Abstract
This study aimed to conjugate glucose oxidase (GOX) with carbon-encapsulated iron nanoparticles (Fe@C) which were functionalized with carboxylic groups and decorated with branched polyethyleneimine (PEI), in order to yield Fe@C-NH-PEI-GOX and Fe@C-(CH2)2-CONH-PEI-GOX derivatives. The process of electrostatic attachment of the GOX enzyme on the Fe@C-NH-PEI and Fe@C-(CH2)2CONH-PEI constructs was optimized, and the amount of enzyme attached on the constructs was also estimated. The steady-state kinetics of β-D-glucose oxidation by molecular oxygen, a reaction catalyzed by GOX, were compared using a native GOX enzyme obtained from Aspergillus niger and nanoparticles-conjugated GOX. The Fe@C-NH-PEI-GOX and Fe@C-(CH2)2-CONH-PEI-GOX constructs were formed by electrostatic interaction between positively charged Fe@C-NH-PEI and Fe@C-(CH2)2-CONH-PEI and negatively charged GOX in water media at pH 6. The activity of the immobilized enzyme on Fe@C-NH-PEI-GOX and Fe@C-(CH2)2-CONH-PEI-GOX derivatives was preserved, with Km values of 3271 and 1605 µM, respectively. However, the catalytic activity of Fe@C-NH-PEI-GOX and Fe@C-(CH2)2-CONH-PEI-GOX was reduced up to 20- and tenfold in comparison to that of the free GOX enzyme. The results of the study suggest that PEI is a promising cationic polymer with a high loading capacity and that the use of a simple adsorption process for preparing Fe@C-NH-PEI-GOX and Fe@C-(CH2)2-CONH-PEI-GOX conjugates is a highly efficient approach for stable immobilization of GOX enzyme on carbon-encapsulated iron nanoparticles.
Similar content being viewed by others
References
Ju-Nam Y, Lead JR (2008) Manufactured nanoparticles: an overview of their chemistry, interactions and potential environmental implications. The Sci Total Environ 400(1–3):396–414. https://doi.org/10.1016/j.scitotenv.2008.06.042
Li J, Xin M, Ma Z, Shi Y, Pan L (2021) Nanomaterials and their applications on bio-inspired wearable electronics. Nanotechnology. https://doi.org/10.1088/1361-6528/abe6c7
Hu X, Zhang Y, Ding T, Liu J, Zhao H (2020) Multifunctional gold nanoparticles: a novel nanomaterial for various medical applications and biological activities. Front Bioeng Biotechnol. https://doi.org/10.3389/fbioe.2020.00990
Rajabathar JR, Periyasami G, Alanazi AM, Govindasamy M, Arunachalam P (2020) Review on carbon nanotube varieties for healthcare application: effect of preparation methods and mechanism insight. Processes. https://doi.org/10.3390/pr8121654
Zhang L, Ying Y, Li Y, Fu Y (2020) Integration and synergy in protein-nanomaterial hybrids for biosensing: strategies and in-field detection applications. Biosens Bioelectron. https://doi.org/10.1016/j.bios.2020.112036
Ates B, Ulu A, Koytepe S, Noma SAA, Kolat VS, Izgi T (2018) Magnetic-propelled Fe3O4-chitosan carriers enhance l-asparaginase catalytic activity: a promising strategy for enzyme immobilization. RSC Adv 8(63):36063–36075. https://doi.org/10.1039/c8ra06346j
Tarhan T, Ulu A, Saricam M, Culha M, Ates B (2020) Maltose functionalized magnetic core/shell Fe3O4@Au nanoparticles for an efficient L-asparaginase immobilization. Int J Biol Macromol 142:443–451. https://doi.org/10.1016/j.ijbiomac.2019.09.116
Giugliano AMM, Michele (2014) Carbon-based smart nanomaterials in biomedicine and neuroengineering. Beilstein J Nanotechnol 5(1):1849-1863. https://doi.org/10.3762/bjnano.5.196
