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Wulf-dieter Moll - One of the best experts on this subject based on the ideXlab platform.
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Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid
BMC Microbiology, 2015Co-Authors: Michaela Thamhesl, Elisabeth Apfelthaler, Heidi Elisabeth Schwartz-zimmermann, Elisavet Kunz-vekiru, Wolfgang Kneifel, Gerd Schatzmayr, Rudolf Krska, Wulf-dieter MollAbstract:Background Ergopeptines are a predominant class of ergot alkaloids produced by tall fescue grass endophyte Neotyphodium coenophialum or cereal pathogen Claviceps purpurea . The vasoconstrictive activity of ergopeptines makes them toxic for mammals, and they can be a problem in Animal husbandry. Results We isolated an ergopeptine degrading bacterial strain, MTHt3, and classified it, based on its 16S rDNA sequence, as a strain of Rhodococcus erythropolis ( Nocardiaceae, Actinobacteria ). For strain isolation, mixed microbial cultures were obtained from artificially ergot alkaloid-enriched soil, and provided with the ergopeptine ergotamine in mineral medium for enrichment. Individual colonies derived from such mixed cultures were screened for ergotamine degradation by high performance liquid chromatography and fluorescence detection. R. erythropolis MTHt3 converted ergotamine to ergine (lysergic acid amide) and further to lysergic acid, which accumulated as an end product. No other tested R. erythropolis strain degraded ergotamine. R. erythropolis MTHt3 degraded all ergopeptines found in an ergot extract, namely ergotamine, ergovaline, ergocristine, ergocryptine, ergocornine, and ergosine, but the simpler lysergic acid derivatives agroclavine, chanoclavine, and ergometrine were not degraded. Temperature and pH dependence of ergotamine and ergine bioconversion activity was different for the two reactions. Conclusions Degradation of ergopeptines to ergine is a previously unknown microbial reaction. The reaction end product, lysergic acid, has no or much lower vasoconstrictive activity than ergopeptines. If the genes encoding enzymes for ergopeptine catabolism can be cloned and expressed in recombinant hosts, application of ergopeptine and ergine degrading enzymes for reduction of toxicity of ergot alkaloid-Contaminated Animal feed may be feasible.
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Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid
BMC Microbiology, 2015Co-Authors: Michaela Thamhesl, Elisabeth Apfelthaler, Heidi Elisabeth Schwartz-zimmermann, Elisavet Kunz-vekiru, Wolfgang Kneifel, Gerd Schatzmayr, Rudolf Krska, Wulf-dieter MollAbstract:Ergopeptines are a predominant class of ergot alkaloids produced by tall fescue grass endophyte Neotyphodium coenophialum or cereal pathogen Claviceps purpurea. The vasoconstrictive activity of ergopeptines makes them toxic for mammals, and they can be a problem in Animal husbandry. We isolated an ergopeptine degrading bacterial strain, MTHt3, and classified it, based on its 16S rDNA sequence, as a strain of Rhodococcus erythropolis (Nocardiaceae, Actinobacteria). For strain isolation, mixed microbial cultures were obtained from artificially ergot alkaloid-enriched soil, and provided with the ergopeptine ergotamine in mineral medium for enrichment. Individual colonies derived from such mixed cultures were screened for ergotamine degradation by high performance liquid chromatography and fluorescence detection. R. erythropolis MTHt3 converted ergotamine to ergine (lysergic acid amide) and further to lysergic acid, which accumulated as an end product. No other tested R. erythropolis strain degraded ergotamine. R. erythropolis MTHt3 degraded all ergopeptines found in an ergot extract, namely ergotamine, ergovaline, ergocristine, ergocryptine, ergocornine, and ergosine, but the simpler lysergic acid derivatives agroclavine, chanoclavine, and ergometrine were not degraded. Temperature and pH dependence of ergotamine and ergine bioconversion activity was different for the two reactions. Degradation of ergopeptines to ergine is a previously unknown microbial reaction. The reaction end product, lysergic acid, has no or much lower vasoconstrictive activity than ergopeptines. If the genes encoding enzymes for ergopeptine catabolism can be cloned and expressed in recombinant hosts, application of ergopeptine and ergine degrading enzymes for reduction of toxicity of ergot alkaloid-Contaminated Animal feed may be feasible.
Charlotta Löfström - One of the best experts on this subject based on the ideXlab platform.
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Evaluation of pre-PCR processing approaches for enumeration of Salmonella enterica in naturally Contaminated Animal feed.
Journal of applied microbiology, 2013Co-Authors: Jenny Schelin, M. Gunnar Andersson, Håkan Vigre, Börje Norling, Per Häggblom, Jeffrey Hoorfar, Peter Rådström, Charlotta LöfströmAbstract:Three pre-PCR processing strategies for the detection and/or quantification of Salmonella in naturally Contaminated soy bean meal were evaluated.
