Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system

Enzyme assays can be performed with the capillary electrophoresis technique (CE) in many approaches, such as the immobilized enzyme micro-reactor. Acetylcholinesterase is a promising enzyme to be used when pursuing such a method, as it has already been explored in the proposal of similar methods of...
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Autor*in:	Siebert, Diogo Alexandre [verfasserIn] Caon, Natália Bruzamarello [verfasserIn] Alberton, Michele Debiasi [verfasserIn] Vitali, Luciano [verfasserIn] Parize, Alexandre Luis [verfasserIn] Micke, Gustavo Amadeu [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	Magnetic nanoparticles Immobilized enzyme microreactor Acetylcholinesterase

Übergeordnetes Werk:	Enthalten in: Analytica chimica acta - Amsterdam : Elsevier Science, 1947, 1275
Übergeordnetes Werk:	volume:1275

DOI / URN:	10.1016/j.aca.2023.341566

Katalog-ID:	ELV061007269

Internformat


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100	1		\|a Siebert, Diogo Alexandre \|e verfasserin \|4 aut
245	1	0	\|a Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system
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520			\|a Enzyme assays can be performed with the capillary electrophoresis technique (CE) in many approaches, such as the immobilized enzyme micro-reactor. Acetylcholinesterase is a promising enzyme to be used when pursuing such a method, as it has already been explored in the proposal of similar methods of miniaturizing enzyme assays. The present work proposes a novel enzyme micro-reactor, based on the anchorage of the enzyme on magnetic nanoparticles of MnFe2O4, with chitosan and glutaraldehyde as the cross-linker in the capillary by means of an arrange of neodymium magnets. The calculated K m of the enzyme evaluated by this method was 1.12 mmol L−1, comparable to other studies in the literature that utilizes immobilized enzymes. Also, IC50 for neostigmine was assessed in 3 different micro-reactors, with an average of 29.42 ± 3.88 μmol L−1. In terms of the micro-reactor stability, it was possible to perform at least 25 experiments with assembled micro-reactor. The method was applied to hydroalcoholic extracts of 7 plant species. Plinia cauliflora had the best result, with 42.31 ± 6.81% of enzyme inhibition in a concentration of 100 mg L−1.
650		4	\|a Magnetic nanoparticles
650		4	\|a Immobilized enzyme microreactor
650		4	\|a Acetylcholinesterase
700	1		\|a Caon, Natália Bruzamarello \|e verfasserin \|0 (orcid)0000-0003-4846-4202 \|4 aut
700	1		\|a Alberton, Michele Debiasi \|e verfasserin \|0 (orcid)0000-0003-3490-9936 \|4 aut
700	1		\|a Vitali, Luciano \|e verfasserin \|4 aut
700	1		\|a Parize, Alexandre Luis \|e verfasserin \|4 aut
700	1		\|a Micke, Gustavo Amadeu \|e verfasserin \|0 (orcid)0000-0002-5518-624X \|4 aut
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912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2088
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
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912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2470
912			\|a GBV_ILN_2507
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912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
936	b	k	\|a 35.23 \|j Analytische Chemie: Allgemeines \|q VZ
951			\|a AR
952			\|d 1275

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publishDate	2023
