Detection of insecticides by Tetronarce californica acetylcholinesterase via expression and in silico analysis
The acetylcholinesterase (AChE) is involved in termination of synaptic transmission at cholinergic synapses and plays a vital role in the insecticide detection and inhibitor screening. Here, we report the heterologous expression of an AChE from Tetronarce californica ( Tc A) in Escherichia coli ( E....
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| Veröffentlicht in: | Applied microbiology and biotechnology 2023-12, Vol.107 (24), p.7657-7671 |
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| creator | Jiang, Shuoqi Gu, Qiuya Yu, Xiaobin |
| description | The acetylcholinesterase (AChE) is involved in termination of synaptic transmission at cholinergic synapses and plays a vital role in the insecticide detection and inhibitor screening. Here, we report the heterologous expression of an AChE from
Tetronarce californica
(
Tc
A) in
Escherichia coli
(
E. coli
) as a soluble active protein.
Tc
A was immobilized in calcium alginate beads; the morphology, biochemical properties, and insecticide detection performance of free and immobilized
Tc
A were characterized. Moreover, we used sequence, structure-based approaches, and molecular docking to investigate structural and functional characterization of
Tc
A. The results showed that
Tc
A exhibited a specific activity of 102 U/mg, with optimal activity at pH 8.0 and 30 °C. Immobilized
Tc
A demonstrated superior thermal stability, pH stability, and storage stability compared to the free enzyme. The highest sensitivity of free
Tc
A was observed with trichlorfon, whereas immobilized
Tc
A showed reduced IC
50
values towards tested insecticides by 3 to 180-fold. Molecular docking analysis revealed the interaction of trichlorfon, acephate, isoprocarb, λ-cyhalothrin, and fenpropathrin in the active site gorge of
Tc
A, particularly mediated through the formation of hydrogen bonds and
π
-
π
stacking. Therefore,
Tc
A expressed heterologously in
E. coli
is a promising candidate for applications in food safety and environmental analysis.
Key points
• T. californica AChE was expressed solubly in prokaryotic system.
• The biochemical properties of free/immobilized enzyme were characterized.
• The sensitivity of enzyme to insecticides was evaluated in vitro and in silico.
Graphical Abstract |
| doi_str_mv | 10.1007/s00253-023-12780-1 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_3153557541</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A773284259</galeid><sourcerecordid>A773284259</sourcerecordid><originalsourceid>FETCH-LOGICAL-c437t-d6d19e1347217961d4c2e8bba51d2aba414a6f16d57a34c7c0d5452177071ac83</originalsourceid><addsrcrecordid>eNqFkluLFDEQhRtRcFz9Az41-KIPvaZy6XQ_LuttYUHQ9TnUpKvHLD3JmOpZdv69aUdYRkRJIFT4zqGqOFX1EsQ5CGHfshDSqEZI1YC0nWjgUbUCrWQjWtCPq5UAaxpr-u5p9Yz5VgiQXduuqviOZvJzSLFOYx0iL4UPA3G9PtQ3NOcUMXuqPU5hTDkGjzV6mg-T_56mEIlnyshU3wWs6X6XiXlxwzgUu5rDFHwqFU4HDvy8ejLixPTi93tWffvw_ubyU3P9-ePV5cV147WyczO0A_QESlsJtm9h0F5St16jgUHiGjVobEdoB2NRaW-9GIw2hbXCAvpOnVWvj767nH7sS49uG9jTNGGktGenwChjrNHwX1R21qquN1oW9NUf6G3a5zLaQvUgyhX6gdrgRC7EMc0Z_WLqLoqV7LQ0faHO_0KVM9C2bCzSGMr_ieDNiaAwM93PG9wzu6uvX05ZeWR9TsyZRrfLYYv54EC4JTDuGBhXAuN-BcYti1BHERc4big_TPcP1U_fv8Ez</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2891091004</pqid></control><display><type>article</type><title>Detection of insecticides by Tetronarce californica acetylcholinesterase via expression and in silico analysis</title><source>SpringerLink Journals</source><creator>Jiang, Shuoqi ; Gu, Qiuya ; Yu, Xiaobin</creator><creatorcontrib>Jiang, Shuoqi ; Gu, Qiuya ; Yu, Xiaobin</creatorcontrib><description>The acetylcholinesterase (AChE) is involved in termination of synaptic transmission at cholinergic synapses and plays a vital role in the insecticide detection and inhibitor screening. Here, we report the heterologous expression of an AChE from
Tetronarce californica
(
Tc
A) in
Escherichia coli
(
E. coli
) as a soluble active protein.
