Copper formate-lysine nanoparticles with polyphenol oxidase-like activity for the detection of epinephrine.
Copper formate
Epinephrine
Laccase mimics
Lysine
Nanoparticles
Journal
Analytical and bioanalytical chemistry
ISSN: 1618-2650
Titre abrégé: Anal Bioanal Chem
Pays: Germany
ID NLM: 101134327
Informations de publication
Date de publication:
12 Dec 2023
12 Dec 2023
Historique:
received:
07
10
2023
accepted:
05
12
2023
revised:
16
11
2023
medline:
12
12
2023
pubmed:
12
12
2023
entrez:
12
12
2023
Statut:
aheadofprint
Résumé
Laccase is an enzyme known for its eco-friendly uses in environmental cleanup and biotechnology. However, it has limitations such as low stability, high cost, and complex recycling. So, there is a need for laccase mimics that can effectively imitate its properties. Herein, we created copper formate-lysine nanoparticles (Cuf-Lys) that mimic laccase's activity. The developed Cuf-Lys demonstrated remarkable polyphenol oxidase-like activity, stability, and recyclability, making them suitable for the fabrication of efficient colorimetric sensors for the detection of epinephrine. These sensors had a specific response and could accurately measure epinephrine concentrations ranging from 2.5 to 50 μM, with a detection limit as low as 1 μM. Furthermore, the biosensor demonstrated high sensitivity and selectivity when applied to the detection of rutin. The limit of detection for rutin was determined to be 0.16 μM while in the linear concentration range of 0.25 to 150.0 μM. We believe that Cuf-Lys provide a new route for the design of laccase mimics, showing potential applications for biomedical diagnosis and environmental monitoring.
Identifiants
pubmed: 38085339
doi: 10.1007/s00216-023-05095-7
pii: 10.1007/s00216-023-05095-7
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : the Fundamental Research Funds for the Central Universities
ID : WUT: 2022IVA160
Organisme : the Fundamental Research Funds for the Central Universities
ID : 2022IVA089
Organisme : National Natural Science Foundation of China
ID : 21905237
Organisme : National Natural Science Foundation of China
ID : 82302275
Organisme : 7th Yong elite scientist sponsorship program by CAST
ID : No. YESS20210191
Organisme : the Young Top-notch Talent Cultivation Program of Hubei Province
ID : No. 40129014
Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH, DE part of Springer Nature.
Références
Keilin D, Mann T. Some properties of laccase from the latex of lacquer trees. Nature. 1940;145(3669):304.
doi: 10.1038/145304a0
TissiÈRes A. Constitution and properties of laccase. Nature. 1949;163(4143):480.
pubmed: 18115104
doi: 10.1038/163480a0
Lou X, Zhi F, Sun X, Wang F, Hou X, Lv C, Hu Q. Construction of co-immobilized laccase and mediator based on MOFs membrane for enhancing organic pollutants removal. Chem Eng J. 2023;451:138080.
doi: 10.1016/j.cej.2022.138080
Rubenwolf S, Strohmeier O, Kloke A, Kerzenmacher S, Zengerle R, von Stetten F. Carbon electrodes for direct electron transfer type laccase cathodes investigated by current density-cathode potential behavior. Biosens Bioelectron. 2010;26(2):841–5.
pubmed: 20627511
doi: 10.1016/j.bios.2010.05.008
Zhang F, Lian M, Alhadhrami A, Huang M, Li B, Mersal GAM, Ibrahim MM, Xu M. Laccase immobilized on functionalized cellulose nanofiber/alginate composite hydrogel for efficient bisphenol a degradation from polluted water. Adv Compos Hybrid Ma. 2022;5(3):1852–64.
doi: 10.1007/s42114-022-00476-5
Xu S, Wu H, Liu S, Du P, Wang H, Yang H, Xu W, Chen S, Song L, Li J, Shi X, Wang Z-G. A supramolecular metalloenzyme possessing robust oxidase-mimetic catalytic function. Nat Commun. 2023;14(1):4040.
pubmed: 37419896
pmcid: 10328989
doi: 10.1038/s41467-023-39779-6
Rodríguez-Delgado MM, Alemán-Nava GS, Rodríguez-Delgado JM, Dieck-Assad G, Martínez-Chapa SO, Barceló D, Parra R. Laccase-based biosensors for detection of phenolic compounds. TRAC-Trend Anal Chem. 2015;74:21–45.
doi: 10.1016/j.trac.2015.05.008
Liang S, Wu X-L, Xiong J, Yuan X, Liu S-L, Zong M-H, Lou W-Y. Multivalent Ce-MOFs as biomimetic laccase nanozyme for environmental remediation. Chem Eng J. 2022;450:138220.