allfields	10.1016/j.aca.2023.341566 doi (DE-627)ELV061007269 (ELSEVIER)S0003-2670(23)00787-0 DE-627 ger DE-627 rda eng 540 VZ 35.23 bkl Siebert, Diogo Alexandre verfasserin aut Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Enzyme assays can be performed with the capillary electrophoresis technique (CE) in many approaches, such as the immobilized enzyme micro-reactor. Acetylcholinesterase is a promising enzyme to be used when pursuing such a method, as it has already been explored in the proposal of similar methods of miniaturizing enzyme assays. The present work proposes a novel enzyme micro-reactor, based on the anchorage of the enzyme on magnetic nanoparticles of MnFe2O4, with chitosan and glutaraldehyde as the cross-linker in the capillary by means of an arrange of neodymium magnets. The calculated K m of the enzyme evaluated by this method was 1.12 mmol L−1, comparable to other studies in the literature that utilizes immobilized enzymes. Also, IC50 for neostigmine was assessed in 3 different micro-reactors, with an average of 29.42 ± 3.88 μmol L−1. In terms of the micro-reactor stability, it was possible to perform at least 25 experiments with assembled micro-reactor. The method was applied to hydroalcoholic extracts of 7 plant species. Plinia cauliflora had the best result, with 42.31 ± 6.81% of enzyme inhibition in a concentration of 100 mg L−1. Magnetic nanoparticles Immobilized enzyme microreactor Acetylcholinesterase Caon, Natália Bruzamarello verfasserin (orcid)0000-0003-4846-4202 aut Alberton, Michele Debiasi verfasserin (orcid)0000-0003-3490-9936 aut Vitali, Luciano verfasserin aut Parize, Alexandre Luis verfasserin aut Micke, Gustavo Amadeu verfasserin (orcid)0000-0002-5518-624X aut Enthalten in Analytica chimica acta Amsterdam : Elsevier Science, 1947 1275 Online-Ressource (DE-627)300896468 (DE-600)1483436-4 (DE-576)081952619 1873-4324 nnns volume:1275 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.23 Analytische Chemie: Allgemeines VZ AR 1275
spelling	10.1016/j.aca.2023.341566 doi (DE-627)ELV061007269 (ELSEVIER)S0003-2670(23)00787-0 DE-627 ger DE-627 rda eng 540 VZ 35.23 bkl Siebert, Diogo Alexandre verfasserin aut Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Enzyme assays can be performed with the capillary electrophoresis technique (CE) in many approaches, such as the immobilized enzyme micro-reactor. Acetylcholinesterase is a promising enzyme to be used when pursuing such a method, as it has already been explored in the proposal of similar methods of miniaturizing enzyme assays. The present work proposes a novel enzyme micro-reactor, based on the anchorage of the enzyme on magnetic nanoparticles of MnFe2O4, with chitosan and glutaraldehyde as the cross-linker in the capillary by means of an arrange of neodymium magnets. The calculated K m of the enzyme evaluated by this method was 1.12 mmol L−1, comparable to other studies in the literature that utilizes immobilized enzymes. Also, IC50 for neostigmine was assessed in 3 different micro-reactors, with an average of 29.42 ± 3.88 μmol L−1. In terms of the micro-reactor stability, it was possible to perform at least 25 experiments with assembled micro-reactor. The method was applied to hydroalcoholic extracts of 7 plant species. Plinia cauliflora had the best result, with 42.31 ± 6.81% of enzyme inhibition in a concentration of 100 mg L−1. Magnetic nanoparticles Immobilized enzyme microreactor Acetylcholinesterase Caon, Natália Bruzamarello verfasserin (orcid)0000-0003-4846-4202 aut Alberton, Michele Debiasi verfasserin (orcid)0000-0003-3490-9936 aut Vitali, Luciano verfasserin aut Parize, Alexandre Luis verfasserin aut Micke, Gustavo Amadeu verfasserin (orcid)0000-0002-5518-624X aut Enthalten in Analytica chimica acta Amsterdam : Elsevier Science, 1947 1275 Online-Ressource (DE-627)300896468 (DE-600)1483436-4 (DE-576)081952619 1873-4324 nnns volume:1275 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.23 Analytische Chemie: Allgemeines VZ AR 1275