Tc
A was immobilized in calcium alginate beads; the morphology, biochemical properties, and insecticide detection performance of free and immobilized
Tc
A were characterized. Moreover, we used sequence, structure-based approaches, and molecular docking to investigate structural and functional characterization of
Tc
A. The results showed that
Tc
A exhibited a specific activity of 102 U/mg, with optimal activity at pH 8.0 and 30 °C. Immobilized
Tc
A demonstrated superior thermal stability, pH stability, and storage stability compared to the free enzyme. The highest sensitivity of free
Tc
A was observed with trichlorfon, whereas immobilized
Tc
A showed reduced IC
50
values towards tested insecticides by 3 to 180-fold. Molecular docking analysis revealed the interaction of trichlorfon, acephate, isoprocarb, λ-cyhalothrin, and fenpropathrin in the active site gorge of
Tc
A, particularly mediated through the formation of hydrogen bonds and
π
-
π
stacking. Therefore,
Tc
A expressed heterologously in
E. coli
is a promising candidate for applications in food safety and environmental analysis.
Key points
• T. californica AChE was expressed solubly in prokaryotic system.
• The biochemical properties of free/immobilized enzyme were characterized.
• The sensitivity of enzyme to insecticides was evaluated in vitro and in silico.
Graphical Abstract</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-023-12780-1</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>acephate ; Acetylcholinesterase ; active sites ; Alginic acid ; Biomedical and Life Sciences ; Biotechnology ; Calcium alginate ; Cholinergics ; computer simulation ; Cyhalothrin ; E coli ; environmental assessment ; Environmental Biotechnology ; Enzymes ; Escherichia coli ; fenpropathrin ; Food safety ; heterologous gene expression ; hydrogen ; Hydrogen bonding ; Hydrogen bonds ; Identification and classification ; immobilized enzymes ; Insecticides ; Life Sciences ; Microbial Genetics and Genomics ; Microbiology ; Molecular docking ; Molecular structure ; Organophosphorus pesticides ; pH stability ; Properties ; storage quality ; Storage stability ; Structural analysis ; Structure-function relationships ; Synapses ; Synaptic transmission ; Tetronarce californica ; Thermal stability ; trichlorfon</subject><ispartof>Applied microbiology and biotechnology, 2023-12, Vol.107 (24), p.7657-7671</ispartof><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>COPYRIGHT 2023 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c437t-d6d19e1347217961d4c2e8bba51d2aba414a6f16d57a34c7c0d5452177071ac83</cites><orcidid>0000-0002-3958-6067</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-023-12780-1$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-023-12780-1$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids></links><search><creatorcontrib>Jiang, Shuoqi</creatorcontrib><creatorcontrib>Gu, Qiuya</creatorcontrib><creatorcontrib>Yu, Xiaobin</creatorcontrib><title>Detection of insecticides by Tetronarce californica acetylcholinesterase via expression and in silico analysis</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><description>The acetylcholinesterase (AChE) is involved in termination of synaptic transmission at cholinergic synapses and plays a vital role in the insecticide detection and inhibitor screening. Here, we report the heterologous expression of an AChE from
Tetronarce californica
(
Tc
A) in
Escherichia coli
(
E. coli
) as a soluble active protein.
