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dc.contributor.author
Kadri, Tayssir
dc.contributor.author
Rouissi, Tarek
dc.contributor.author
Brar, Satinder Kaur
dc.contributor.author
Cledón, Maximiliano
dc.contributor.author
Sarma, Saurabhjyoti
dc.contributor.author
Verma, Mausam
dc.date.available
2020-03-27T18:46:16Z
dc.date.issued
2017-01
dc.identifier.citation
Kadri, Tayssir; Rouissi, Tarek; Brar, Satinder Kaur; Cledón, Maximiliano; Sarma, Saurabhjyoti; et al.; Biodegradation of polycyclic aromatic hydrocarbons (PAHs) by fungal enzymes: A review; Science Press; Journal of Environmental Sciences; 51; 1-2017; 52-74
dc.identifier.issn
1001-0742
dc.identifier.uri
http://hdl.handle.net/11336/101093
dc.description.abstract
Polycyclic aromatic hydrocarbons (PAHs) are a large group of chemicals. They represent an important concern due to their widespread distribution in the environment, their resistance to biodegradation, their potential to bioaccumulate and their harmful effects. Several pilot treatments have been implemented to prevent economic consequences and deterioration of soil and water quality. As a promising option, fungal enzymes are regarded as a powerful choice for degradation of PAHs. Phanerochaete chrysosporium, Pleurotus ostreatus and Bjerkandera adusta are most commonly used for the degradation of such compounds due to their production of ligninolytic enzymes such as lignin peroxidase, manganese peroxidase and laccase. The rate of biodegradation depends on many culture conditions, such as temperature, oxygen, accessibility of nutrients and agitated or shallow culture. Moreover, the addition of biosurfactants can strongly modify the enzyme activity. The removal of PAHs is dependent on the ionization potential. The study of the kinetics is not completely comprehended, and it becomes more challenging when fungi are applied for bioremediation. Degradation studies in soil are much more complicated than liquid cultures because of the heterogeneity of soil, thus, many factors should be considered when studying soil bioremediation, such as desorption and bioavailability of PAHs. Different degradation pathways can be suggested. The peroxidases are heme-containing enzymes having common catalytic cycles. One molecule of hydrogen peroxide oxidizes the resting enzyme withdrawing two electrons. Subsequently, the peroxidase is reduced back in two steps of one electron oxidation. Laccases are copper-containing oxidases. They reduce molecular oxygen to water and oxidize phenolic compounds.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Science Press
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
BIODEGRADATION
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ENZYMES
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FUNGI
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POLYCYCLIC AROMATIC HYDROCARBONS (PAHS)
dc.subject.classification
Otras Ingeniería del Medio Ambiente
dc.subject.classification
Ingeniería del Medio Ambiente
dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS
dc.title
Biodegradation of polycyclic aromatic hydrocarbons (PAHs) by fungal enzymes: A review
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-03-25T13:59:51Z
dc.journal.volume
51
dc.journal.pagination
52-74
dc.journal.pais
China
dc.description.fil
Fil: Kadri, Tayssir. Université du Québec a Montreal; Canadá
dc.description.fil
Fil: Rouissi, Tarek. Université du Québec a Montreal; Canadá
dc.description.fil
Fil: Brar, Satinder Kaur. Université du Québec a Montreal; Canadá
dc.description.fil
Fil: Cledón, Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; Argentina. Université du Québec a Montreal; Canadá
dc.description.fil
Fil: Sarma, Saurabhjyoti. Université du Québec a Montreal; Canadá
dc.description.fil
Fil: Verma, Mausam. Université du Québec a Montreal; Canadá
dc.journal.title
Journal of Environmental Sciences
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.jes.2016.08.023
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1001074216306167
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