Detection of insecticides by Tetronarce californica acetylcholinesterase via expression and in silico analysis.
Acetylcholinesterase
Immobilization
Insecticide detection
Prokaryotic expression
Journal
Applied microbiology and biotechnology
ISSN: 1432-0614
Titre abrégé: Appl Microbiol Biotechnol
Pays: Germany
ID NLM: 8406612
Informations de publication
Date de publication:
Dec 2023
Dec 2023
Historique:
received:
13
04
2023
accepted:
06
09
2023
revised:
16
08
2023
medline:
20
11
2023
pubmed:
13
10
2023
entrez:
13
10
2023
Statut:
ppublish
Résumé
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 (TcA) in Escherichia coli (E. coli) as a soluble active protein. TcA was immobilized in calcium alginate beads; the morphology, biochemical properties, and insecticide detection performance of free and immobilized TcA were characterized. Moreover, we used sequence, structure-based approaches, and molecular docking to investigate structural and functional characterization of TcA. The results showed that TcA exhibited a specific activity of 102 U/mg, with optimal activity at pH 8.0 and 30 °C. Immobilized TcA demonstrated superior thermal stability, pH stability, and storage stability compared to the free enzyme. The highest sensitivity of free TcA was observed with trichlorfon, whereas immobilized TcA showed reduced IC
Identifiants
pubmed: 37831186
doi: 10.1007/s00253-023-12780-1
pii: 10.1007/s00253-023-12780-1
doi:
Substances chimiques
Insecticides
0
Acetylcholinesterase
EC 3.1.1.7
Trichlorfon
DBF2DG4G2K
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
7657-7671Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
Références
Abdella MAA, Ahmed SA, Hassan ME (2023) Protease immobilization on a novel activated carrier alginate/dextrose beads: improved stability and catalytic activity via covalent binding. Int J Biol Macromol 230:123139. https://doi.org/10.1016/j.ijbiomac.2023.123139
doi: 10.1016/j.ijbiomac.2023.123139
pubmed: 36621737
Ariaeenejad S, Motamedi E (2023) Improved saccharification of rice straw by removing phenolic compounds using a stable immobilized metagenome-derived laccase on sodium alginate-based hydrogel. Biochem Eng J 198:109021. https://doi.org/10.1016/j.bej.2023.109021
doi: 10.1016/j.bej.2023.109021
Bailey TL, Boden M, Buske FA, Frith M, Grant CE, Clementi L, Ren JY, Li WW, Noble WS (2009) MEME SUITE: tools for motif discovery and searching. Nucleic Acids Res 37:W202–W208. https://doi.org/10.1093/nar/gkp335
doi: 10.1093/nar/gkp335
pubmed: 19458158
pmcid: 2703892
Caldas ED (2023) Approaches for cumulative dietary risk assessment of pesticides. Curr Opin Food Sci:101079. https://doi.org/10.1016/j.cofs.2023.101079
Chaabihi H, Fournier D, Fedon Y, Bossy JP, Ravallec M, Devauchelle G, Cerutti M (1994) Biochemical-characterization of Drosophila melanogaster acetylcholinesterase expressed by recombinant baculoviruses. Biochem Biophys Res Commun 203(1):734–742. https://doi.org/10.1006/bbrc.1994.2243
doi: 10.1006/bbrc.1994.2243
pubmed: 8074730
Cheung J, Mahmood A, Kalathur R, Liu L, Carlier PR (2018) Structure of the G119S mutant acetylcholinesterase of the malaria vector Anopheles gambiae reveals basis of insecticide resistance. Structure 26(1):130–136 e132. https://doi.org/10.1016/j.str.2017.11.021
