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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 |
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creator | Chen, Xu Zhang, Xiaolong Yang, Yu Yue, Dongmei Xiao, Lin Yang, Liuyan |
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 |
format | article |
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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.</description><identifier>ISSN: 0923-9820</identifier><identifier>EISSN: 1572-9729</identifier><identifier>DOI: 10.1007/s10532-015-9725-6</identifier><identifier>PMID: 25773337</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>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</subject><ispartof>Biodegradation (Dordrecht), 2015-04, Vol.26 (2), p.171-182</ispartof><rights>Springer Science+Business Media Dordrecht 2015</rights><rights>COPYRIGHT 2015 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c613t-a4c3c69b26222cbcc494eaad68631296b660ba591d198c17df5daa102c4948af3</citedby><cites>FETCH-LOGICAL-c613t-a4c3c69b26222cbcc494eaad68631296b660ba591d198c17df5daa102c4948af3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25773337$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chen, Xu</creatorcontrib><creatorcontrib>Zhang, Xiaolong</creatorcontrib><creatorcontrib>Yang, Yu</creatorcontrib><creatorcontrib>Yue, Dongmei</creatorcontrib><creatorcontrib>Xiao, Lin</creatorcontrib><creatorcontrib>Yang, Liuyan</creatorcontrib><title>Biodegradation of an endocrine-disrupting chemical di-n-butyl phthalate by newly isolated Camelimonas sp. and enzymatic properties of its hydrolase</title><title>Biodegradation (Dordrecht)</title><addtitle>Biodegradation</addtitle><addtitle>Biodegradation</addtitle><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.</description><subject>Aerobiosis</subject><subject>Alphaproteobacteria - chemistry</subject><subject>Alphaproteobacteria - enzymology</subject><subject>Amino Acid Sequence</subject><subject>Analysis</subject><subject>Aquatic Pollution</subject><subject>Bacteria</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biodegradation</subject><subject>Biodegradation, Environmental</subject><subject>Biomedical and Life Sciences</subject><subject>Brucella</subject><subject>Cloning, Molecular</subject><subject>Degradation</subject><subject>Dibutyl Phthalate - metabolism</subject><subject>Dimethyl</subject><subject>Endocrine Disruptors - metabolism</subject><subject>Enzymes</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Esters</subject><subject>Ethylenediaminetetraacetic acid</subject><subject>Gene Expression</subject><subject>Genes</subject><subject>Geochemistry</subject><subject>Humans</subject><subject>Hydrolases</subject><subject>Hydrolases - genetics</subject><subject>Hydrolases - metabolism</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Optimization</subject><subject>Original Paper</subject><subject>Phosphate esters</subject><subject>Phthalates</subject><subject>Phylogeny</subject><subject>Plastics industry</subject><subject>Recombinant</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Sewage - chemistry</subject><subject>Soil Science & Conservation</subject><subject>Strain</subject><subject>Terrestrial Pollution</subject><subject>Waste Management/Waste Technology</subject><subject>Waste Water Technology</subject><subject>Water Management</subject><subject>Water Pollutants, Chemical - metabolism</subject><subject>Water Pollution Control</subject><issn>0923-9820</issn><issn>1572-9729</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><recordid>eNqNkl-LFSEYxoco2rNbH6CbELrpxpN_ZnS83A7VBgvd1LU46pzjMqOTOsTs1-gLp5wtIggWL8TX3_O8r_g0zSuM9hgh_i5h1FECEe6g4KSD7Emzwx0n9SSeNjskCIWiJ-iiuUzpDiEkOCLPmwvScU4p5bvm53sXjD1GZVR2wYMwAuWB9Sbo6LyFxqW4Ltn5I9AnOzutJmAc9HBY8zaB5ZRPalLZgmED3v6YNuBSqAUDDmq2k5uDVwmkZV98TTG-3-bSSYMlhsXG7GyqPV1O4LSZWKTJvmiejWpK9uXDftV8-_jh6-EG3n759PlwfQs1wzRD1WqqmRgII4ToQetWtFYpw3pGMRFsYAwNqhPYYNFrzM3YGaUwIhXs1Uivmrdn3zLL99WmLGeXtJ0m5W1Yk8Ss73rMKcePQVHb9j1vH4FyTJAQbUXf_IPehTX68uZCMdFxgVHtvT9TRzVZ6fwYclS6LFP_I3g7ulK_Lq7l0aSrtvgs0DGkFO0ol-hmFTeJkazBkefgyBIcWYMjWdG8fhhlHWZr_ih-J6UA5AykcuWPNv41639dfwH3es7O</recordid><startdate>20150401</startdate><enddate>20150401</enddate><creator>Chen, Xu</creator><creator>Zhang, Xiaolong</creator><creator>Yang, Yu</creator><creator>Yue, Dongmei</creator><creator>Xiao, Lin</creator><creator>Yang, Liuyan</creator><general>Springer Netherlands</general><general>Springer</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7ST</scope><scope>7T7</scope><scope>7UA</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H97</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L.G</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>SOI</scope><scope>7X8</scope><scope>7QO</scope><scope>KR7</scope></search><sort><creationdate>20150401</creationdate><title>Biodegradation of an endocrine-disrupting chemical di-n-butyl phthalate by newly isolated Camelimonas sp. and enzymatic properties of its hydrolase</title><author>Chen, Xu ; Zhang, Xiaolong ; Yang, Yu ; Yue, Dongmei ; Xiao, Lin ; Yang, Liuyan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c613t-a4c3c69b26222cbcc494eaad68631296b660ba591d198c17df5daa102c4948af3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Aerobiosis</topic><topic>Alphaproteobacteria - chemistry</topic><topic>Alphaproteobacteria - enzymology</topic><topic>Amino Acid Sequence</topic><topic>Analysis</topic><topic>Aquatic Pollution</topic><topic>Bacteria</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biodegradation</topic><topic>Biodegradation, Environmental</topic><topic>Biomedical and Life Sciences</topic><topic>Brucella</topic><topic>Cloning, Molecular</topic><topic>Degradation</topic><topic>Dibutyl Phthalate - metabolism</topic><topic>Dimethyl</topic><topic>Endocrine Disruptors - metabolism</topic><topic>Enzymes</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Esters</topic><topic>Ethylenediaminetetraacetic acid</topic><topic>Gene Expression</topic><topic>Genes</topic><topic>Geochemistry</topic><topic>Humans</topic><topic>Hydrolases</topic><topic>Hydrolases - genetics</topic><topic>Hydrolases - metabolism</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Optimization</topic><topic>Original Paper</topic><topic>Phosphate esters</topic><topic>Phthalates</topic><topic>Phylogeny</topic><topic>Plastics industry</topic><topic>Recombinant</topic><topic>Recombinant Proteins - 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Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Civil Engineering Abstracts</collection><jtitle>Biodegradation (Dordrecht)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Xu</au><au>Zhang, Xiaolong</au><au>Yang, Yu</au><au>Yue, Dongmei</au><au>Xiao, Lin</au><au>Yang, Liuyan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biodegradation of an endocrine-disrupting chemical di-n-butyl phthalate by newly isolated Camelimonas sp. and enzymatic properties of its hydrolase</atitle><jtitle>Biodegradation (Dordrecht)</jtitle><stitle>Biodegradation</stitle><addtitle>Biodegradation</addtitle><date>2015-04-01</date><risdate>2015</risdate><volume>26</volume><issue>2</issue><spage>171</spage><epage>182</epage><pages>171-182</pages><issn>0923-9820</issn><eissn>1572-9729</eissn><abstract>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.</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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