Identification and characterization of a novel carboxylesterase from Phaseolus vulgaris for detection of organophosphate and carbamates pesticides
BACKGROUND Organophosphate and carbamate pesticide residues in food and the environment pose a great threat to human health and have made the easy and rapid detection of these pesticide residues an important task. Discovering new enzyme sources from plants can help reduce the cost of large‐scale app...
Gespeichert in:
| Veröffentlicht in: | Journal of the science of food and agriculture 2018-10, Vol.98 (13), p.5095-5104 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 5104 |
|---|---|
| container_issue | 13 |
| container_start_page | 5095 |
| container_title | Journal of the science of food and agriculture |
| container_volume | 98 |
| creator | Yang, Xiao Dai, Juan Zhao, Sujuan Li, Rong Goulette, Tim Chen, Xianggui Xiao, Hang |
| description | BACKGROUND
Organophosphate and carbamate pesticide residues in food and the environment pose a great threat to human health and have made the easy and rapid detection of these pesticide residues an important task. Discovering new enzyme sources from plants can help reduce the cost of large‐scale applications of rapid pesticide detection via enzyme inhibition.
RESULTS
Plant esterase from kidney beans was purified. Kidney bean esterase is identified as a carboxylesterase by substrate and inhibitor specificity tests and mass spectrometry identification. The kidney bean esterase demonstrates optimal catalytic activity at 40 °C, pH 6.5 and an enzyme concentration of 0.30 µg mL−1. The kidney bean esterase can be inhibited by organophosphate and carbamate pesticides, which can be substituted for acetylcholinesterase. The limit of detection of the purified kidney bean esterase was two‐ to 20‐fold higher than that of the crude one. The method detection limit meets the detection requirement for the maximum residue limits (MRL) in actual samples.
CONCLUSION
The findings of the present study provide a new source of enzymes for pesticides detection by enzyme inhibition. © 2018 Society of Chemical Industry |
| doi_str_mv | 10.1002/jsfa.9048 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_2097383610</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2097383610</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3538-c400b8acbc6b0666748b025268dc7fe8e64e3206c1d3ab6013a4e8c1b8a2d1723</originalsourceid><addsrcrecordid>eNp1kM1O4zAURi3EaCgwC14AWWLFInDtpK6zRIhfIc1IM6yjG-eGukrjYCdAeQyeGJe07GZl-97j80kfY0cCzgSAPF-EGs9yyPQOmwjIZwmAgF02iTuZTEUm99h-CAsAyHOlfrI9mSvIQE8n7OOuora3tTXYW9dybCtu5ujR9OTt-zh0NUfeuhdquEFfurdVQyHuMRCvvVvyP_N4dc0Q-MvQPKG3gdfO84p6MluD80_Yum7uQjfHnsakaMNlfAXeRaM1tqJwyH7U2AT6tTkP2OP11b_L2-Th983d5cVDYtJpqhOTAZQaTWlUCUqpWaZLkFOpdGVmNWlSGaUSlBFViqUCkWJG2oj4R1ZiJtMDdjJ6O--ehxhfLNzg2xhZyFhiqlMlIFKnI2W8C8FTXXTeLtGvCgHFuv1i3X6xbj-yxxvjUC6p-ia3dUfgfARebUOr_5uK-7_XF1_KT2Kfkr0</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2097383610</pqid></control><display><type>article</type><title>Identification and characterization of a novel carboxylesterase from Phaseolus vulgaris for detection of organophosphate and carbamates pesticides</title><source>Wiley Online Library Journals Frontfile Complete</source><creator>Yang, Xiao ; Dai, Juan ; Zhao, Sujuan ; Li, Rong ; Goulette, Tim ; Chen, Xianggui ; Xiao, Hang</creator><creatorcontrib>Yang, Xiao ; Dai, Juan ; Zhao, Sujuan ; Li, Rong ; Goulette, Tim ; Chen, Xianggui ; Xiao, Hang</creatorcontrib><description>BACKGROUND
Organophosphate and carbamate pesticide residues in food and the environment pose a great threat to human health and have made the easy and rapid detection of these pesticide residues an important task. Discovering new enzyme sources from plants can help reduce the cost of large‐scale applications of rapid pesticide detection via enzyme inhibition.