doi: 10.1016/j.str.2017.11.021
pubmed: 29276037
Chuiko GM (2000) Comparative study of acetylcholinesterase and butyrylcholinesterase in brain and serum of several freshwater fish: specific activities and in vitro inhibition by DDVP, an organophosphorus pesticide. Comp Biochem Physiol C Toxicol Pharmacol 127(3):233–242. https://doi.org/10.1016/S0742-8413(00)00150-X
doi: 10.1016/S0742-8413(00)00150-X
pubmed: 11246494
Cui C, Jiang H, Guan M, Ji N, Xiong L, Sun Q (2022) Characterization and in vitro digestibility of potato starch encapsulated in calcium alginate beads. Food Hydrocoll 126:107458. https://doi.org/10.1016/j.foodhyd.2021.107458
doi: 10.1016/j.foodhyd.2021.107458
Das A, Banks S, Chatterjee S, Paul N, Sarkar K, Chatterjee A, Chakraborty S, Banerjee C, Majumdar A, Das M, Ghosh S (2023) Bifenthrin disrupts cytochrome c oxidase activity and reduces mitochondrial DNA copy number through oxidative damage in pool barb (Puntius sophore). Chemosphere 332:138848. https://doi.org/10.1016/j.chemosphere.2023.138848
doi: 10.1016/j.chemosphere.2023.138848
pubmed: 37156291
de Abreu SM, Sette CDAB, Kiametis AS, Romeiro LAS, Gargano R (2019) Molecular modeling of cardanol-derived AChE inhibitors. Chem Phys Lett 731:136591. https://doi.org/10.1016/j.cplett.2019.07.019
doi: 10.1016/j.cplett.2019.07.019
Dvir H, Wong DM, Harel M, Barril X, Orozco M, Luque FJ, Muñoz-Torrero D, Camps P, Rosenberry TL, Silman I, Sussman JL (2002) 3D Structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 Å resolution: kinetic and molecular dynamic correlates. Biochemistry 41(9):2970–2981. https://doi.org/10.1021/bi011652i
doi: 10.1021/bi011652i
pubmed: 11863435
Ekström FJ, Åstot C, Pang YP (2007) Novel nerve-agent antidote design based on crystallographic and mass spectrometric analyses of tabun-conjugated acetylcholinesterase in complex with antidotes. Clin Pharmacol Ther 82(3):282–293. https://doi.org/10.1038/sj.clpt.6100151
doi: 10.1038/sj.clpt.6100151
pubmed: 17443135
Ellman GL, Courtney KD, Andres V Jr, Feather-Stone RM (1961) A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 7:88–95 https://www.ncbi.nlm.nih.gov/pubmed/13726518
doi: 10.1016/0006-2952(61)90145-9
pubmed: 13726518
Gasteiger E, Hoogland C, Gattiker A, Se D, Wilkins MR, Appel RD, Bairoch A (2005) Protein identification and analysis tools on the ExPASy server. In: Walker JM (ed) The proteomics protocols handbook. Humana Press, Totowa, NJ, pp 571–607. https://doi.org/10.1385/1-59259-890-0:571
doi: 10.1385/1-59259-890-0:571
GB/T 2763-2021 (2021) National food safety standard-maximum residue limits for pesticides in food, National health and family planning commission of the People’s Republic of China and Ministry of Agriculture of the People’s Republic of China. China Agriculture Press, Beijing (in Chinese). http://www.aqsc.agri.cn/zlbz/gzdt/202106/t20210603_379939.htm . Accessed 27 Mar 2022
Gholivand K, Ebrahimi Valmoozi AA, Mahzouni HR, Ghadimi S, Rahimi R (2013) Molecular docking and QSAR studies: noncovalent interaction between acephate analogous and the receptor site of human acetylcholinesterase. J Agric Food Chem 61(28):6776–6785. https://doi.org/10.1021/jf401092h
