Abstract
In today’s world, there is a wide array of materials engineered at the nano- and microscale, with numerous applications attributed to these innovations. This review aims to provide a concise overview of how nano- and micromaterials are utilized for enzyme immobilization. Enzymes act as eco-friendly biocatalysts extensively used in various industries and medicine. However, their widespread adoption faces challenges due to factors such as enzyme instability under different conditions, resulting in reduced effectiveness, high costs, and limited reusability. To address these issues, researchers have explored immobilization techniques using nano- and microscale materials as a potential solution. Such techniques offer the promise of enhancing enzyme stability against varying temperatures, solvents, pH levels, pollutants, and impurities. Consequently, enzyme immobilization remains a subject of great interest within both the scientific community and the industrial sector. As of now, the primary goal of enzyme immobilization is not solely limited to enabling reusability and stability. It has been demonstrated as a powerful tool to enhance various enzyme properties and improve biocatalyst performance and characteristics. The integration of nano- and microscale materials into biomedical devices is seamless, given the similarity in size to most biological systems. Common materials employed in developing these nanotechnology products include synthetic polymers, carbon-based nanomaterials, magnetic micro- and nanoparticles, metal and metal oxide nanoparticles, metal–organic frameworks, nano-sized mesoporous hydrogen-bonded organic frameworks, protein-based nano-delivery systems, lipid-based nano- and micromaterials, and polysaccharide-based nanoparticles.
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References
Ahmad R, Sardar M (2015) Enzyme immobilization: an overview on nanoparticles as immobilization matrix. Anal Biochem 4:178–186. https://doi.org/10.4172/2161-1009.1000178
Ahmed S, Saifullah AM, Swami BL, Ikram S (2016) Green synthesis of silver nanoparticles using Azadirachta indica aqueous leaf extract. J Radiation Res Appl Sci 9(1):1–7. https://doi.org/10.1016/j.jrras.2015.06.006
Alshammari GM, Al-Ayed MS, Abdelhalim MA, Al-Harbi LN, Qasem AA, Yahya MA (2023) Development of luminescence carbon quantum dots for metal ions detection and photocatalytic degradation of organic dyes from aqueous media. Environ Res 226:115661. https://doi.org/10.1016/j.envres.2023.115661
Altinkaynak C, Kocazorbaz E, Özdemir N, Zihnioglu F (2018) Egg white hybrid nanoflower (EW-hNF) with biomimetic polyphenol oxidase reactivity: synthesis, characterization and potential use in decolorization of synthetic dyes. Int J Biol Macromol 109:205–211. https://doi.org/10.1016/j.ijbiomac.2017.12.072
Altinkaynak C, Tavlasoglu S, Kalin R, Sadeghian N, Ozdemir H, Ocsoy I, Özdemir N (2017) A hierarchical assembly of flower-like hybrid Turkish black radish peroxidase-Cu2+ nanobiocatalyst and its effective use in dye decolorization. Chemosphere 182:122–128. https://doi.org/10.1016/j.chemosphere.2017.05.01
Altinkaynak C, Tavlasoglu S, Ozdemir N, Ocsoy I (2016) A new generation approach in enzyme immobilization: organic-inorganic hybrid nanoflowers with enhanced catalytic activity and stability. Enzyme Microb Technol 93–94:105–112. https://doi.org/10.1016/j.enzmictec.2016.06.011
Amari A, