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1.
Chemosphere ; 239: 124796, 2020 Jan.
Article in English | MEDLINE | ID: mdl-31520972

ABSTRACT

In July 2013, a fatal train derailment led to an explosion and fire in the town of Lac-Mégantic (LM), Quebec, and the crude oil contamination of regional surface water, soil, and sediment in the adjacent Lake Mégantic. This study investigated the degradation potential of the spilled crude oil by using the sediments from the incident site as the source of microorganisms. Two light crude oils (LM source oil and Alberta Sweet Mixed Blend (ASMB)) were tested at 22 °C for 4 weeks and 4 °C for 8 weeks, respectively. The post-incubation biological and chemical information of the samples were analysed. There was no marked difference in degradation efficacy and biological activities for both the LM and ASMB oils, although the biodegradation potential differed between the two incubations. Higher temperature favoured the growth of microorganisms, thus for the degradation of all petroleum hydrocarbons, except for some conservative biomarkers. The degradation of both oils followed the order of resolved components > total saturated hydrocarbons (TSH) > unresolved complex mixture (UCM) >total aromatic hydrocarbons (TAH). Normal alkanes were generally degraded more significantly than branched ones, and polycyclic aromatic hydrocarbons (PAHs). Degradation of polycyclic aromatic hydrocarbons (PAHs) and their alkylated congeners (APAHs) for both incubations generally decreased as the number of aromatic rings, and the degree of alkylation increased. This study showed that the LM sediments can biodegrade the petroleum hydrocarbons efficaciously if appropriate ambient temperatures are generated to favour the growth of autochthonous microorganisms.


Subject(s)
Geologic Sediments/microbiology , Hydrocarbons/chemistry , Hydrocarbons/metabolism , Petroleum/metabolism , Water Pollutants, Chemical/metabolism , Alkanes/chemistry , Alkanes/metabolism , Biodegradation, Environmental , Lakes/microbiology , Petroleum Pollution , Polycyclic Aromatic Hydrocarbons/chemistry , Polycyclic Aromatic Hydrocarbons/metabolism , Quebec , Temperature , Water Pollutants, Chemical/chemistry
2.
In Vitro Cell Dev Biol Anim ; 51(6): 644-50, 2015 Jun.
Article in English | MEDLINE | ID: mdl-25588777

ABSTRACT

New health safety concerns may arise from the increasing production and use of Jatropha oil, a biodiesel feedstock that also contains toxic, pro-inflammatory, and co-carcinogenic phorbol esters. Based on the exceptional sensitivity of Madin-Darby canine kidney (MDCK) cells to the model phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA), a robust bioassay was developed to quantify the biological activity of Jatropha phorbol esters directly in oil, without sample extraction. We first verified that the characteristic response of MDCK cells to TPA was also observed following direct exposure to phorbol esters in Jatropha oil. We further confirmed that similarly to TPA, Jatropha oil's phorbol esters can activate protein kinase C (PKC). We then assessed the transcriptional response of MDCK cells to Jatropha oil exposure by measuring the expression of cyclooxygenase-2 (COX-2), a gene involved in inflammatory processes which is strongly upregulated following PKC activation. Based on the parameterization of a TPA dose-response curve, the transcriptional response of MDCK cells to Jatropha oil exposure was expressed in term of TPA toxic equivalent (TEQ), a convenient metric to report the inflammatory potential of complex mixtures. The sensitive bioassay described in this manuscript may prove useful for risk assessment, as it provides a quantitative method and a convenient metric to report the inflammatory potential of phorbol esters in Jatropha oil. This bioassay may also be adapted for the detection of bioactive phorbol esters in other matrices.


Subject(s)
Biological Assay/methods , Inflammation Mediators/pharmacology , Jatropha/chemistry , Plant Oils/chemistry , Tetradecanoylphorbol Acetate/pharmacology , Animals , Cell Shape/drug effects , Cyclooxygenase 2/genetics , Cyclooxygenase 2/metabolism , Dogs , Enzyme Activation/drug effects , Gene Expression Regulation, Enzymologic/drug effects , Madin Darby Canine Kidney Cells , Protein Kinase C/metabolism
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