Ulu A, Noma SAA, Koytepe S, Ates B (2018) Magnetic Fe3O4@MCM-41 core-shell nanoparticles functionalized with thiol silane for efficient l-asparaginase immobilization. Artif Cells Nanomed Biotechnol 46:1035–1045. https://doi.org/10.1080/21691401.2018.1478422
Bamburowicz-Klimkowska M, Poplawska M, Grudzinski IP (2019) Nanocomposites as biomolecules delivery agents in nanomedicine. J Nanobiotechnol. https://doi.org/10.1186/s12951-019-0479-x
Noma SAA, Ulu A, Acet O, Sanz R, Sanz-Perez ES, Odabasi M, Ates B (2020) Comparative study of ASNase immobilization on tannic acid-modified magnetic Fe3O4/SBA-15 nanoparticles to enhance stability and reusability. New J Chem 44(11):4440–4451. https://doi.org/10.1039/d0nj00127a
Bankar SB, Bule MV, Singhal RS, Ananthanarayan L (2009) Glucose oxidase - an overview. Biotechnol Adv 27(4):489–501. https://doi.org/10.1016/j.biotechadv.2009.04.003
Leskovac V, Trivic S, Wohlfahrt G, Kandrac J, Pericin D (2005) Glucose oxidase from Aspergillus niger: the mechanism of action with molecular oxygen, quinones, and one-electron acceptors. Int J Biochem Cell Biol 37(4):731–750. https://doi.org/10.1016/j.biocel.2004.10.014
Ammam M, Fransaer J (2011) Effects of AC-electrolysis on the enzymatic activity of glucose oxidase. Electroanalysis 23(3):755–763. https://doi.org/10.1002/elan.201000598
Fu LH, Qi C, Lin J, Huang P (2018) Catalytic chemistry of glucose oxidase in cancer diagnosis and treatment. Chem Soc Rev 47(17):6454–6472. https://doi.org/10.1039/c7cs00891k
Dubey MK, Zehra A, Aamir M, Meena M, Ahirwal L, Singh S, Shukla S, Upadhyay RS, Bueno-Mari R, Bajpai VK (2017) Improvement strategies, cost effective production, and potential applications of fungal glucose oxidase (GOD): current updates. Front Microbiol. https://doi.org/10.3389/fmicb.2017.01032
Wong CM, Wong KH, Chen XD (2008) Glucose oxidase: natural occurrence, function, properties and industrial applications. Appl Microbiol Biotechnol 78(6):927–938. https://doi.org/10.1007/s00253-008-1407-4
Li XJ, Xie XF, Xing FG, Xu L, Zhang J, Wang ZD (2019) Glucose oxidase as a control agent against the fungal pathogen Botrytis cinerea in postharvest strawberry. Food Control 105:277–284. https://doi.org/10.1016/j.foodcont.2019.05.037
Maity D, Minitha CR, Kumar RTR (2019) Glucose oxidase immobilized amine terminated multiwall carbon nanotubes/reduced graphene oxide/polyaniline/gold nanoparticles modified screen-printed carbon electrode for highly sensitive amperometric glucose detection. Mater Sci Eng C-Mater Biol Appl. https://doi.org/10.1016/j.msec.2019.110075
Siddique S, Mukhtar H (2019) Probing the performance of glucose oxidase treated graphene-based field effect transistors. J Nanosci Nanotechnol 19(11):7442–7446. https://doi.org/10.1166/jnn.2019.16723
Raba J, Mottola HA (1995) Glucose-oxidase as an analytical reagent. Crit Rev Anal Chem 25(1):1–42. https://doi.org/10.1080/10408349508050556
Bahulekar R, Ayyangar NR, Ponrathnam S (1991) Polyethyleneimine in immobilization of biocataysts. Enzyme Microb Technol 13(11):858–868. https://doi.org/10.1016/0141-0229(91)90101-f
Altikatoglu M, Basaran Y, Arioz C, Ogan A, Kuzu H (2010) Glucose oxidase-dextran conjugates with enhanced stabilities against temperature and pH. Appl Biochem Biotechnol 160(8):2187–2197. https://doi.org/10.1007/s12010-009-8812-8