RESULTS
Plant esterase from kidney beans was purified. Kidney bean esterase is identified as a carboxylesterase by substrate and inhibitor specificity tests and mass spectrometry identification. The kidney bean esterase demonstrates optimal catalytic activity at 40 °C, pH 6.5 and an enzyme concentration of 0.30 µg mL−1. The kidney bean esterase can be inhibited by organophosphate and carbamate pesticides, which can be substituted for acetylcholinesterase. The limit of detection of the purified kidney bean esterase was two‐ to 20‐fold higher than that of the crude one. The method detection limit meets the detection requirement for the maximum residue limits (MRL) in actual samples.
CONCLUSION
The findings of the present study provide a new source of enzymes for pesticides detection by enzyme inhibition. © 2018 Society of Chemical Industry</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.9048</identifier><identifier>PMID: 29604085</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Acetylcholinesterase ; Beans ; Carbamate pesticides ; Carbamates (tradename) ; Carboxylesterase ; Catalysis ; Catalytic activity ; enzyme inhibition‐based detection ; Enzymes ; Esterase ; Health risks ; kidney bean esterase ; Kidney beans ; Mass spectrometry ; Mass spectroscopy ; Organic chemistry ; organophosphate and carbamate pesticide ; Organophosphates ; Pesticide residues ; Pesticides ; Phaseolus vulgaris ; Residues ; Substrate inhibition</subject><ispartof>Journal of the science of food and agriculture, 2018-10, Vol.98 (13), p.5095-5104</ispartof><rights>2018 Society of Chemical Industry</rights><rights>2018 Society of Chemical Industry.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3538-c400b8acbc6b0666748b025268dc7fe8e64e3206c1d3ab6013a4e8c1b8a2d1723</citedby><cites>FETCH-LOGICAL-c3538-c400b8acbc6b0666748b025268dc7fe8e64e3206c1d3ab6013a4e8c1b8a2d1723</cites><orcidid>0000-0001-6194-2796 ; 0000-0001-7968-7260</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjsfa.9048$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.9048$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29604085$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Xiao</creatorcontrib><creatorcontrib>Dai, Juan</creatorcontrib><creatorcontrib>Zhao, Sujuan</creatorcontrib><creatorcontrib>Li, Rong</creatorcontrib><creatorcontrib>Goulette, Tim</creatorcontrib><creatorcontrib>Chen, Xianggui</creatorcontrib><creatorcontrib>Xiao, Hang</creatorcontrib><title>Identification and characterization of a novel carboxylesterase from Phaseolus vulgaris for detection of organophosphate and carbamates pesticides</title><title>Journal of the science of food and agriculture</title><addtitle>J Sci Food Agric</addtitle><description>BACKGROUND
Organophosphate and carbamate pesticide residues in food and the environment pose a great threat to human health and have made the easy and rapid detection of these pesticide residues an important task. Discovering new enzyme sources from plants can help reduce the cost of large‐scale applications of rapid pesticide detection via enzyme inhibition.
RESULTS
Plant esterase from kidney beans was purified. Kidney bean esterase is identified as a carboxylesterase by substrate and inhibitor specificity tests and mass spectrometry identification. The kidney bean esterase demonstrates optimal catalytic activity at 40 °C, pH 6.5 and an enzyme concentration of 0.30 µg mL−1. The kidney bean esterase can be inhibited by organophosphate and carbamate pesticides, which can be substituted for acetylcholinesterase. The limit of detection of the purified kidney bean esterase was two‐ to 20‐fold higher than that of the crude one. The method detection limit meets the detection requirement for the maximum residue limits (MRL) in actual samples.