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Validation of a Diagnostic PCR Method for Routine Analysis of Salmonella spp. in Animal Feed Samples
Food Analytical Methods, 2008Co-Authors: Charlotta Löfström, Charlotta Engdahl Axelsson, Peter RådströmAbstract:As a part of a validation study, a comparative study of a PCR method and the standard culture-based method NMKL-71, for detection of Salmonella, was performed according to the validation protocol from the Nordic validation organ for validation of alternative microbiological methods (NordVal) on 250 artificially or naturally Contaminated Animal feed samples. The PCR method is based on culture enrichment in buffered peptone water followed by PCR using the DNA polymerase Tth and an internal amplification control. No significant difference was found between the two methods. The relative accuracy, relative sensitivity and relative specificity were found to be 96.0, 97.3, and 98.8%, respectively. PCR inhibition was observed for rape seed samples. For the acidified feed samples, more Salmonella -positive samples were found with the PCR method compared to the NMKL method. This study focuses on the growing demand for validated diagnostic PCR methods for routine analysis of Animal feed and food samples to assure safety in the food production chain.
Michaela Thamhesl - One of the best experts on this subject based on the ideXlab platform.
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Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid
BMC Microbiology, 2015Co-Authors: Michaela Thamhesl, Elisabeth Apfelthaler, Heidi Elisabeth Schwartz-zimmermann, Elisavet Kunz-vekiru, Wolfgang Kneifel, Gerd Schatzmayr, Rudolf Krska, Wulf-dieter MollAbstract:Background Ergopeptines are a predominant class of ergot alkaloids produced by tall fescue grass endophyte Neotyphodium coenophialum or cereal pathogen Claviceps purpurea . The vasoconstrictive activity of ergopeptines makes them toxic for mammals, and they can be a problem in Animal husbandry. Results We isolated an ergopeptine degrading bacterial strain, MTHt3, and classified it, based on its 16S rDNA sequence, as a strain of Rhodococcus erythropolis ( Nocardiaceae, Actinobacteria ). For strain isolation, mixed microbial cultures were obtained from artificially ergot alkaloid-enriched soil, and provided with the ergopeptine ergotamine in mineral medium for enrichment. Individual colonies derived from such mixed cultures were screened for ergotamine degradation by high performance liquid chromatography and fluorescence detection. R. erythropolis MTHt3 converted ergotamine to ergine (lysergic acid amide) and further to lysergic acid, which accumulated as an end product. No other tested R. erythropolis strain degraded ergotamine. R. erythropolis MTHt3 degraded all ergopeptines found in an ergot extract, namely ergotamine, ergovaline, ergocristine, ergocryptine, ergocornine, and ergosine, but the simpler lysergic acid derivatives agroclavine, chanoclavine, and ergometrine were not degraded. Temperature and pH dependence of ergotamine and ergine bioconversion activity was different for the two reactions. Conclusions Degradation of ergopeptines to ergine is a previously unknown microbial reaction. The reaction end product, lysergic acid, has no or much lower vasoconstrictive activity than ergopeptines. If the genes encoding enzymes for ergopeptine catabolism can be cloned and expressed in recombinant hosts, application of ergopeptine and ergine degrading enzymes for reduction of toxicity of ergot alkaloid-Contaminated Animal feed may be feasible.
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Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid
BMC Microbiology, 2015Co-Authors: Michaela Thamhesl, Elisabeth Apfelthaler, Heidi Elisabeth Schwartz-zimmermann, Elisavet Kunz-vekiru, Wolfgang Kneifel, Gerd Schatzmayr, Rudolf Krska, Wulf-dieter MollAbstract:Ergopeptines are a predominant class of ergot alkaloids produced by tall fescue grass endophyte Neotyphodium coenophialum or cereal pathogen Claviceps purpurea. The vasoconstrictive activity of ergopeptines makes them toxic for mammals, and they can be a problem in Animal husbandry. We isolated an ergopeptine degrading bacterial strain, MTHt3, and classified it, based on its 16S rDNA sequence, as a strain of Rhodococcus erythropolis (Nocardiaceae, Actinobacteria). For strain isolation, mixed microbial cultures were obtained from artificially ergot alkaloid-enriched soil, and provided with the ergopeptine ergotamine in mineral medium for enrichment. Individual colonies derived from such mixed cultures were screened for ergotamine degradation by high performance liquid chromatography and fluorescence detection. R. erythropolis MTHt3 converted ergotamine to ergine (lysergic acid amide) and further to lysergic acid, which accumulated as an end product. No other tested R. erythropolis strain degraded ergotamine. R. erythropolis MTHt3 degraded all ergopeptines found in an ergot extract, namely ergotamine, ergovaline, ergocristine, ergocryptine, ergocornine, and ergosine, but the simpler lysergic acid derivatives agroclavine, chanoclavine, and ergometrine were not degraded. Temperature and pH dependence of ergotamine and ergine bioconversion activity was different for the two reactions. Degradation of ergopeptines to ergine is a previously unknown microbial reaction. The reaction end product, lysergic acid, has no or much lower vasoconstrictive activity than ergopeptines. If the genes encoding enzymes for ergopeptine catabolism can be cloned and expressed in recombinant hosts, application of ergopeptine and ergine degrading enzymes for reduction of toxicity of ergot alkaloid-Contaminated Animal feed may be feasible.