Holland JT, Lau C, Brozik S, Atanassov P, Banta S (2011) Engineering of glucose oxidase for direct electron transfer via site-specific gold nanoparticle conjugation. J Am Chem Soc 133(48):19262–19265. https://doi.org/10.1021/ja2071237
Zhu Z, Wang M, Gautam A, Nazor J, Momeu C, Prodanovic R, Schwaneberg U (2007) Directed evolution of glucose oxidase from Aspergillus niger for ferrocenemethanol-mediated electron transfer. Biotechnol J 2(2):241–248. https://doi.org/10.1002/biot.200600185
Bilal M, Ashraf SS, Romanholo Ferreira LF, Cui J, Lou W-Y, Franco M, Iqbal HMN (2020) Nanostructured materials as a host matrix to develop robust peroxidases-based nanobiocatalytic systems. Int J Biol Macromol 162:1906–1923. https://doi.org/10.1016/j.ijbiomac.2020.08.122
Malar CG, Seenuvasan M, Kumar KS, Kumar A, Parthiban R (2020) Review on surface modification of nanocarriers to overcome diffusion limitations: an enzyme immobilization aspect. Biochem Eng J. https://doi.org/10.1016/j.bej.2020.107574
Bolivar JM, Nidetzky B (2019) The microenvironment in immobilized enzymes: methods of characterization and its role in determining enzyme performance. Molecules. https://doi.org/10.3390/molecules24193460
Reis CLB, de Sousa EYA, Serpa JD, Oliveira RC, dos Santos JCS (2019) Design of immobilized enzyme biocatalysts: drawbacks and opportunities. Quim Nova 42(7):768–783
Virgen-Ortiz JJ, dos Santos JCS, Berenguer-Murcia A, Barbosa O, Rodrigues RC, Fernandez-Lafuente R (2017) Polyethylenimine: a very useful ionic polymer in the design of immobilized enzyme biocatalysts. J Mater Chem B 5(36):7461–7490. https://doi.org/10.1039/c7tb01639e
Xiang XR, Huang H, Hu Y (2017) Research progress on enzyme immobilized on nanocomposites. Chin J Inorg Chem 33(1):1–15
Jager M, Schubert S, Ochrimenko S, Fischer D, Schubert US (2012) Branched and linear poly(ethylene imine)-based conjugates: synthetic modification, characterization, and application. Chem Soc Rev 41(13):4755–4767. https://doi.org/10.1039/c2cs35146c
Gao SQ, Tian HY, Xing ZK, Zhang DW, Guo Y, Guo ZP, Zhu XJ, Chen XS (2016) A non-viral suicide gene delivery system traversing the blood brain barrier for non-invasive glioma targeting treatment. J Control Release 243:357–369. https://doi.org/10.1016/j.jconrel.2016.10.027
Demeneix B, Behr JP (2005). Polyethylenimine (PEI). Non-viral vectors for gene therapy, 2nd Edition: Part 1. Huang L, Hung MC and Wagner E. 53:217–230
Zhang YG, Shu HM, Hu J, Zhang M, Wu JW, Liu KH, Zhu Q (2016) Binding affinity, cellular uptake, and subsequent intracellular trafficking of the nano-gene vector P123-PEI-R13. J Nanomater. https://doi.org/10.1155/2016/7064246
Choosakoonkriang S, Lobo BA, Koe GS, Koe JG, Middaugh CR (2003) Biophysical characterization of PEI/DNA complexes. J Pharm Sci 92(8):1710–1722. https://doi.org/10.1002/jps.10437
Sun CB, Tang T, Uludag H, Cuervo JE (2011) Molecular dynamics simulations of DNA/PEI complexes: effect of pei branching and protonation state. Biophys J 100(11):2754–2763. https://doi.org/10.1016/j.bpj.2011.04.045
Taranejoo S, Liu J, Verma P, Hourigan K (2015) A review of the developments of characteristics of PEI derivatives for gene delivery applications. J Appl Polym Sci. https://doi.org/10.1002/app.42096
Degors IMS, Wang CF, Rehman ZU, Zuhorn IS (2019) Carriers break barriers in drug delivery: endocytosis and endosomal escape of gene delivery vectors. Acc Chem Res 52(7):1750–1760. https://doi.org/10.1021/acs.accounts.9b00177