doi: 10.1016/j.cej.2022.138220
Fernandez-Fernandez M, Sanroman MA, Moldes D. Recent developments and applications of immobilized laccase. Biotechnol Adv. 2013;31(8):1808–25.
pubmed: 22398306
doi: 10.1016/j.biotechadv.2012.02.013
Guo S, Li H, Liu J, Yang Y, Kong W, Qiao S, Huang H, Liu Y, Kang Z. Visible-light-induced effects of au nanoparticle on laccase catalytic activity. ACS Appl Mater Interfaces. 2015;7(37):20937–44.
pubmed: 26322738
doi: 10.1021/acsami.5b06472
Jones SM, Solomon EI. Electron transfer and reaction mechanism of laccases. Cell Mol Life Sci. 2015;72(5):869–83.
pubmed: 25572295
pmcid: 4323859
doi: 10.1007/s00018-014-1826-6
Xia Y, Xia L, Lin X. Laccase-based self-amplifying catalytic system enables efficient antibiotic degradation for sustainable environmental remediation. Adv Sci. 2023;10(21):2300210.
doi: 10.1002/advs.202300210
Hitaishi VP, Clément R, Quattrocchi L, Parent P, Duché D, Zuily L, Ilbert M, Lojou E, Mazurenko I. Interplay between orientation at electrodes and copper activation of Thermus thermophilus laccase for O
doi: 10.1021/jacs.9b11147
Singha A, Sekretareva A, Tao L, Lim H, Ha Y, Braun A, Jones SM, Hedman B, Hodgson KO, Britt RD, Kosman DJ, Solomon EI. Tuning the type 1 reduction potential of multicopper oxidases: uncoupling the effects of electrostatics and H-bonding to histidine ligands. J Am Chem Soc. 2023;145(24):13284–301.
pubmed: 37294874
pmcid: 10392966
doi: 10.1021/jacs.3c03241
Tran TD, Nguyen PT, Le TN, Kim MI. DNA-copper hybrid nanoflowers as efficient laccase mimics for colorimetric detection of phenolic compounds in paper microfluidic devices. Biosens Bioelectron. 2021;182:113187.
pubmed: 33799029
doi: 10.1016/j.bios.2021.113187
Brissos V, Borges PT, Nunez-Franco R, Lucas MF, Frazao C, Monza E, Masgrau L, Cordeiro TN, Martins LO. Distal mutations shape substrate-binding sites during evolution of a metallo-oxidase into a laccase. ACS Catal. 2022;12(9):5022–35.
pubmed: 36567772
pmcid: 9775220
doi: 10.1021/acscatal.2c00336
Castrovilli MC, Bolognesi P, Chiarinelli J, Avaldi L, Calandra P, Antonacci A, Scognamiglio V. The convergence of forefront technologies in the design of laccase-based biosensors - an update. TRAC-Trend Anal Chem. 2019;119:115615.
doi: 10.1016/j.trac.2019.07.026
Lassouane F, Ait-Amar H, Amrani S, Rodriguez-Couto S. A promising laccase immobilization approach for bisphenol A removal from aqueous solutions. Bioresour Technol. 2019;271:360–7.
pubmed: 30293031
doi: 10.1016/j.biortech.2018.09.129
Mahmoodi NM, Saffar-Dastgerdi MH. Clean laccase immobilized nanobiocatalysts (graphene oxide-zeolite nanocomposites): from production to detailed biocatalytic degradation of organic pollutant. Appl Catal B-environ. 2020;268:118443.
doi: 10.1016/j.apcatb.2019.118443
Zhou W, Zhang W, Cai Y. Laccase immobilization for water purification: a comprehensive review. Chem Eng J. 2021;403:126272.
doi: 10.1016/j.cej.2020.126272
Niu X, Wu L, Wu F, Guan J, Wang H. Electron coupling effect-triggered monatomic copper laccase-mimicking nanozyme for the degradation and detection of guaiacol produced by Alicyclobacillus acidoterrestris. Biosens Bioelectron. 2023;238:115606.
pubmed: 37595476
doi: 10.1016/j.bios.2023.115606
Cui H, Zhang L, Söder D, Tang X, Davari MD, Schwaneberg U. Rapid and oriented immobilization of laccases on electrodes via a methionine-rich peptide. ACS Catal. 2021;11(4):2445–53.
doi: 10.1021/acscatal.0c05490
Cao P, Liu H, Wu D, Wang X. Immobilization of laccase on phase-change microcapsules as self-thermoregulatory enzyme carrier for biocatalytic enhancement. Chem Eng J. 2021;405:126695.
doi: 10.1016/j.cej.2020.126695
Wang K-Y, Zhang J, Hsu Y-C, Lin H, Han Z, Pang J, Yang Z, Liang R-R, Shi W, Zhou H-C. Bioinspired framework catalysts: from enzyme immobilization to biomimetic catalysis. Chem Rev. 2023;123(9):5347–420.
