Non-enzymatic Transformation of Aflatoxin B1 by Pseudomonas geniculata m29.
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ABSTRACT:
SUBMITTER: Yao Y
PROVIDER: S-EPMC8383447 | biostudies-literature |
REPOSITORIES: biostudies-literature
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Project description:Due to toxicity and persistence of paraquat (a widely used herbicide), eco-friendly remediation approaches to its contamination and effective antidotes to its poisoning have been highly desired and raised increasing concerns. Paraquat degradation was lesser in aerobic soil in comparison with anaerobic soil, and humic-reducing microorganisms (HRMs) play a key role in paraquat anaerobic transformation process. However, the degradation pathways and related mechanisms remain poorly understood. In this study, we investigated the specific interaction mechanisms of the paraquat transformation processes mediated by a humic-reducing strain under anaerobic conditions. A strain of pure culture, designated as PQ01, was successfully isolated from paddy soil using anaerobic enrichment procedure, and identified as Pseudomonas geniculata using phenotypic and phylogenetic analysis. Sucrose, glucose, pyruvate, formic acid, and acetic acid were shown to be favorable electron donors for the reduction of anthrahydroquinone-2,6-disulfonate (AQDS) reduction by PQ01. The strain also had the ability of reducing Fe(III) (hydr)oxides in the presence of sucrose with efficiencies in the order of ferrihydrite > ?-FeOOH/?-FeOOH > ?-Fe2O3 > ?-Fe2O3. In the "PQ01 + paraquat + AQDS + sucrose" system, AQDS reduction and paraquat biotransformation by strain PQ01 occurred simultaneously, and the presence of sucrose significantly enhanced the biotransformation. Specific mechanisms of the electron transfer processes are promoted by both PQ01 and AQDS, and proceed in two aspects: (1) paraquat served as electron donor in the anaerobic reduction of AQDS by strain PQ01; (2) AQDS was reduced by PQ01 anaerobic metabolism to produce AH2QDS, which can directly react with paraquat under anaerobic conditions to generate a single crystal compound (molecular formula of the unit structure is C2 6H2 0N2O8S2), causing the paraquat to decline dramatically. In conclusion, this main mechanism included the microbial reduction of AQDS to AH2QDS, followed by the abiotic reaction between AH2QDS and paraquat. This study reported the new characteristics of P. geniculata capable of reducing humics analogs, Fe(III) (hydr)oxides, and paraquat, and proposed a novel electron transformation mechanism of the HRMs' mediated degradation of organic contaminants.
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Project description:Degradation or the removal of aflatoxin B1 from agriculture commodities is very important because of its acute toxicity and economic loss due to rejection of about 25% contaminated agri produce. The present study aimed at using Pseudomonas putida for the aflatoxin B1 (AFB1) degradation and to understand the mechanism involved. AFB1 degradation was studied with P. putida culture, culture supernatant, cell lysate, cell lysate in the presence of protease inhibitor, and heat-inactivated cell lysate. The remaining AFB1 was qualitatively and quantitatively measured by thin-layer chromatography and HPLC with a UV detector. P. putida culture and culture supernatant showed 80% reduction in AFB1 within 24 h of incubation. Cell lysate and the lysate in the presence of protease inhibitor showed the same reduction in 6 and 4 h respectively. The protease-inhibited lysate showed greater thermostability, broad pH range, and tolerance to some of the solvents and detergents in terms of aflatoxin B1 degrading activity. The heat-inactivated lysate showed only 20% reduction in 24 h of incubation indicating loss of activity on heating. As cell-free supernatant and cell lysate are capable of reducing AFB1 effectively, actively growing cells are not necessary for degradation. The active principle for degradation might be proteinaceous; therefore, heat-inactivated lysate is ineffective for reducing the AFB1. These results showed that degradation of aflatoxin B1 by P. putida might be an enzymatic process and could be used in a broad range of conditions.
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Project description:A bacterium, isolated from nodules of chickpea grown in alluvial soils of Haryana state of India, designated as IC-76 was characterized for in vitro plant growth-promoting (PGP) properties and further evaluated under greenhouse, on-station and on-farm field conditions for PGP activity in chickpea. The isolate IC-76 produced indole acetic acid, siderophore, hydrocyanic acid, cellulase, protease, and β-1,3-glucanase. When the bacterium was evaluated individually for their PGP potential in the greenhouse on chickpea and in combination with five Streptomyces sp. (strains CAI-24, CAI-121, CAI-127, KAI-32, and KAI-90; demonstrated earlier as biocontrol potential against Fusarium wilt disease in chickpea), the traits, including nodule number and weight, shoot, and root weight, pod number and weight, seed number and weight, available phosphorus and % organic carbon were found significantly, enhanced over un-inoculated control. In the on-station and on-farm field conditions, IC-76 significantly enhanced nodule number and weight, shoot, and root weight, stover and grain yield and total dry matter. In the rhizosphere (0-15 cm soil), the bacterium also significantly enhanced the total nitrogen, available phosphorus and % organic carbon. The sequence of 16S rDNA gene of the IC-76 was matched with Pseudomonas geniculata in BLAST analysis. This study demonstrates that IC-76 has the potential for PGP in chickpea.