Di Gioia S, Conese M (2009) Polyethylenimine-mediated gene delivery to the lung and therapeutic applications. Drug Des Dev Ther 2:163–188
Merlin JL, N’Doye A, Bouriez T, Dolivet G (2002) Polyethylenimine derivatives as potent nonviral vectors for gene transfer. Drug News Perspect 15(7):445–451. https://doi.org/10.1358/dnp.2002.15.7.840080
Kasprzak A, Poplawska M, Bystrzejewski M, Labedz O, Grudzinski IP (2015) Conjugation of polyethylenimine and its derivatives to carbon-encapsulated iron nanoparticles. RSC Adv 5(104):85556–85567. https://doi.org/10.1039/c5ra17912b
Masotti A, Pitta A, Ortaggi G, Corti M, Innocenti C, Lascialfari A, Marinone M, Marzola P, Daducci A, Sbarbati A, Micotti E, Orsini F, Poletti G, Sangregorio C (2009) Synthesis and characterization of polyethylenimine-based iron oxide composites as novel contrast agents for MRI. Magn Reson Mater Phys, Biol Med 22(2):77–87. https://doi.org/10.1007/s10334-008-0147-x
Guller AE, Nadort A, Generalova AN, Khaydukov EV, Nechaev AV, Kornienko IA, Petersen EV, Liang L, Shekhter AB, Qian Y, Goldys EM, Zvyagin AV (2018) Rational surface design of upconversion nanoparticles with polyethylenimine coating for biomedical applications: Better Safe than brighter? ACS Biomater Sci Eng 4(9):3143–3153. https://doi.org/10.1021/acsbiomaterials.8b00633
Zhang Y, Tan X, Ren T, Jia C, Yang Z, Sun H (2018) Folate-modified carboxymethyl-chitosan/polyethylenimine/bovine serum albumin based complexes for tumor site-specific drug delivery. Carbohyd Polym 198:76–85. https://doi.org/10.1016/j.carbpol.2018.06.055
Zakeri A, Kouhbanani MAJ, Beheshtkhoo N, Beigi V, Mousavi SM, Hashemi SAR, Zade AK, Amani AM, Savardashtaki A, Mirzaei E, Jahandideh S, Movahedpour A (2018) Polyethylenimine-based nanocarriers in co-delivery of drug and gene: a developing horizon. Nano Rev Exp. https://doi.org/10.1080/20022727.2018.1488497
Xue HY, Liu SM, Wong HL (2014) Nanotoxicity: a key obstacle to clinical translation of siRNA-based nanomedicine. Nanomedicine 9(2):295–312. https://doi.org/10.2217/nnm.13.204
Padilla-Martinez SG, Martinez-Jothar L, Sampedro JG, Tristan F, Perez E (2015) Enhanced thermal stability and pH behavior of glucose oxidase on electrostatic interaction with polyethylenimine. Int J Biol Macromol 75:453–459. https://doi.org/10.1016/j.ijbiomac.2015.02.005
Adeel M, Bilal M, Rasheed T, Sharma A, Iqbal HMN (2018) Graphene and graphene oxide: functionalization and nano-bio-catalytic system for enzyme immobilization and biotechnological perspective. Int J Biol Macromol 120:1430–1440. https://doi.org/10.1016/j.ijbiomac.2018.09.144
Krishnan SK, Singh E, Singh P, Meyyappan M, Nalwa HS (2019) A review on graphene-based nanocomposites for electrochemical and fluorescent biosensors. RSC Adv 9(16):8778–8881. https://doi.org/10.1039/c8ra09577a
Borysiuk J, Grabias A, Szczytko J, Bystrzejewski M, Twardowski A, Lange H (2008) Structure and magnetic properties of carbon encapsulated Fe nanoparticles obtained by arc plasma and combustion synthesis. Carbon 46(13):1693–1701. https://doi.org/10.1016/j.carbon.2008.07.011
Bystrzejewski M, Huczko A, Lange H (2005) Arc plasma route to carbon-encapsulated magnetic nanoparticles for biomedical applications. Sens Actuators B-Chem 109(1):81–85. https://doi.org/10.1016/j.snb.2005.03.029