doi: 10.1021/jf401092h
pubmed: 23796225
Giordano D, Langini C, Caflisch A, Marabotti A, Facchiano A (2022) Molecular dynamics analysis of the structural properties of the transglutaminases of Kutzneria albida and Streptomyces mobaraensis. Comput Struct Biotechnol J 20:3924–3934. https://doi.org/10.1016/j.csbj.2022.07.024
doi: 10.1016/j.csbj.2022.07.024
pubmed: 35950183
pmcid: 9334925
Goldenzweig A, Goldsmith M, Hill Shannon E, Gertman O, Laurino P, Ashani Y, Dym O, Unger T, Albeck S, Prilusky J, Lieberman Raquel L, Aharoni A, Silman I, Sussman Joel L, Tawfik Dan S, Fleishman Sarel J (2016) Automated structure- and sequence-based design of proteins for high bacterial expression and stability. Mol Cell 63(2):337–346. https://doi.org/10.1016/j.molcel.2016.06.012
doi: 10.1016/j.molcel.2016.06.012
pubmed: 27425410
pmcid: 4961223
Hackenhaar CR, Rosa CF, Flores EEE, Santagapita PR, Klein MP, Hertz PF (2022) Development of a biocomposite based on alginate/gelatin crosslinked with genipin for β-galactosidase immobilization: Performance and characteristics. Carbohydr Polym 291:119483. https://doi.org/10.1016/j.carbpol.2022.119483
doi: 10.1016/j.carbpol.2022.119483
pubmed: 35698322
Heim J, Schmidt-Dannert C, Atomi H, Schmid RD (1998) Functional expression of a mammalian acetylcholinesterase in Pichia pastoris: comparison to acetylcholinesterase, expressed and reconstituted from Escherichia coli. Biochim Biophys Acta Gene Struct Expr 1396(3):306–319. https://doi.org/10.1016/S0167-4781(97)00196-6
doi: 10.1016/S0167-4781(97)00196-6
Işık M (2020) High stability of immobilized acetylcholinesterase on chitosan beads. ChemistrySelect 5(15):4623–4627. https://doi.org/10.1002/slct.202000559
doi: 10.1002/slct.202000559
Ki M-R, Pack SP (2020) Fusion tags to enhance heterologous protein expression. Appl Microbiol Biotechnol 104(6):2411–2425. https://doi.org/10.1007/s00253-020-10402-8
doi: 10.1007/s00253-020-10402-8
pubmed: 31993706
Kim S, Yoon KA, Cho S, Lee SH (2022) Molecular and kinetic characterization of two acetylcholinesterases with particular focus on the roles of two amino acid substitutions (Y390N and F392W) in Bemisia tabaci. Pestic Biochem Physiol 182:105039. https://doi.org/10.1016/j.pestbp.2022.105039
doi: 10.1016/j.pestbp.2022.105039
pubmed: 35249657
Lalut J, Santoni G, Karila D, Lecoutey C, Davis A, Nachon F, Silman I, Sussman J, Weik M, Maurice T, Dallemagne P, Rochais C (2019) Novel multitarget-directed ligands targeting acetylcholinesterase and σ1 receptors as lead compounds for treatment of Alzheimer’s disease: synthesis, evaluation, and structural characterization of their complexes with acetylcholinesterase. Eur J Med Chem 162:234–248. https://doi.org/10.1016/j.ejmech.2018.10.064
doi: 10.1016/j.ejmech.2018.10.064
pubmed: 30447434
Latif A, Maqbool A, Sun K, Si Y (2022) Immobilization of Trametes Versicolor laccase on Cu-alginate beads for biocatalytic degradation of bisphenol A in water: optimized immobilization, degradation and toxicity assessment. J Environ Chem Eng 10(1):107089. https://doi.org/10.1016/j.jece.2021.107089