Andreas Schäffer - One of the best experts on this subject based on the ideXlab platform.
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Safety Evaluation for a Biodiesel Process Using Prion-Contaminated Animal Fat as a Source (6 pp)
Environmental Science and Pollution Research, 2006Co-Authors: Björn Seidel, Martin Alm, Rainer Peters, Werner Kördel, Andreas SchäfferAbstract:Background Due to the bovine spongiform encephalopathy (BSE), specified risk material (SRM) as well as Animal meat and bone meal (MBM) are banned from the food and feed chain because of a possible infection with pathogenic prions (PrPSc). Nowadays, prions are widely accepted to be responsible for TSE(transmissible spongiform encephalopathies)-caused illnesses like BSE and scrapie, and especially for the occurrence of the new variant of CJD in humans. Presently, SRM and MBM are burnt under high temperatures to avoid any hazards for humans, Animals or the environment. The aim of this study was to evaluate a method using Animal fat separated from Category I material which includes SRM and the carcasses of TSE-infected Animals, or Animals suspected of being infected with TSE, as a source for producing biodiesel by transesterification, analogous to the biodiesel process using vegetable oil. Methods For this purpose, Animal fat was spiked with scrapie-infected hamster brain equivalents – as representative for a TSE-infected Animal – and the biodiesel manufacturing process was downscaled and performed under lab-scale conditions. Results and Discussion The results analysed by Western blotting showed clearly that almost each single step of the process leads to a significant reduction of the concentration of the pathogenic prion protein (PrPSc) in the main and side-products. Conclusion The data revealed that the biodiesel production, even from material with a high concentration of pathogenic prions, can be considered as safe. Recommendations and Outlook The obtained results indicated that biodiesel produced from prion-Contaminated fat was safe under the tested process conditions. However, it has to be pointed out that the results cannot be generalized because a different process control using other conditions may lead to different results and then has to be analysed independently. It is clear that the production of biodiesel from high risk material represents a more economic usage than the combustion of such material.
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Safety Evaluation for a Biodiesel Process Using Prion-Contaminated Animal Fat as a Source (6 pp)
Environmental science and pollution research international, 2005Co-Authors: Björn Seidel, Martin Alm, Rainer Peters, Werner Kördel, Andreas SchäfferAbstract:Background Due to the bovine spongiform encephalopathy (BSE), specified risk material (SRM) as well as Animal meat and bone meal (MBM) are banned from the food and feed chain because of a possible infection with pathogenic prions (PrPSc). Nowadays, prions are widely accepted to be responsible for TSE(transmissible spongiform encephalopathies)-caused illnesses like BSE and scrapie, and especially for the occurrence of the new variant of CJD in humans. Presently, SRM and MBM are burnt under high temperatures to avoid any hazards for humans, Animals or the environment. The aim of this study was to evaluate a method using Animal fat separated from Category I material which includes SRM and the carcasses of TSE-infected Animals, or Animals suspected of being infected with TSE, as a source for producing biodiesel by transesterification, analogous to the biodiesel process using vegetable oil.
Peter Rådström - One of the best experts on this subject based on the ideXlab platform.
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Evaluation of pre-PCR processing approaches for enumeration of Salmonella enterica in naturally Contaminated Animal feed.
Journal of applied microbiology, 2013Co-Authors: Jenny Schelin, M. Gunnar Andersson, Håkan Vigre, Börje Norling, Per Häggblom, Jeffrey Hoorfar, Peter Rådström, Charlotta LöfströmAbstract:Three pre-PCR processing strategies for the detection and/or quantification of Salmonella in naturally Contaminated soy bean meal were evaluated.
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Validation of a Diagnostic PCR Method for Routine Analysis of Salmonella spp. in Animal Feed Samples
Food Analytical Methods, 2008Co-Authors: Charlotta Löfström, Charlotta Engdahl Axelsson, Peter RådströmAbstract:As a part of a validation study, a comparative study of a PCR method and the standard culture-based method NMKL-71, for detection of Salmonella, was performed according to the validation protocol from the Nordic validation organ for validation of alternative microbiological methods (NordVal) on 250 artificially or naturally Contaminated Animal feed samples. The PCR method is based on culture enrichment in buffered peptone water followed by PCR using the DNA polymerase Tth and an internal amplification control. No significant difference was found between the two methods. The relative accuracy, relative sensitivity and relative specificity were found to be 96.0, 97.3, and 98.8%, respectively. PCR inhibition was observed for rape seed samples. For the acidified feed samples, more Salmonella -positive samples were found with the PCR method compared to the NMKL method. This study focuses on the growing demand for validated diagnostic PCR methods for routine analysis of Animal feed and food samples to assure safety in the food production chain.