Poplawska M, Bystrzejewski M, Grudzinski IP, Cywinska MA, Ostapko J, Cieszanowski A (2014) Immobilization of gamma globulins and polyclonal antibodies of class IgG onto carbon-encapsulated iron nanoparticles functionalized with various surface linkers. Carbon 74:180–194. https://doi.org/10.1016/j.carbon.2014.03.022
Kasprzak A, Poplawska M, Bystrzejewski M, Grudzinski IP (2016) Sulfhydrylated graphene-encapsulated iron nanoparticles directly aminated with polyethylenimine: a novel magnetic nanoplatform for bioconjugation of gamma globulins and polyclonal antibodies. J Mater Chem B 4(33):5593–5607. https://doi.org/10.1039/c6tb00838k
Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC (1985) Measurement of protein using bicinchoninic acid. Anal Biochem 150(1):76–85. https://doi.org/10.1016/0003-2697(85)90442-7
Gimeno P, Bousquet C, Lassu N, Maggio A-F, Civade C, Brenier C, Lempereur L (2015) High-performance liquid chromatography method for the determination of hydrogen peroxide present or released in teeth bleaching kits and hair cosmetic products. J Pharm Biomed Anal 107:386–393. https://doi.org/10.1016/j.jpba.2015.01.018
Petteys BJ, Frank EL (2011) Rapid determination of vitamin B-2 (riboflavin) in plasma by HPLC. Clin Chim Acta 412(1–2):38–43. https://doi.org/10.1016/j.cca.2010.08.037
Cao X, Li Y, Zhang Z, Yu J, Qian J, Liu S (2012) Catalytic activity and stability of glucose oxidase/horseradish peroxidase co-confined in macroporous silica foam. Analyst 137(24):5785–5791. https://doi.org/10.1039/c2an36237f
Cui JH, Cui HX, Wang Y, Sun CJ, Li K, Ren HY, Du W (2012) Application of PEI-modified magnetic nanoparticles as gene transfer vector for the genetic modification of animals. Adv Mater Sci Eng. https://doi.org/10.1155/2012/764521
Ciaurriz P, Bravo E, Hamad-Schifferli K (2014) Effect of architecture on the activity of glucose oxidase/horseradish peroxidase/carbon nanoparticle conjugates. J Coll Interface Sci 414:73–81. https://doi.org/10.1016/j.jcis.2013.09.039
Sun J, Wang CH, Wang YZ, Ji SX, Liu WF (2019) Immobilization of carbonic anhydrase on polyethylenimine/dopamine codeposited membranes. J Appl Polym Sci. https://doi.org/10.1002/app.47784
Ozyilmaz G, Tukel SS, Alptekin O (2005) Activity and storage stability of immobilized glucose oxidase onto magnesium silicate. J Mol Catal B-Enzymatic 35(4–6):154–160. https://doi.org/10.1016/j.molcatb.2005.07.001
Sozugecer S, Bayramgil NP (2013) Activity of glucose oxidase immobilized onto Fe3+ attached hydroxypropyl methylcellulose films. Coll Surf B-Biointerfaces 101:19–25. https://doi.org/10.1016/j.colsurfb.2012.05.029
Wang H, Suo JQ, Wang CY, Wang RW (2020) Glucose oxidase immobilization with amino dendritic mesoporous silica nanoparticles and its application in glucose detection. Chem J Chin Univ Chin 41(8):1731–1738. https://doi.org/10.7503/cjcu20200146
Gunzer G, Hennrich N (1984) Purification of alpha-1-proteinase Inhibitor by Triazine dye affinity-chromatography, ion-exchange chromatography and gel-filtration on fractogel TSK. J Chromatogr 296:221–229. https://doi.org/10.1016/s0021-9673(01)96415-5
Lin P, Zhang YH, Yao GX, Huo HY, Ren H, Wang YX, Wang SZ, Fang BS (2019) Immobilization of formate dehydrogenase on polyethylenimine-grafted graphene oxide with kinetics and stability study. Eng Life Sci. https://doi.org/10.1002/elsc.201900134