CONCLUSION
The findings of the present study provide a new source of enzymes for pesticides detection by enzyme inhibition. © 2018 Society of Chemical Industry</description><subject>Acetylcholinesterase</subject><subject>Beans</subject><subject>Carbamate pesticides</subject><subject>Carbamates (tradename)</subject><subject>Carboxylesterase</subject><subject>Catalysis</subject><subject>Catalytic activity</subject><subject>enzyme inhibition‐based detection</subject><subject>Enzymes</subject><subject>Esterase</subject><subject>Health risks</subject><subject>kidney bean esterase</subject><subject>Kidney beans</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Organic chemistry</subject><subject>organophosphate and carbamate pesticide</subject><subject>Organophosphates</subject><subject>Pesticide residues</subject><subject>Pesticides</subject><subject>Phaseolus vulgaris</subject><subject>Residues</subject><subject>Substrate inhibition</subject><issn>0022-5142</issn><issn>1097-0010</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNp1kM1O4zAURi3EaCgwC14AWWLFInDtpK6zRIhfIc1IM6yjG-eGukrjYCdAeQyeGJe07GZl-97j80kfY0cCzgSAPF-EGs9yyPQOmwjIZwmAgF02iTuZTEUm99h-CAsAyHOlfrI9mSvIQE8n7OOuora3tTXYW9dybCtu5ujR9OTt-zh0NUfeuhdquEFfurdVQyHuMRCvvVvyP_N4dc0Q-MvQPKG3gdfO84p6MluD80_Yum7uQjfHnsakaMNlfAXeRaM1tqJwyH7U2AT6tTkP2OP11b_L2-Th983d5cVDYtJpqhOTAZQaTWlUCUqpWaZLkFOpdGVmNWlSGaUSlBFViqUCkWJG2oj4R1ZiJtMDdjJ6O--ehxhfLNzg2xhZyFhiqlMlIFKnI2W8C8FTXXTeLtGvCgHFuv1i3X6xbj-yxxvjUC6p-ia3dUfgfARebUOr_5uK-7_XF1_KT2Kfkr0</recordid><startdate>201810</startdate><enddate>201810</enddate><creator>Yang, Xiao</creator><creator>Dai, Juan</creator><creator>Zhao, Sujuan</creator><creator>Li, Rong</creator><creator>Goulette, Tim</creator><creator>Chen, Xianggui</creator><creator>Xiao, Hang</creator><general>John Wiley & Sons, Ltd</general><general>John Wiley and Sons, Limited</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QL</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7T5</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>SOI</scope><orcidid>https://orcid.org/0000-0001-6194-2796</orcidid><orcidid>https://orcid.org/0000-0001-7968-7260</orcidid></search><sort><creationdate>201810</creationdate><title>Identification and characterization of a novel carboxylesterase from Phaseolus vulgaris for detection of organophosphate and carbamates pesticides</title><author>Yang, Xiao ; Dai, Juan ; Zhao, Sujuan ; Li, Rong ; Goulette, Tim ; Chen, Xianggui ; Xiao, Hang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3538-c400b8acbc6b0666748b025268dc7fe8e64e3206c1d3ab6013a4e8c1b8a2d1723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Acetylcholinesterase</topic><topic>Beans</topic><topic>Carbamate pesticides</topic><topic>Carbamates (tradename)</topic><topic>Carboxylesterase</topic><topic>Catalysis</topic><topic>Catalytic activity</topic><topic>enzyme inhibition‐based detection</topic><topic>Enzymes</topic><topic>Esterase</topic><topic>Health risks</topic><topic>kidney bean esterase</topic><topic>Kidney beans</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Organic chemistry</topic><topic>organophosphate and carbamate pesticide</topic><topic>Organophosphates</topic><topic>Pesticide residues</topic><topic>Pesticides</topic><topic>Phaseolus vulgaris</topic><topic>Residues</topic><topic>Substrate inhibition</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, Xiao</creatorcontrib><creatorcontrib>Dai, Juan</creatorcontrib><creatorcontrib>Zhao, Sujuan</creatorcontrib><creatorcontrib>Li, Rong</creatorcontrib><creatorcontrib>Goulette, Tim</creatorcontrib><creatorcontrib>Chen, Xianggui</creatorcontrib><creatorcontrib>Xiao, Hang</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><jtitle>Journal