allfields_unstemmed	10.1016/j.aca.2023.341566 doi (DE-627)ELV061007269 (ELSEVIER)S0003-2670(23)00787-0 DE-627 ger DE-627 rda eng 540 VZ 35.23 bkl Siebert, Diogo Alexandre verfasserin aut Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Enzyme assays can be performed with the capillary electrophoresis technique (CE) in many approaches, such as the immobilized enzyme micro-reactor. Acetylcholinesterase is a promising enzyme to be used when pursuing such a method, as it has already been explored in the proposal of similar methods of miniaturizing enzyme assays. The present work proposes a novel enzyme micro-reactor, based on the anchorage of the enzyme on magnetic nanoparticles of MnFe2O4, with chitosan and glutaraldehyde as the cross-linker in the capillary by means of an arrange of neodymium magnets. The calculated K m of the enzyme evaluated by this method was 1.12 mmol L−1, comparable to other studies in the literature that utilizes immobilized enzymes. Also, IC50 for neostigmine was assessed in 3 different micro-reactors, with an average of 29.42 ± 3.88 μmol L−1. In terms of the micro-reactor stability, it was possible to perform at least 25 experiments with assembled micro-reactor. The method was applied to hydroalcoholic extracts of 7 plant species. Plinia cauliflora had the best result, with 42.31 ± 6.81% of enzyme inhibition in a concentration of 100 mg L−1. Magnetic nanoparticles Immobilized enzyme microreactor Acetylcholinesterase Caon, Natália Bruzamarello verfasserin (orcid)0000-0003-4846-4202 aut Alberton, Michele Debiasi verfasserin (orcid)0000-0003-3490-9936 aut Vitali, Luciano verfasserin aut Parize, Alexandre Luis verfasserin aut Micke, Gustavo Amadeu verfasserin (orcid)0000-0002-5518-624X aut Enthalten in Analytica chimica acta Amsterdam : Elsevier Science, 1947 1275 Online-Ressource (DE-627)300896468 (DE-600)1483436-4 (DE-576)081952619 1873-4324 nnns volume:1275 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.23 Analytische Chemie: Allgemeines VZ AR 1275
allfieldsGer	10.1016/j.aca.2023.341566 doi (DE-627)ELV061007269 (ELSEVIER)S0003-2670(23)00787-0 DE-627 ger DE-627 rda eng 540 VZ 35.23 bkl Siebert, Diogo Alexandre verfasserin aut Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Enzyme assays can be performed with the capillary electrophoresis technique (CE) in many approaches, such as the immobilized enzyme micro-reactor. Acetylcholinesterase is a promising enzyme to be used when pursuing such a method, as it has already been explored in the proposal of similar methods of miniaturizing enzyme assays. The present work proposes a novel enzyme micro-reactor, based on the anchorage of the enzyme on magnetic nanoparticles of MnFe2O4, with chitosan and glutaraldehyde as the cross-linker in the capillary by means of an arrange of neodymium magnets. The calculated K m of the enzyme evaluated by this method was 1.12 mmol L−1, comparable to other studies in the literature that utilizes immobilized enzymes. Also, IC50 for neostigmine was assessed in 3 different micro-reactors, with an average of 29.42 ± 3.88 μmol L−1. In terms of the micro-reactor stability, it was possible to perform at least 25 experiments with assembled micro-reactor. The method was applied to hydroalcoholic extracts of 7 plant species. Plinia cauliflora had the best result, with 42.31 ± 6.81% of enzyme inhibition in a concentration of 100 mg L−1. Magnetic nanoparticles Immobilized enzyme microreactor Acetylcholinesterase Caon, Natália Bruzamarello verfasserin (orcid)0000-0003-4846-4202 aut Alberton, Michele Debiasi verfasserin (orcid)0000-0003-3490-9936 aut Vitali, Luciano verfasserin aut Parize, Alexandre Luis verfasserin aut Micke, Gustavo Amadeu verfasserin (orcid)0000-0002-5518-624X aut Enthalten in Analytica chimica acta Amsterdam : Elsevier Science, 1947 1275 Online-Ressource (DE-627)300896468 (DE-600)1483436-4 (DE-576)081952619 1873-4324 nnns volume:1275 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.23 Analytische Chemie: Allgemeines VZ AR 1275