Wang Y, Wang Q, Song X, Cai J (2019) Hydrophilic polyethylenimine modified magnetic graphene oxide composite as an efficient support for dextranase immobilization with improved stability and recyclable performance. Biochem Eng J 141:163–172. https://doi.org/10.1016/j.bej.2018.10.015
Weng Y, Jiang B, Yang K, Sui Z, Zhang L, Zhang Y (2015) Polyethyleneimine-modified graphene oxide nanocomposites for effective protein functionalization. Nanoscale 7(34):14284–14291. https://doi.org/10.1039/c5nr03370e
Cheng C, Nie SQ, Li S, Peng H, Yang H, Ma L, Sun SD, Zhao CS (2013) Biopolymer functionalized reduced graphene oxide with enhanced biocompatibility via mussel inspired coatings/anchors. J Mater Chem B 1(3):265–275. https://doi.org/10.1039/c2tb00025c
Sharifi M, Sohrabi MJ, Hosseinali SH, Hasan A, Kani PH, Talaei AJ, Karim AY, Nanakali NMQ, Salihi A, Aziz FM, Yan B, Khan RH, Saboury AA, Falahati M (2020) Enzyme immobilization onto the nanomaterials: application in enzyme stability and prodrug-activated cancer therapy. Int J Biol Macromol 143:665–676. https://doi.org/10.1016/j.ijbiomac.2019.12.064
Ren H, Zhang Y, Su J, Lin P, Wang B, Fang B, Wang S (2017) Encapsulation of amine dehydrogenase in hybrid titania nanoparticles by polyethylenimine coating and templated biomineralization. J Biotechnol 241:33–41. https://doi.org/10.1016/j.jbiotec.2016.11.006
Pazur JH, Kleppe K (1964) Oxidation of glucose and related compounds by glucose oxidase from Aspergillus Niger. Biochemistry 3(4):578–580. https://doi.org/10.1021/bi00892a018
Cheng KW, Zhang Y, Li YJ, Gao ZG, Chen FH, Sun K, An PJ, Sun C, Jiang Y, Sun BW (2019) A novel pH-responsive hollow mesoporous silica nanoparticle (HMSN) system encapsulating doxorubicin (DOX) and glucose oxidase (GOX) for potential cancer treatment. J Mater Chem B 7(20):3291–3302. https://doi.org/10.1039/c8tb03198c
Jia HF, Zhu GY, Wang P (2003) Catalytic behaviors of enzymes attached to nanoparticles: the effect of particle mobility. Biotechnol Bioeng 84(4):406–414. https://doi.org/10.1002/bit.10781
Ramakrishna TRB, Nalder TD, Yang WR, Marshall SN, Barrow CJ (2018) Controlling enzyme function through immobilisation on graphene, graphene derivatives and other two dimensional nanomaterials. J Mater Chem B 6(20):3200–3218. https://doi.org/10.1039/c8tb00313k
Szefler B, Diudea MV, Grudzinski IP (2016) Nature of polyethyleneimine-glucose oxidase interactions. Stud Univ Babes-Bolyai, Chem 61(1):249–260
D’Auria S, Marín-Navarro J, Roupain N, Talens-Perales D, Polaina J (2015) Identification and structural analysis of amino acid substitutions that increase the stability and activity of Aspergillus niger glucose oxidase. PLoS ONE 10(12):e0144289. https://doi.org/10.1371/journal.pone.0144289
Kouassi GK, Irudayaraj J, McCarty G (2005) Activity of glucose oxidase functionalized onto magnetic nanoparticles. Biomagn Res Technol 3(1):1. https://doi.org/10.1186/1477-044x-3-1
Gouda MD, Singh SA, Rao AGA, Thakur MS, Karanth NG (2003) Thermal inactivation of glucose oxidase - mechanism and stabilization using additives. J Biol Chem 278(27):24324–24333. https://doi.org/10.1074/jbc.M208711200
Eremin AN, Metelitsa DI, Shishko ZF, Mikhailova RV, Yasenko MI, Lobanok AG (2001) Thermal stability of glucose oxidase from Penicillium adametzii. Appl Biochem Microbiol 37(6):578–586. https://doi.org/10.1023/a:1012398900194
