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Biodegradation of an endocrine-disrupting chemical di-n-butyl phthalate by newly isolated Camelimonas sp. and enzymatic properties of its hydrolase

An aerobic bacterial strain M11 capable of degrading dibutyl phthalate (DBP) was isolated and identified as Camelimonas sp. This strain could not grow on dialkyl phthalates, including dimethyl, diethyl, dipropyl, dibutyl and dipentyl phthalate, but suspensions of cells could transform these compound...

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Published in:Biodegradation (Dordrecht) 2015-04, Vol.26 (2), p.171-182
Main Authors: Chen, Xu, Zhang, Xiaolong, Yang, Yu, Yue, Dongmei, Xiao, Lin, Yang, Liuyan
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creator Chen, Xu
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description An aerobic bacterial strain M11 capable of degrading dibutyl phthalate (DBP) was isolated and identified as Camelimonas sp. This strain could not grow on dialkyl phthalates, including dimethyl, diethyl, dipropyl, dibutyl and dipentyl phthalate, but suspensions of cells could transform these compounds to phthalate via corresponding monoalkyl phthalates. The degradation kinetics of DBP was best fitted by first-order kinetic equation. During growth in Brucella Selective Medium, M11 produced the high amounts of non-DBP-induced intracellular hydrolase in the stationary phase. The DBP hydrolase gene of M11 was cloned, and the recombinant DBP hydrolase had a high optimum degradation temperature (50 °C), and a wide range of pH and temperature stability.
doi_str_mv 10.1007/s10532-015-9725-6
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This strain could not grow on dialkyl phthalates, including dimethyl, diethyl, dipropyl, dibutyl and dipentyl phthalate, but suspensions of cells could transform these compounds to phthalate via corresponding monoalkyl phthalates. The degradation kinetics of DBP was best fitted by first-order kinetic equation. During growth in Brucella Selective Medium, M11 produced the high amounts of non-DBP-induced intracellular hydrolase in the stationary phase. The DBP hydrolase gene of M11 was cloned, and the recombinant DBP hydrolase had a high optimum degradation temperature (50 °C), and a wide range of pH and temperature stability.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>25773337</pmid><doi>10.1007/s10532-015-9725-6</doi><tpages>12</tpages></addata></record>
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subjects Aerobiosis
Alphaproteobacteria - chemistry
Alphaproteobacteria - enzymology
Amino Acid Sequence
Analysis
Aquatic Pollution
Bacteria
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biodegradation
Biodegradation, Environmental
Biomedical and Life Sciences
Brucella
Cloning, Molecular
Degradation
Dibutyl Phthalate - metabolism
Dimethyl
Endocrine Disruptors - metabolism
Enzymes
Escherichia coli - genetics
Escherichia coli - metabolism
Esters
Ethylenediaminetetraacetic acid
Gene Expression
Genes
Geochemistry
Humans
Hydrolases
Hydrolases - genetics
Hydrolases - metabolism
Kinetics
Life Sciences
Microbiology
Molecular Sequence Data
Optimization
Original Paper
Phosphate esters
Phthalates
Phylogeny
Plastics industry
Recombinant
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Sequence Alignment
Sewage - chemistry
Soil Science & Conservation
Strain
Terrestrial Pollution
Waste Management/Waste Technology
Waste Water Technology
Water Management
Water Pollutants, Chemical - metabolism
Water Pollution Control
title Biodegradation of an endocrine-disrupting chemical di-n-butyl phthalate by newly isolated Camelimonas sp. and enzymatic properties of its hydrolase
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