pubmed: 37043332
doi: 10.1021/acs.chemrev.2c00879
Zhang Y, Ge J, Liu Z. Enhanced activity of immobilized or chemically modified enzymes. ACS Catal. 2015;5(8):4503–13.
doi: 10.1021/acscatal.5b00996
Wan J, Zhang L, Yang B, Jia B, Yang J, Su X. Enzyme immobilization on amino-functionalized Fe
doi: 10.1016/j.cej.2021.131976
Datta S, Veena R, Samuel MS, Selvarajan E. Immobilization of laccases and applications for the detection and remediation of pollutants: a review. Environ Chem Lett. 2020;19(1):521–38.
doi: 10.1007/s10311-020-01081-y
Daronch NA, Kelbert M, Pereira CS, de Araújo PHH, de Oliveira D. Elucidating the choice for a precise matrix for laccase immobilization: a review. Chem Eng J. 2020;397:125506.
doi: 10.1016/j.cej.2020.125506
Li X, Wu Z, Tao X, Li R, Tian D, Liu X. Gentle one-step co-precipitation to synthesize bimetallic CoCu-MOF immobilized laccase for boosting enzyme stability and Congo red removal. J Hazard Mater. 2022;438:129525.
pubmed: 35816800
doi: 10.1016/j.jhazmat.2022.129525
Peng J, Wu E, Lou X, Deng Q, Hou X, Lv C, Hu Q. Anthraquinone removal by a metal-organic framework/polyvinyl alcohol cryogel-immobilized laccase: effect and mechanism exploration. Chem Eng J. 2021;418:129473.
doi: 10.1016/j.cej.2021.129473
Huang W, Zhang W, Gan Y, Yang J, Zhang S. Laccase immobilization with metal-organic frameworks: current status, remaining challenges and future perspectives. Crit Rev Env Sci Tec. 2020;52(8):1282–324.
doi: 10.1080/10643389.2020.1854565
Liang M, Yan X. Nanozymes: from new concepts, mechanisms, and standards to applications. Acc Chem Res. 2019;52(8):2190–200.
pubmed: 31276379
doi: 10.1021/acs.accounts.9b00140
Wang Z, Zhang R, Yan X, Fan K. Structure and activity of nanozymes: inspirations for de novo design of nanozymes. Mater Today. 2020;41:81–119.
doi: 10.1016/j.mattod.2020.08.020
Liu Y, Liu L, Qu Z, Yu L, Sun Y. Supramolecular assembly of benzophenone alanine and copper presents high laccase-like activity for the degradation of phenolic pollutants. J Hazard Mater. 2023;443:130198.
pubmed: 36279648
doi: 10.1016/j.jhazmat.2022.130198
Le TN, Le XA, Tran TD, Lee KJ, Kim MI. Laccase-mimicking Mn-Cu hybrid nanoflowers for paper-based visual detection of phenolic neurotransmitters and rapid degradation of dyes. J Nanobiotechnol. 2022;20(1):358.
doi: 10.1186/s12951-022-01560-0
Xu W, Zhang Y, Zhang X, Xu X, Wang Q. One stone, two birds: a Cu-S cluster as a laccase-mimicking nanozyme and sulfite activator for phenol remediation in marine environments. J Hazard Mater. 2023;457:131776.
pubmed: 37285787
doi: 10.1016/j.jhazmat.2023.131776
Wang J, Huang R, Qi W, Su R, Binks BP, He Z. Construction of a bioinspired laccase-mimicking nanozyme for the degradation and detection of phenolic pollutants. Appl Catal B-environ. 2019;254:452–62.
doi: 10.1016/j.apcatb.2019.05.012
Zhang X, Wu D, Wu Y, Li G. Bioinspired nanozyme for portable immunoassay of allergenic proteins based on a smartphone. Biosens Bioelectron. 2021;172:112776.
pubmed: 33157408
doi: 10.1016/j.bios.2020.112776
Tang Y, Jiang S, Li W, Jalil Shah S, Zhao Z, Pan L, Zhao Z. Confined construction of COF@Cu-nanozyme with high activity and stability as laccase biomimetic catalyst for the efficient degradation of phenolic pollutants. Chem Eng J. 2022;448:137701.
doi: 10.1016/j.cej.2022.137701
Makam P, Yamijala S, Bhadram VS, Shimon LJW, Wong BM, Gazit E. Single amino acid bionanozyme for environmental remediation. Nat Commun. 2022;13(1):1505.
pubmed: 35314678
pmcid: 8938493
doi: 10.1038/s41467-022-28942-0
Koyappayil A, Kim HT, Lee MH. ‘Laccase-like’ properties of coral-like silver citrate micro-structures for the degradation and determination of phenolic pollutants and adrenaline. J Hazard Mater. 2021;412:125211.