of the science of food and agriculture</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yang, Xiao</au><au>Dai, Juan</au><au>Zhao, Sujuan</au><au>Li, Rong</au><au>Goulette, Tim</au><au>Chen, Xianggui</au><au>Xiao, Hang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and characterization of a novel carboxylesterase from Phaseolus vulgaris for detection of organophosphate and carbamates pesticides</atitle><jtitle>Journal of the science of food and agriculture</jtitle><addtitle>J Sci Food Agric</addtitle><date>2018-10</date><risdate>2018</risdate><volume>98</volume><issue>13</issue><spage>5095</spage><epage>5104</epage><pages>5095-5104</pages><issn>0022-5142</issn><eissn>1097-0010</eissn><abstract>BACKGROUND
Organophosphate and carbamate pesticide residues in food and the environment pose a great threat to human health and have made the easy and rapid detection of these pesticide residues an important task. Discovering new enzyme sources from plants can help reduce the cost of large‐scale applications of rapid pesticide detection via enzyme inhibition.
RESULTS
Plant esterase from kidney beans was purified. Kidney bean esterase is identified as a carboxylesterase by substrate and inhibitor specificity tests and mass spectrometry identification. The kidney bean esterase demonstrates optimal catalytic activity at 40 °C, pH 6.5 and an enzyme concentration of 0.30 µg mL−1. The kidney bean esterase can be inhibited by organophosphate and carbamate pesticides, which can be substituted for acetylcholinesterase. The limit of detection of the purified kidney bean esterase was two‐ to 20‐fold higher than that of the crude one. The method detection limit meets the detection requirement for the maximum residue limits (MRL) in actual samples.
CONCLUSION
The findings of the present study provide a new source of enzymes for pesticides detection by enzyme inhibition. © 2018 Society of Chemical Industry</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>29604085</pmid><doi>10.1002/jsfa.9048</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-6194-2796</orcidid><orcidid>https://orcid.org/0000-0001-7968-7260</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-5142 |
| ispartof | Journal of the science of food and agriculture, 2018-10, Vol.98 (13), p.5095-5104 |
| issn | 0022-5142 1097-0010 |
| language | eng |
| recordid | cdi_proquest_journals_2097383610 |
| source | Wiley Online Library Journals Frontfile Complete |
| subjects | Acetylcholinesterase Beans Carbamate pesticides Carbamates (tradename) Carboxylesterase Catalysis Catalytic activity enzyme inhibition‐based detection Enzymes Esterase Health risks kidney bean esterase Kidney beans Mass spectrometry Mass spectroscopy Organic chemistry organophosphate and carbamate pesticide Organophosphates Pesticide residues Pesticides Phaseolus vulgaris Residues Substrate inhibition |
| title | Identification and characterization of a novel carboxylesterase from Phaseolus vulgaris for detection of organophosphate and carbamates pesticides |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-26T22%3A22%3A36IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20and%20characterization%20of%20a%20novel%20carboxylesterase%20from%20Phaseolus%20vulgaris%20for%20detection%20of%20organophosphate%20and%20carbamates%20pesticides&rft.jtitle=Journal%20of%20the%20science%20of%20food%20and%20agriculture&rft.au=Yang,%20Xiao&rft.date=2018-10&rft.volume=98&rft.issue=13&rft.spage=5095&rft.epage=5104&rft.pages=5095-5104&rft.issn=0022-5142&rft.eissn=1097-0010&rft_id=info:doi/10.1002/jsfa.9048&rft_dat=%3Cproquest_cross%3E2097383610%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2097383610&rft_id=info:pmid/29604085&rfr_iscdi=true |