doi: 10.1016/j.jece.2021.107089
Letunic I, Bork P (2021) Interactive Tree of Life (iTOL) v5: an online tool for phylogenetic tree display and annotation. Nucleic Acids Res 49(W1):W293–W296. https://doi.org/10.1093/nar/gkab301
doi: 10.1093/nar/gkab301
pubmed: 33885785
pmcid: 8265157
Li C, Zhu H, Guo Y, Xie Y, Cheng Y, Yu H, Qian H, Yao W (2021) Investigation of the transformation and toxicity of trichlorfon at the molecular level during enzymic hydrolysis of apple juice. Food Chem 344:128653. https://doi.org/10.1016/j.foodchem.2020.128653
doi: 10.1016/j.foodchem.2020.128653
pubmed: 33229164
Liang Z, Mahmoud Abdelshafy A, Luo Z, Belwal T, Lin X, Xu Y, Wang L, Yang M, Qi M, Dong Y, Li L (2022) Occurrence, detection, and dissipation of pesticide residue in plant-derived foodstuff: a state-of-the-art review. Food Chem 384:132494. https://doi.org/10.1016/j.foodchem.2022.132494
doi: 10.1016/j.foodchem.2022.132494
pubmed: 35189435
Madauss KP, Deng S-J, Austin RJH, Lambert MH, McLay I, Pritchard J, Short SA, Stewart EL, Uings IJ, Williams SP (2004) Progesterone receptor ligand binding pocket flexibility: crystal structures of the norethindrone and mometasone furoate complexes. J Med Chem 47(13):3381–3387. https://doi.org/10.1021/jm030640n
doi: 10.1021/jm030640n
pubmed: 15189034
Madeira F, Pearce M, Tivey ARN, Basutkar P, Lee J, Edbali O, Madhusoodanan N, Kolesnikov A, Lopez R (2022) Search and sequence analysis tools services from EMBL-EBI in 2022. Nucleic Acids Res 50 W(1):W276–W279. https://doi.org/10.1093/nar/gkac240
doi: 10.1093/nar/gkac240
Martín MC, López OV, Ciolino AE, Morata VI, Villar MA, Ninago MD (2019) Immobilization of enological pectinase in calcium alginate hydrogels: a potential biocatalyst for winemaking. Biocatal Agric Biotechnol 18:101091. https://doi.org/10.1016/j.bcab.2019.101091
doi: 10.1016/j.bcab.2019.101091
Martins-Gomes C, Coutinho TE, Silva TL, Andreani T, Silva AM (2022) Neurotoxicity assessment of four different pesticides using in vitro enzymatic inhibition assays. Toxics 10(8):448. https://doi.org/10.3390/toxics10080448
doi: 10.3390/toxics10080448
pubmed: 36006126
pmcid: 9413506
Mechri S, Allala F, Bouacem K, Hasnaoui I, Gwaithan H, Chalbi TB, Saalaoui E, Asehraou A, Noiriel A, Abousalham A, Hacene H, Bouanane-Darenfed A, Le Roes-Hill M, Jaouadi B (2022) Preparation, characterization, immobilization, and molecular docking analysis of a novel detergent-stable subtilisin-like serine protease from Streptomyces mutabilis strain TN-X30. Int J Biol Macromol 222:1326–1342. https://doi.org/10.1016/j.ijbiomac.2022.09.161
doi: 10.1016/j.ijbiomac.2022.09.161
pubmed: 36242508
Morel N, MassouliÉ J (1997) Expression and processing of vertebrate acetylcholinesterase in the yeast Pichia pastoris. Biochem J 328(1):121–129. https://doi.org/10.1042/bj3280121
doi: 10.1042/bj3280121
pubmed: 9359842
pmcid: 1218895
Nachon F, Carletti E, Ronco C, Trovaslet M, Nicolet Y, Jean L, Renard P-Y (2013) Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer’s drugs targeting acetyl- and butyryl-cholinesterase. Biochem J 453(3):393–399. https://doi.org/10.1042/BJ20130013
doi: 10.1042/BJ20130013
pubmed: 23679855
