10.1002/jsfa.13637
Catechin-based procyanidins from Peumus boldus Mol. aqueous extract inhibit Helicobacter pylori urease and adherence to adenocarcinoma gastric cells.
Pastene Edgar,Parada Víctor,Avello Marcia,Ruiz Antonieta,García Apolinaria
Phytotherapy research : PTR
In this work, the anti-Helicobacter pylori effect of an aqueous extract from dried leaves of Peumus boldus Mol. (Monimiaceae) was evaluated. This extract displayed high inhibitory activity against H. pylori urease. Therefore, in order to clarify the type of substances responsible for such effect, a bioassay-guided fractionation strategy was carried out. The active compounds in the fractions were characterized through different chromatographic methods (RP-HPLC; HILIC-HPLC). The fraction named F5 (mDP = 7.8) from aqueous extract was the most active against H. pylori urease with an IC50 = 15.9 µg gallic acid equivalents (GAE)/mL. HPLC analysis evidenced that F5 was composed mainly by catechin-derived proanthocyanidins (LC-MS and phloroglucinolysis). The anti-adherent effect of boldo was assessed by co-culture of H. pylori and AGS cells. Both the aqueous extract and F5 showed an anti-adherent effect in a concentration-dependent manner. An 89.3% of inhibition was reached at 2.0 mg GAE/mL of boldo extract. In conjunction, our results suggest that boldo extract has a potent anti-urease activity and anti-adherent effect against H. pylori, properties directly linked with the presence of catechin-derived proanthocyanidins.
10.1002/ptr.5176