allfieldsSound	10.1016/j.aca.2023.341566 doi (DE-627)ELV061007269 (ELSEVIER)S0003-2670(23)00787-0 DE-627 ger DE-627 rda eng 540 VZ 35.23 bkl Siebert, Diogo Alexandre verfasserin aut Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Enzyme assays can be performed with the capillary electrophoresis technique (CE) in many approaches, such as the immobilized enzyme micro-reactor. Acetylcholinesterase is a promising enzyme to be used when pursuing such a method, as it has already been explored in the proposal of similar methods of miniaturizing enzyme assays. The present work proposes a novel enzyme micro-reactor, based on the anchorage of the enzyme on magnetic nanoparticles of MnFe2O4, with chitosan and glutaraldehyde as the cross-linker in the capillary by means of an arrange of neodymium magnets. The calculated K m of the enzyme evaluated by this method was 1.12 mmol L−1, comparable to other studies in the literature that utilizes immobilized enzymes. Also, IC50 for neostigmine was assessed in 3 different micro-reactors, with an average of 29.42 ± 3.88 μmol L−1. In terms of the micro-reactor stability, it was possible to perform at least 25 experiments with assembled micro-reactor. The method was applied to hydroalcoholic extracts of 7 plant species. Plinia cauliflora had the best result, with 42.31 ± 6.81% of enzyme inhibition in a concentration of 100 mg L−1. Magnetic nanoparticles Immobilized enzyme microreactor Acetylcholinesterase Caon, Natália Bruzamarello verfasserin (orcid)0000-0003-4846-4202 aut Alberton, Michele Debiasi verfasserin (orcid)0000-0003-3490-9936 aut Vitali, Luciano verfasserin aut Parize, Alexandre Luis verfasserin aut Micke, Gustavo Amadeu verfasserin (orcid)0000-0002-5518-624X aut Enthalten in Analytica chimica acta Amsterdam : Elsevier Science, 1947 1275 Online-Ressource (DE-627)300896468 (DE-600)1483436-4 (DE-576)081952619 1873-4324 nnns volume:1275 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.23 Analytische Chemie: Allgemeines VZ AR 1275
language	English
source	Enthalten in Analytica chimica acta 1275 volume:1275
sourceStr	Enthalten in Analytica chimica acta 1275 volume:1275
format_phy_str_mv	Article
bklname	Analytische Chemie: Allgemeines
institution	findex.gbv.de
topic_facet	Magnetic nanoparticles Immobilized enzyme microreactor Acetylcholinesterase
dewey-raw	540
isfreeaccess_bool	false
container_title	Analytica chimica acta
authorswithroles_txt_mv	Siebert, Diogo Alexandre @@aut@@ Caon, Natália Bruzamarello @@aut@@ Alberton, Michele Debiasi @@aut@@ Vitali, Luciano @@aut@@ Parize, Alexandre Luis @@aut@@ Micke, Gustavo Amadeu @@aut@@
publishDateDaySort_date	2023-01-01T00:00:00Z
hierarchy_top_id	300896468
dewey-sort	3540
id	ELV061007269
language_de	englisch
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author	Siebert, Diogo Alexandre
spellingShingle	Siebert, Diogo Alexandre ddc 540 bkl 35.23 misc Magnetic nanoparticles misc Immobilized enzyme microreactor misc Acetylcholinesterase Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system
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topic_title	540 VZ 35.23 bkl Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system Magnetic nanoparticles Immobilized enzyme microreactor Acetylcholinesterase
topic	ddc 540 bkl 35.23 misc Magnetic nanoparticles misc Immobilized enzyme microreactor misc Acetylcholinesterase
topic_unstemmed	ddc 540 bkl 35.23 misc Magnetic nanoparticles misc Immobilized enzyme microreactor misc Acetylcholinesterase
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title	Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system
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title_full	Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system
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author_browse	Siebert, Diogo Alexandre Caon, Natália Bruzamarello Alberton, Michele Debiasi Vitali, Luciano Parize, Alexandre Luis Micke, Gustavo Amadeu
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title_sort	immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system
title_auth	Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system