Nasiri M, Babaie J, Amiri S, Azimi E, Shamshiri S, Khalaj V, Golkar M, Fard-Esfahani P (2017) SHuffle™ T7 strain is capable of producing high amount of recombinant human fibroblast growth factor-1 (rhFGF-1) with proper physicochemical and biological properties. J Biotechnol 259:30–38. https://doi.org/10.1016/j.jbiotec.2017.08.015
doi: 10.1016/j.jbiotec.2017.08.015
pubmed: 28827102
Omasits U, Ahrens CH, Müller S, Wollscheid B (2014) Protter: interactive protein feature visualization and integration with experimental proteomic data. Bioinformatics 30(6):884–886. https://doi.org/10.1093/bioinformatics/btt607
doi: 10.1093/bioinformatics/btt607
pubmed: 24162465
Owczarek B, Gerszberg A, Hnatuszko-Konka K (2019) A brief reminder of systems of production and chromatography-based recovery of recombinant protein biopharmaceuticals. Biomed Res Int 2019:4216060. https://doi.org/10.1155/2019/4216060
doi: 10.1155/2019/4216060
pubmed: 30729123
pmcid: 6341259
Qing G, Ma LC, Khorchid A, Inouye M (2004) Cold-shock induced high-yield protein production in Escherichia coli. Nat Biotechnol 22(7):877–882. https://doi.org/10.1038/nbt984
doi: 10.1038/nbt984
pubmed: 15195104
Radi Z, Taylor P (2006) Chapter 12 - Structure and function of cholinesterases. In: Gupta RC (ed) Toxicology of organophosphate & carbamate compounds. Academic Press, Burlington, pp 161–186. https://doi.org/10.1016/B978-012088523-7/50013-2
doi: 10.1016/B978-012088523-7/50013-2
Radic Z, Gibney G, Kawamoto S, Macpheequigley K, Bongiorno C, Taylor P (1992) Expression of recombinant acetylcholinesterase in a baculovirus system - kinetic-properties of glutamate 199 mutants. Biochemistry 31(40):9760–9767. https://doi.org/10.1021/bi00155a032
doi: 10.1021/bi00155a032
pubmed: 1356436
Raves ML, Harel M, Pang YP, Silman I, Kozikowski AP, Sussman JL (1997) Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A. Nat Struct Biol 4(1):57–63. https://doi.org/10.1038/nsb0197-57
doi: 10.1038/nsb0197-57
pubmed: 8989325
Rehman HU, Aman A, Silipo A, Qader SAU, Molinaro A, Ansari A (2013) Degradation of complex carbohydrate: immobilization of pectinase from Bacillus licheniformis KIBGE-IB21 using calcium alginate as a support. Food Chem 139(1):1081–1086. https://doi.org/10.1016/j.foodchem.2013.01.069
doi: 10.1016/j.foodchem.2013.01.069
pubmed: 23561212
Renault L, Negre V, Hotelier T, Cousin X, Marchot P, Chatonnet A (2005) New friendly tools for users of ESTHER, the database of the α/β-hydrolase fold superfamily of proteins. Chem Biol Interact 157–158:339–343. https://doi.org/10.1016/j.cbi.2005.10.100
doi: 10.1016/j.cbi.2005.10.100
pubmed: 16297901
Reshmi R, Sanjay G, Sugunan S (2007) Immobilization of α-amylase on zirconia: a heterogeneous biocatalyst for starch hydrolysis. Catal Commun 8(3):393–399. https://doi.org/10.1016/j.catcom.2006.07.009
doi: 10.1016/j.catcom.2006.07.009
Ribeiro EB, Ribeiro DB, dos Santos Soares AM, Marques PRBO, Badea M, Targa M, Granato JA, Nunes GS (2022) A novel glutathione-S-transferase-based biosensor for pyrethroid insecticides: from inhibition study to detection. Sens Actuators Rep 4:100093. https://doi.org/10.1016/j.snr.2022.100093
doi: 10.1016/j.snr.2022.100093