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Project description:Aflatoxins B1 (AFB1) and G1 (AFG1) are carcinogenic mycotoxins that contaminate crops such as maize and groundnuts worldwide. The broadly accepted method to assess chronic human aflatoxin exposure is by quantifying the amount of aflatoxin adducted to human serum albumin. This has been reported using ELISA, HPLC, or LC-MS/MS to measure the amount of AFB1-lysine released after proteolysis of serum albumin. LC-MS/MS is the most accurate method but requires both isotopically labelled and unlabelled AFB1-lysine standards, which are not commercially available. In this work, we report a simplified synthetic route to produce unlabelled, deuterated and 13C6 15N2 labelled aflatoxin B1-lysine and for the first-time aflatoxin G1-lysine. Additionally, we report on the stability of these compounds during storage. This simplified synthetic approach will make the production of these important standards more feasible for laboratories performing aflatoxin exposure studies.
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Project description:Management of solid wastes with high nicotine content, such as those accumulated during tobacco manufacturing, poses a major challenge, which can be addressed by using bacteria such as Pseudomonas and Arthrobacter. In this study, a new species of Pseudomonas geniculata, namely strain N1, which is capable of efficiently degrading nicotine, was isolated and identified. The optimal growth conditions for strain N1 are a temperature of 30°C, and a pH 6.5, at a rotation rate of 120 rpm min(-1) with 1 g l(-1) nicotine as the sole source of carbon and nitrogen. Myosmine, cotinine, 6-hydroxynicotine, 6-hydroxy-N-methylmyosmine, and 6-hydroxy-pseudooxynicotine were detected as the five intermediates through gas chromatography-mass and liquid chromatography-mass analyses. The identified metabolites were different from those generated by Pseudomonas putida strains. The analysis also highlighted the bacterial metabolic diversity in relation to nicotine degradation by different Pseudomonas strains.
| S-EPMC3885553 | biostudies-literature
Project description:Aflatoxin B1 (AFB1), one of the most potent naturally occurring mutagens and carcinogens, causes significant threats to the food industry and animal production. In this study, 25 bacteria isolates were collected from grain kernels and soils displaying AFB1 reduction activity. Based on its degradation effectiveness, isolate N17-1 was selected for further characterization and identified as Pseudomonas aeruginosa. P. aeruginosa N17-1 could degrade AFB?, AFB? and AFM? by 82.8%, 46.8% and 31.9% after incubation in Nutrient Broth (NB) medium at 37 °C for 72 h, respectively. The culture supernatant of isolate N17-1 degraded AFB? effectively, whereas the viable cells and intra cell extracts were far less effective. Factors influencing AFB1 degradation by the culture supernatant were investigated. Maximum degradation was observed at 55 °C. Ions Mn²? and Cu²? were activators for AFB1 degradation, however, ions Mg²?, Li?, Zn²?, Se²?, Fe³? were strong inhibitors. Treatments with proteinase K and proteinase K plus SDS significantly reduced the degradation activity of the culture supernatant. No degradation products were observed based on preliminary LC-QTOF/MS analysis, indicating AFB? was metabolized to degradation products with chemical properties different from that of AFB?. The results indicated that the degradation of AFB? by P. aeruginosa N17-1 was enzymatic and could have a great potential in industrial applications. This is the first report indicating that the isolate of P. aeruginosa possesses the ability to degrade aflatoxin.
| S-EPMC4210884 | biostudies-literature
Project description:MotivationThe design of enzymes is as challenging as it is consequential for making chemical synthesis in medical and industrial applications more efficient, cost-effective and environmentally friendly. While several aspects of this complex problem are computationally assisted, the drafting of catalytic mechanisms, i.e. the specification of the chemical steps-and hence intermediate states-that the enzyme is meant to implement, is largely left to human expertise. The ability to capture specific chemistries of multistep catalysis in a fashion that enables its computational construction and design is therefore highly desirable and would equally impact the elucidation of existing enzymatic reactions whose mechanisms are unknown.ResultsWe use the mathematical framework of graph transformation to express the distinction between rules and reactions in chemistry. We derive about 1000 rules for amino acid side chain chemistry from the M-CSA database, a curated repository of enzymatic mechanisms. Using graph transformation, we are able to propose hundreds of hypothetical catalytic mechanisms for a large number of unrelated reactions in the Rhea database. We analyze these mechanisms to find that they combine in chemically sound fashion individual steps from a variety of known multistep mechanisms, showing that plausible novel mechanisms for catalysis can be constructed computationally.Availability and implementationThe source code of the initial prototype of our approach is available at https://github.com/Nojgaard/mechsearch.Supplementary informationSupplementary data are available at Bioinformatics online.