Tc
A was immobilized in calcium alginate beads; the morphology, biochemical properties, and insecticide detection performance of free and immobilized
Tc
A were characterized. Moreover, we used sequence, structure-based approaches, and molecular docking to investigate structural and functional characterization of
Tc
A. The results showed that
Tc
A exhibited a specific activity of 102 U/mg, with optimal activity at pH 8.0 and 30 °C. Immobilized
Tc
A demonstrated superior thermal stability, pH stability, and storage stability compared to the free enzyme. The highest sensitivity of free
Tc
A was observed with trichlorfon, whereas immobilized
Tc
A showed reduced IC
50
values towards tested insecticides by 3 to 180-fold. Molecular docking analysis revealed the interaction of trichlorfon, acephate, isoprocarb, λ-cyhalothrin, and fenpropathrin in the active site gorge of
Tc
A, particularly mediated through the formation of hydrogen bonds and
π
-
π
stacking. Therefore,
Tc
A expressed heterologously in
E. coli
is a promising candidate for applications in food safety and environmental analysis.
Key points
• T. californica AChE was expressed solubly in prokaryotic system.
• The biochemical properties of free/immobilized enzyme were characterized.
• The sensitivity of enzyme to insecticides was evaluated in vitro and in silico.
Graphical Abstract</description><subject>acephate</subject><subject>Acetylcholinesterase</subject><subject>active sites</subject><subject>Alginic acid</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Calcium alginate</subject><subject>Cholinergics</subject><subject>computer simulation</subject><subject>Cyhalothrin</subject><subject>E coli</subject><subject>environmental assessment</subject><subject>Environmental Biotechnology</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>fenpropathrin</subject><subject>Food safety</subject><subject>heterologous gene expression</subject><subject>hydrogen</subject><subject>Hydrogen bonding</subject><subject>Hydrogen bonds</subject><subject>Identification and classification</subject><subject>immobilized enzymes</subject><subject>Insecticides</subject><subject>Life Sciences</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Molecular docking</subject><subject>Molecular structure</subject><subject>Organophosphorus pesticides</subject><subject>pH stability</subject><subject>Properties</subject><subject>storage quality</subject><subject>Storage stability</subject><subject>Structural analysis</subject><subject>Structure-function relationships</subject><subject>Synapses</subject><subject>Synaptic transmission</subject><subject>Tetronarce californica</subject><subject>Thermal stability</subject><subject>trichlorfon</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNqFkluLFDEQhRtRcFz9Az41-KIPvaZy6XQ_LuttYUHQ9TnUpKvHLD3JmOpZdv69aUdYRkRJIFT4zqGqOFX1EsQ5CGHfshDSqEZI1YC0nWjgUbUCrWQjWtCPq5UAaxpr-u5p9Yz5VgiQXduuqviOZvJzSLFOYx0iL4UPA3G9PtQ3NOcUMXuqPU5hTDkGjzV6mg-T_56mEIlnyshU3wWs6X6XiXlxwzgUu5rDFHwqFU4HDvy8ejLixPTi93tWffvw_ubyU3P9-ePV5cV147WyczO0A_QESlsJtm9h0F5St16jgUHiGjVobEdoB2NRaW-9GIw2hbXCAvpOnVWvj767nH7sS49uG9jTNGGktGenwChjrNHwX1R21qquN1oW9NUf6G3a5zLaQvUgyhX6gdrgRC7EMc0Z_WLqLoqV7LQ0faHO_0KVM9C2bCzSGMr_ieDNiaAwM93PG9wzu6uvX05ZeWR9TsyZRrfLYYv54EC4JTDuGBhXAuN-BcYti1BHERc4big_TPcP1U_fv8Ez</recordid><startdate>20231201</startdate><enddate>20231201</enddate><creator>Jiang, Shuoqi</creator><creator>Gu, Qiuya</creator><creator>Yu, Xiaobin</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature 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of insecticides by Tetronarce californica acetylcholinesterase via expression and in silico analysis</title><author>Jiang, Shuoqi ; Gu, Qiuya ; Yu, Xiaobin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c437t-d6d19e1347217961d4c2e8bba51d2aba414a6f16d57a34c7c0d5452177071ac83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>acephate</topic><topic>Acetylcholinesterase</topic><topic>active sites</topic><topic>Alginic acid</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Calcium alginate</topic><topic>Cholinergics</topic><topic>computer simulation</topic><topic>Cyhalothrin</topic><topic>E coli</topic><topic>environmental assessment</topic><topic>Environmental Biotechnology</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>fenpropathrin</topic><topic>Food safety</topic><topic>heterologous