pubmed: 33516111
doi: 10.1016/j.jhazmat.2021.125211
Liang H, Lin F, Zhang Z, Liu B, Jiang S, Yuan Q, Liu J. Multicopper laccase mimicking nanozymes with nucleotides as ligands. ACS Appl Mater Interfaces. 2017;9(2):1352–60.
pubmed: 28004568
doi: 10.1021/acsami.6b15124
Wang J, Huang R, Qi W, Su R, He Z. Preparation of amorphous MOF based biomimetic nanozyme with high laccase- and catecholase-like activity for the degradation and detection of phenolic compounds. Chem Eng J. 2022;434:134677.
doi: 10.1016/j.cej.2022.134677
Li M, Chen J, Wu W, Fang Y, Dong S. Oxidase-like MOF-818 nanozyme with high specificity for catalysis of catechol oxidation. J Am Chem Soc. 2020;142(36):15569–74.
pubmed: 32790301
doi: 10.1021/jacs.0c07273
Liu S, Liu G, Yang L, Li D, Zheng M. Critical influences of metal compounds on the formation and stabilization of environmentally persistent free radicals. Chem Eng J. 2022;427:131666.
doi: 10.1016/j.cej.2021.131666
Zhou Y, Chen X, Zhan S, Wang Q, Deng F, Wu Q, Peng J. Stabilized and controlled release of radicals within copper formate-based nanozymes for biosensing. ACS Appl Mater Interfaces. 2023;15(37):43431–40.
pubmed: 37674322
pmcid: 10520911
doi: 10.1021/acsami.3c08326
Zhang R, Yan X, Fan K. Nanozymes inspired by natural enzymes. Acc Mater Res. 2021;2(7):534–47.
doi: 10.1021/accountsmr.1c00074
Lin Y, Wang F, Yu J, Zhang X, Lu GP. Iron single-atom anchored N-doped carbon as a ‘laccase-like’ nanozyme for the degradation and detection of phenolic pollutants and adrenaline. J Hazard Mater. 2022;425:127763.
pubmed: 34801307
doi: 10.1016/j.jhazmat.2021.127763
Mohtashami M, Fooladi J, Haddad-Mashadrizeh A, Housaindokht MR, Monhemi H. Molecular mechanism of enzyme tolerance against organic solvents: insights from molecular dynamics simulation. Int J Biol Macromol. 2019;122:914–23.
pubmed: 30445665
doi: 10.1016/j.ijbiomac.2018.10.172
Radhakrishnan R, Manna B, Ghosh A. Solvent induced conformational changes for the altered activity of laccase: a molecular dynamics study. J Hazard Mater. 2022;423:127123.
pubmed: 34530268
doi: 10.1016/j.jhazmat.2021.127123
Levy B, Clere-Jehl R, Legras A, Morichau-Beauchant T, Leone M, Frederique G, Quenot J-P, Kimmoun A, Cariou A, Lassus J, Harjola V-P, Meziani F, Louis G, Rossignol P, Duarte K, Girerd N, Mebazaa A, Vignon P, Mattei M, Thivilier C, Perez P, Auchet T, Fritz C, Boisrame-Helme J, Mercier E, Garot D, Perny J, Gette S, Hammad E, Vigne C, Dargent A, Andreu P, Guiot P. Epinephrine versus norepinephrine for cardiogenic shock after acute myocardial infarction. J Am Coll Cardiol. 2018;72(2):173–82.
pubmed: 29976291
doi: 10.1016/j.jacc.2018.04.051
Fatma S, Prasad BB, Jaiswal S, Singh R, Singh K. Electrochemical simultaneous analysis of dopamine and epinephrine using double imprinted One MoNomer acryloylated graphene oxide-carbon black composite polymer. Biosens Bioelectron. 2019;135:36–44.
pubmed: 30991270
doi: 10.1016/j.bios.2019.04.016
Křen V, Bojarová P. Rutinosidase and other diglycosidases: rising stars in biotechnology. Biotechnol Adv. 2023;68:108217.
pubmed: 37481095
doi: 10.1016/j.biotechadv.2023.108217
Li M-Y, Niu X, Pei W-Y, Xu H-L, Ma J-F. Synthesis of sulfonylcalix[4]arene complexes and research on electrochemical detection of rutin by the composites of the complexes with multi-walled carbon nanotubes. Chem Eng J. 2023;470:144060.
doi: 10.1016/j.cej.2023.144060
Ouyang Q, Liu K, Zhu Q, Deng H, Le Y, Ouyang W, Yan X, Zhou W, Tong J. Brain-penetration and neuron-targeting DNA nanoflowers co-delivering miR-124 and rutin for synergistic therapy of Alzheimer’s disease. Small. 2022;18(14):2107534.
doi: 10.1002/smll.202107534