Biotransformation of benzo[a]pyrene by the thermophilic bacterium <Emphasis Type="Italic">Bacillus licheniformis</Emphasis> M2-7 |
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Authors: | Joseph Guevara-Luna Patricia Alvarez-Fitz Elvira Ríos-Leal Macdiel Acevedo-Quiroz Sergio Encarnación-Guevara Ma Elena Moreno-Godinez Mildred Castellanos-Escamilla Jeiry Toribio-Jiménez Yanet Romero-Ramírez |
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Institution: | 1.Laboratorio de Microbiología Molecular y Biotecnología Ambiental, Unidad Académica de Ciencias Químico Biológicas,Universidad Autónoma de Guerrero,Chilpancingo,Mexico;2.Laboratorio de Toxicología y Salud Ambiental,Universidad Autónoma de Guerrero, México,Chilpancingo,Mexico;3.Departamento de Biotecnología y Bioingeniería,Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional,Mexico,Mexico;4.Centro de Investigaciones Químicas,Universidad Autónoma de Morelos,Cuernavaca,Mexico;5.Laboratorio de proteómica, Centro de Ciencias Genómicas,Universidad Nacional Autónoma de México,Cuernavaca,Mexico;6.Biochemistry and Molecular Biology Department,University of Calgary,Calgary,Canada |
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Abstract: | Benzoa]pyrene (BaP) is recognized as a potentially carcinogenic and mutagenic hydrocarbon, and thus, its removal from the environment is a priority. The use of thermophilic bacteria capable of biodegrading or biotransforming this compound to less toxic forms has been explored in recent decades, since it provides advantages compared to mesophilic organisms. This study assessed the biotransformation of BaP by the thermophilic bacterium Bacillus licheniformis M2-7. Our analysis of the biotransformation process mediated by strain M2-7 on BaP shows that it begins during the first 3 h of culture. The gas chromatogram of the compound produced shows a peak with a retention time of 17.38 min, and the mass spectra shows an approximate molecular ion of m/z 167, which coincides with the molecular weight of the chemical formula C6H4(COOH)2, confirming a chemical structure corresponding to phthalic acid. Catechol 2,3-dioxygenase (C23O) enzyme activity was detected in minimal saline medium supplemented with BaP (0.33 U mg?1 of protein). This finding suggests that B. licheniformis M2-7 uses the meta pathway for biodegrading BaP using the enzyme C23O, thereby generating phthalic acid as an intermediate. |
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