Ruiz E, Busto MD, Ramos-Gómez S, Palacios D, Pilar-Izquierdo MC, Ortega N (2018) Encapsulation of glucose oxidase in alginate hollow beads to reduce the fermentable sugars in simulated musts. Food Biosci 24:67–72. https://doi.org/10.1016/j.fbio.2018.06.004
doi: 10.1016/j.fbio.2018.06.004
Sanson B, Colletier J-P, Xu Y, Lang PT, Jiang H, Silman I, Sussman JL, Weik M (2011) Backdoor opening mechanism in acetylcholinesterase based on X-ray crystallography and molecular dynamics simulations. Protein Sci 20(7):1114–1118. https://doi.org/10.1002/pro.661
doi: 10.1002/pro.661
pubmed: 21594947
pmcid: 3149184
Santos JC, Handa S, Fernandes LGV, Bleicher L, Gandin CA, de Oliveira-Neto M, Ghosh P, Nascimento ALTO (2023) Structural and biochemical characterization of Leptospira interrogans Lsa45 reveals a penicillin-binding protein with esterase activity. Process Biochem 125:141–153. https://doi.org/10.1016/j.procbio.2022.12.010
doi: 10.1016/j.procbio.2022.12.010
pubmed: 36643388
Sato R, Matsumoto T, Hidaka N, Imai Y, Abe K, Takahashi S, Yamada R-h, Kera Y (2009) Cloning and expression of carp acetylcholinesterase gene in Pichia pastoris and characterization of the recombinant enzyme. Protein Expr Purif 64(2):205–212. https://doi.org/10.1016/j.pep.2008.12.003
doi: 10.1016/j.pep.2008.12.003
pubmed: 19121395
Shukla E, Thorat L, Bhavnani V, Bendre AD, Pal JK, Nath BB, Gaikwad SM (2016) Molecular cloning and in silico studies of physiologically significant trehalase from Drosophila melanogaster. Int J Biol Macromol 92:282–292. https://doi.org/10.1016/j.ijbiomac.2016.06.097
doi: 10.1016/j.ijbiomac.2016.06.097
pubmed: 27377458
Silman I, Shnyrov VL, Ashani Y, Roth E, Nicolas A, Sussman JL, Weiner L (2021) Torpedo californica acetylcholinesterase is stabilized by binding of a divalent metal ion to a novel and versatile 4D motif. Protein Sci 30(5):966–981. https://doi.org/10.1002/pro.4061
doi: 10.1002/pro.4061
pubmed: 33686648
pmcid: 8040873
Sindhu T, Venkatesan T, Prabhu D, Jeyakanthan J, Gracy GR, Jalali SK, Rai A (2018) Insecticide-resistance mechanism of Plutella xylostella (L.) associated with amino acid substitutions in acetylcholinesterase-1: a molecular docking and molecular dynamics investigation. Comput Biol Chem 77:240–250. https://doi.org/10.1016/j.compbiolchem.2018.09.004
doi: 10.1016/j.compbiolchem.2018.09.004
pubmed: 30368112
Šinko G (2023) Modeling of a near-attack conformation of oxime in phosphorylated acetylcholinesterase via a reactivation product, a phosphorylated oxime. Chem Biol Interact:110656. https://doi.org/10.1016/j.cbi.2023.110656
Sugiki T, Fujiwara T, Kojima C (2017) Cold-shock expression system in E. coli for protein NMR studies. Methods Mol Biol 1586:345–357. https://doi.org/10.1007/978-1-4939-6887-9_23
doi: 10.1007/978-1-4939-6887-9_23
pubmed: 28470617
Sun L, Li Z, Wu H, Li X, Gao F, Qian Y, Wang X (2019) Expression and preparation of recombinant human acetylcholinesterase in vitro and screening of micromolecule for anti-AchE activity. Chin J Pharm Anal 39(3):386–392
Sussman JL, Harel M, Frolow F, Varon L, Toker L, Futerman AH, Silman I (1988) Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C. J Mol Biol 203(3):821–823. https://doi.org/10.1016/0022-2836(88)90213-6