gene expression</topic><topic>hydrogen</topic><topic>Hydrogen bonding</topic><topic>Hydrogen bonds</topic><topic>Identification and classification</topic><topic>immobilized enzymes</topic><topic>Insecticides</topic><topic>Life Sciences</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Molecular docking</topic><topic>Molecular structure</topic><topic>Organophosphorus pesticides</topic><topic>pH stability</topic><topic>Properties</topic><topic>storage quality</topic><topic>Storage stability</topic><topic>Structural analysis</topic><topic>Structure-function relationships</topic><topic>Synapses</topic><topic>Synaptic transmission</topic><topic>Tetronarce californica</topic><topic>Thermal stability</topic><topic>trichlorfon</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jiang, Shuoqi</creatorcontrib><creatorcontrib>Gu, Qiuya</creatorcontrib><creatorcontrib>Yu, Xiaobin</creatorcontrib><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>ABI/INFORM Collection</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital 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Biotechnol</stitle><date>2023-12-01</date><risdate>2023</risdate><volume>107</volume><issue>24</issue><spage>7657</spage><epage>7671</epage><pages>7657-7671</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>The acetylcholinesterase (AChE) is involved in termination of synaptic transmission at cholinergic synapses and plays a vital role in the insecticide detection and inhibitor screening. Here, we report the heterologous expression of an AChE from
Tetronarce californica
(
Tc
A) in
Escherichia coli
(
E. coli
) as a soluble active protein.
Tc
A was immobilized in calcium alginate beads; the morphology, biochemical properties, and insecticide detection performance of free and immobilized
Tc
A were characterized. Moreover, we used sequence, structure-based approaches, and molecular docking to investigate structural and functional characterization of
Tc
A. The results showed that
Tc
A exhibited a specific activity of 102 U/mg, with optimal activity at pH 8.0 and 30 °C. Immobilized
Tc
A demonstrated superior thermal stability, pH stability, and storage stability compared to the free enzyme. The highest sensitivity of free
Tc
A was observed with trichlorfon, whereas immobilized
Tc
A showed reduced IC
50
values towards tested insecticides by 3 to 180-fold. Molecular docking analysis revealed the interaction of trichlorfon, acephate, isoprocarb, λ-cyhalothrin, and fenpropathrin in the active site gorge of
Tc
A, particularly mediated through the formation of hydrogen bonds and
π
-
π
stacking. Therefore,
Tc
A expressed heterologously in
E. coli
is a promising candidate for applications in food safety and environmental analysis.
Key points
• T. californica AChE was expressed solubly in prokaryotic system.
• The biochemical properties of free/immobilized enzyme were characterized.
• The sensitivity of enzyme to insecticides was evaluated in vitro and in silico.
Graphical Abstract</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><doi>10.1007/s00253-023-12780-1</doi><tpages>15</tpages><orcidid>https://orcid.org/0000-0002-3958-6067</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0175-7598 |
| ispartof | Applied microbiology and biotechnology, 2023-12, Vol.107 (24), p.7657-7671 |
| issn | 0175-7598 1432-0614 |
| language | eng |
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| source | SpringerLink Journals |
| subjects | acephate Acetylcholinesterase active sites Alginic acid Biomedical and Life Sciences Biotechnology Calcium alginate Cholinergics computer simulation Cyhalothrin E coli environmental assessment Environmental Biotechnology Enzymes Escherichia coli fenpropathrin Food safety heterologous gene expression hydrogen Hydrogen bonding Hydrogen bonds Identification and classification immobilized enzymes Insecticides Life Sciences Microbial Genetics and Genomics Microbiology Molecular docking Molecular structure Organophosphorus pesticides pH stability Properties storage quality Storage stability Structural analysis Structure-function relationships Synapses Synaptic transmission Tetronarce californica Thermal stability trichlorfon |
| title | Detection of insecticides by Tetronarce californica acetylcholinesterase via expression and in silico analysis |
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