RESUMO
Bacterial strain Delftia sp. TBKNP-05, isolated by para-hydroxybenzoate enrichment technique, is capable of degrading di-n-butylphthalate (DBP) as a sole source of carbon and energy. Analysis of intermediates by thin-layer chromatography and high-performance liquid chromatography indicated the presence of monobutylphthalate (MBP), phthalate (PA), and protocatechuate (PCA). The washed cells grown on DBP and PA showed appreciable oxidation of DBP, MBP, PA, and PCA. The enzyme activities in cell-free extracts of Delftia sp. TBKNP-05 exhibited the presence of DBP esterase, MBP esterase, PA-dioxygenase, and PCA 4,5-dioxygenase. The PCA is metabolized by meta-cleavage pathway, leading to further mineralization of the compound in this bacterium.
Assuntos
Delftia/metabolismo , Dibutilftalato/metabolismo , Plastificantes/metabolismo , Biodegradação Ambiental , Meios de Cultura , DNA Ribossômico/análise , Delftia/classificação , Delftia/enzimologia , Delftia/genética , Dioxigenases/metabolismo , Esterases/metabolismo , Dados de Sequência Molecular , Oxirredução , Ácidos Ftálicos/metabolismo , Filogenia , RNA Ribossômico 16S/genética , Análise de Sequência de DNARESUMO
A bacterial strain Delftia sp. TBKNP-05 isolated by para-hydroxybenzoate enrichment technique is capable of degrading di-n-butylphthalate (DBP) as a sole source of carbon and energy. Analysis of intermediates by thin layer chromatography and high performance liquid chromatography indicated the presence of monobutylphthalate (MBP), phthalate (PA), and protocatechuate (PCA). The washed cells grown on DBP and PA showed appreciable oxidation of DBP, MBP, PA, and PCA. The enzyme activities in cell free extracts of Delftia sp. TBKNP-05 exhibited the presence of DBP esterase, MBP esterase, PA-dioxygenase, and protocatechuate 4, 5-dioxygenase. The protocatechuate is metabolized by a meta-cleavage pathway leading to further mineralization of the compound in this bacterium.