doi: 10.1016/0022-2836(88)90213-6
pubmed: 2850366
Sussman JL, Harel M, Frolow F, Varon L, Toker L, Futerman AH, Silman I (1991) Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 253(5022):872–879. https://doi.org/10.1126/science.1678899
doi: 10.1126/science.1678899
pubmed: 1678899
Tamagno WA, Alves C, Pompermaier A, Barcellos LJG (2023) Pyrethroid-based insecticides exert transgenerational, persistent, and chronic effects in Caenorhabditis elegans. Comp Biochem Physiol C 270:109653. https://doi.org/10.1016/j.cbpc.2023.109653
doi: 10.1016/j.cbpc.2023.109653
Tamura K, Stecher G, Kumar S (2021) MEGA11 Molecular evolutionary genetics analysis version 11. Mol Biol Evol 38(7):3022–3027. https://doi.org/10.1093/molbev/msab120
doi: 10.1093/molbev/msab120
pubmed: 33892491
pmcid: 8233496
Teufel F, Armenteros JJA, Johansen AR, Gislason MH, Pihl SI, Tsirigos KD, Winther O, Brunak S, von Heijne G, Nielsen H (2022) SignalP 6.0 predicts all five types of signal peptides using protein language models. Nat Biotechnol. https://doi.org/10.1038/s41587-021-01156-3
Thirumavalavan M (2023) Functionalized chitosan and sodium alginate for the effective removal of recalcitrant organic pollutants. Int J Biol Macromol 243:125276. https://doi.org/10.1016/j.ijbiomac.2023.125276
doi: 10.1016/j.ijbiomac.2023.125276
pubmed: 37301344
Vahab J, Khadijeh B, Jabraeil Z, Shima K, Parisa G (2020) Improved expression of recombinant sweet-tasting brazzein using codon optimization and host change as new strategies. Food Biotechnol 34(1):62–76. https://doi.org/10.1080/08905436.2019.1711113
doi: 10.1080/08905436.2019.1711113
Villatte F, Marcel V, Estrada-Mondaca S, Fournier D (1998) Engineering sensitive acetylcholinesterase for detection of organophosphate and carbamate insecticides. Biosens Bioelectron 13(2):157–164. https://doi.org/10.1016/S0956-5663(97)00108-5
doi: 10.1016/S0956-5663(97)00108-5
pubmed: 9597732
Yin H, Shen G, Zhu H, Jiang G, Lu Y (2010) Magnetic particle-based enzyme linked immunosorbent assay for detection of organophosphorus pesticide. Environ Pollut Control 32(09):41–45. https://doi.org/10.1360/972010-1322
doi: 10.1360/972010-1322
Yushkova ED, Nazarova EA, Matyuhina AV, Noskova AO, Shavronskaya DO, Vinogradov VV, Skvortsova NN, Krivoshapkina EF (2019) Application of immobilized enzymes in food industry. J Agric Food Chem 67(42):11553–11567. https://doi.org/10.1021/acs.jafc.9b04385
doi: 10.1021/acs.jafc.9b04385
pubmed: 31553885
Zhao P, Wang Y, Jiang H (2013) Biochemical properties, expression profiles, and tissue localization of orthologous acetylcholinesterase-2 in the mosquito, Anopheles gambiae. Insect Biochem Mol Biol 43(3):260–271. https://doi.org/10.1016/j.ibmb.2012.12.005
doi: 10.1016/j.ibmb.2012.12.005
pubmed: 23267863
Zhu Y, Wang M, Zhang X, Cao J, She Y, Cao Z, Wang J, Abd El-Aty AM (2022) Acetylcholinesterase immobilized on magnetic mesoporous silica nanoparticles coupled with fluorescence analysis for rapid detection of carbamate pesticides. ACS Appl Nano Mater 5(1):1327–1338. https://doi.org/10.1021/acsanm.1c03884
doi: 10.1021/acsanm.1c03884