Bayramoglu G, Denizli A, Arica MY (2002) Membrane with incorporated hydrophobic ligand for hydrophobic interaction with proteins: application to lipase adsorption. Polym Int 51(10):966–972. https://doi.org/10.1002/pi.899
Rodrigues RC, Ortiz C, Berenguer-Murcia A, Torres R, Fernandez-Lafuente R (2013) Modifying enzyme activity and selectivity by immobilization. Chem Soc Rev 42(15):6290–6307. https://doi.org/10.1039/c2cs35231a
Willner I, Baron R, Willner B (2007) Integrated nanoparticle-biomolecule systems for biosensing and bioelectronics. Biosens Bioelectron 22(9–10):1841–1852. https://doi.org/10.1016/j.bios.2006.09.018
Zhou L, Jiang Y, Gao J, Zhao X, Ma L, Zhou Q (2012) Oriented immobilization of glucose oxidase on graphene oxide. Biochem Eng J 69:28–31. https://doi.org/10.1016/j.bej.2012.07.025
Zhou L, Jiang Y, Gao J, Zhao X, Ma L (2012) Graphene oxide as a matrix for the immobilization of glucose oxidase. Appl Biochem Biotechnol 168(6):1635–1642. https://doi.org/10.1007/s12010-012-9884-4
Cooper CL, Dubin PL, Kayitmazer AB, Turksen S (2005) Polyelectrolyte-protein complexes. Curr Opin Coll Interface Sci 10(1–2):52–78. https://doi.org/10.1016/j.cocis.2005.05.007
Wang Y, Wang Q, Song X, Cai J (2018) Improving the stability and reusability of dextranase by immobilization on polyethylenimine modified magnetic particles. New J Chem 42(11):8391–8399. https://doi.org/10.1039/c8nj00227d
An JD, Patterson DA, McNeil S, Hossain MM (2014) Immobilization of lipase on woolen fabrics: enhanced effectiveness in stain removal. Biotechnol Prog 30(4):806–817. https://doi.org/10.1002/btpr.1912
Dreyer DR, Todd AD, Bielawski CW (2014) Harnessing the chemistry of graphene oxide. Chem Soc Rev 43(15):5288–5301. https://doi.org/10.1039/c4cs00060a
Hill A, Karboune S, Mateo C (2017) Investigating and optimizing the immobilization of levansucrase for increased transfructosylation activity and thermal stability. Process Biochem 61:63–72. https://doi.org/10.1016/j.procbio.2017.06.011
Torres R, Mateo C, Fuentes M, Palomo JM, Ortiz C, Fernandez-Lafuente R, Guisan JM (2002) Reversible immobilization of invertase on Sepabeads coated with polyethyleneimine: optimization of the biocatalyst’s stability. Biotechnol Prog 18(6):1221–1226. https://doi.org/10.1021/bp020082q
Acknowledgements
This work was financially supported by GEMNS project funded by the European Union’s Seventh Framework Program under ERA NET EuroNanoMed II European Innovative Research and Technological Development Projects in Nanomedicine (NCBR Funding No. 08/09/10/ EuroNanoMed/2015). A part of this work was also supported by TEPCAN project funded by the Program "Applied research" under the Norwegian Financial Mechanisms 2014 – 2021/POLNOR 2019 (EEA and Norway Grants), Thematic areas: Welfare, health and care (NCBR Funding No. NOR/POLNOR/TEPCAN/0057/2019-00).
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Conflict of interest
There are no conflicts to declare.
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Bamburowicz-Klimkowska, M., Kasprzak, A., Bystrzejewski, M. et al. Characteristics of glucose oxidase immobilized on carbon-encapsulated iron nanoparticles decorated with polyethyleneimine. Polym. Bull. 80, 1565–1586 (2023). https://doi.org/10.1007/s00289-022-04125-1
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00289-022-04125-1