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Project description:This study proposes the development of an electrochemical sensor based on fabrication of a glassy carbon electrode (GCE) with Fe3O4-polyaniline (Fe3O4-PANI) nanocomposite, which was further used for enzyme-less detection of 2,4-dichlorophenoxyacetic acid (2,4-D) in aqueous medium. Spectroscopic studies, microstructural studies, and elemental analysis established the formation of Fe3O4 nanoparticles with polyaniline coating. The fabricated Fe3O4-PANI-GCE was characterized by electrochemical techniques like cyclic voltammetry and electrochemical impedance spectroscopy. The electrochemical response of 2,4-D on Fe3O4-PANI-GCE was evaluated by performing cyclic voltammetry and amperometry experiments. The synergistic effect of the composite causes the superior electrochemical behavior of Fe3O4-PANI-GCE toward the detection of 2,4-D. Amperometric measurements exhibited a linear concentration range from 1.35 to 2.7 μM. The sensitivity and detection limit were evaluated from the amperometric responses, which were found to be 4.62 × 10-7 μA μM-1 cm-2 and 0.21 μM, respectively. The electrochemical sensing response could be attributed to adsorption of 2,4-D onto the Fe3O4-PANI-modified GCE (Fe3O4-PANI-GCE) surface. Fe3O4-PANI-GCE is found to be a simple, low-cost, and biocompatible non-enzymatic sensor for detection of 2,4-D in aqueous medium at ambient temperature.
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Project description:The global demand for food could double in another 40 y owing to growth in the population and food consumption per capita. To meet the world's future food and sustainability needs for biofuels and renewable materials, the production of starch-rich cereals and cellulose-rich bioenergy plants must grow substantially while minimizing agriculture's environmental footprint and conserving biodiversity. Here we demonstrate one-pot enzymatic conversion of pretreated biomass to starch through a nonnatural synthetic enzymatic pathway composed of endoglucanase, cellobiohydrolyase, cellobiose phosphorylase, and alpha-glucan phosphorylase originating from bacterial, fungal, and plant sources. A special polypeptide cap in potato alpha-glucan phosphorylase was essential to push a partially hydrolyzed intermediate of cellulose forward to the synthesis of amylose. Up to 30% of the anhydroglucose units in cellulose were converted to starch; the remaining cellulose was hydrolyzed to glucose suitable for ethanol production by yeast in the same bioreactor. Next-generation biorefineries based on simultaneous enzymatic biotransformation and microbial fermentation could address the food, biofuels, and environment trilemma.
| S-EPMC3645547 | biostudies-literature
Project description:BackgroundAflatoxins are carcinogenic compounds produced by certain species of Aspergillus fungi. The consumption of crops contaminated with this toxin cause serious detrimental health effects, including death, in both livestock and humans. As a consequence, both the detection and quantification of this toxin in food/feed items is tightly regulated with crops exceeding the allowed limits eliminated from food chains. Globally, this toxin causes massive agricultural and economic losses each year.ResultsIn this paper we investigate the feasibility of using an aflatoxin-degrading enzyme strategy to reduce/eliminate aflatoxin loads in developing maize kernels. We used an endoplasmic reticulum (ER) targeted sub-cellular compartmentalization stabilizing strategy to accumulate an aflatoxin-degrading enzyme isolated from the edible Honey mushroom Armillariella tabescens and expressed it in embryo tissue in developing maize kernels. Three transgenic maize lines that were determined to be expressing the aflatoxin-degrading enzyme both at the RNA and protein level, were challenged with the aflatoxin-producing strain Aspergillus flavus AF13 and shown to accumulate non-detectable levels of aflatoxin at 14-days post-infection and significantly reduced levels of aflatoxin at 30-days post-infection compared to nontransgenic control Aspergillus-challenged samples.ConclusionsThe expression of an aflatoxin-degrading enzyme in developing maize kernels was shown to be an effective means to control aflatoxin in maize in pre-harvest conditions. This aflatoxin-degradation strategy could play a significant role in the enhancement of both US and global food security and sustainability.
| S-EPMC8684248 | biostudies-literature