abstract	Enzyme assays can be performed with the capillary electrophoresis technique (CE) in many approaches, such as the immobilized enzyme micro-reactor. Acetylcholinesterase is a promising enzyme to be used when pursuing such a method, as it has already been explored in the proposal of similar methods of miniaturizing enzyme assays. The present work proposes a novel enzyme micro-reactor, based on the anchorage of the enzyme on magnetic nanoparticles of MnFe2O4, with chitosan and glutaraldehyde as the cross-linker in the capillary by means of an arrange of neodymium magnets. The calculated K m of the enzyme evaluated by this method was 1.12 mmol L−1, comparable to other studies in the literature that utilizes immobilized enzymes. Also, IC50 for neostigmine was assessed in 3 different micro-reactors, with an average of 29.42 ± 3.88 μmol L−1. In terms of the micro-reactor stability, it was possible to perform at least 25 experiments with assembled micro-reactor. The method was applied to hydroalcoholic extracts of 7 plant species. Plinia cauliflora had the best result, with 42.31 ± 6.81% of enzyme inhibition in a concentration of 100 mg L−1.
abstractGer	Enzyme assays can be performed with the capillary electrophoresis technique (CE) in many approaches, such as the immobilized enzyme micro-reactor. Acetylcholinesterase is a promising enzyme to be used when pursuing such a method, as it has already been explored in the proposal of similar methods of miniaturizing enzyme assays. The present work proposes a novel enzyme micro-reactor, based on the anchorage of the enzyme on magnetic nanoparticles of MnFe2O4, with chitosan and glutaraldehyde as the cross-linker in the capillary by means of an arrange of neodymium magnets. The calculated K m of the enzyme evaluated by this method was 1.12 mmol L−1, comparable to other studies in the literature that utilizes immobilized enzymes. Also, IC50 for neostigmine was assessed in 3 different micro-reactors, with an average of 29.42 ± 3.88 μmol L−1. In terms of the micro-reactor stability, it was possible to perform at least 25 experiments with assembled micro-reactor. The method was applied to hydroalcoholic extracts of 7 plant species. Plinia cauliflora had the best result, with 42.31 ± 6.81% of enzyme inhibition in a concentration of 100 mg L−1.
abstract_unstemmed	Enzyme assays can be performed with the capillary electrophoresis technique (CE) in many approaches, such as the immobilized enzyme micro-reactor. Acetylcholinesterase is a promising enzyme to be used when pursuing such a method, as it has already been explored in the proposal of similar methods of miniaturizing enzyme assays. The present work proposes a novel enzyme micro-reactor, based on the anchorage of the enzyme on magnetic nanoparticles of MnFe2O4, with chitosan and glutaraldehyde as the cross-linker in the capillary by means of an arrange of neodymium magnets. The calculated K m of the enzyme evaluated by this method was 1.12 mmol L−1, comparable to other studies in the literature that utilizes immobilized enzymes. Also, IC50 for neostigmine was assessed in 3 different micro-reactors, with an average of 29.42 ± 3.88 μmol L−1. In terms of the micro-reactor stability, it was possible to perform at least 25 experiments with assembled micro-reactor. The method was applied to hydroalcoholic extracts of 7 plant species. Plinia cauliflora had the best result, with 42.31 ± 6.81% of enzyme inhibition in a concentration of 100 mg L−1.
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title_short	Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system
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author2	Caon, Natália Bruzamarello Alberton, Michele Debiasi Vitali, Luciano Parize, Alexandre Luis Micke, Gustavo Amadeu
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up_date	2024-07-06T17:06:09.297Z
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Immobilized acetylcholinesterase in magnetic nanoparticles for in-line inhibition studies using a capillary electrophoresis system

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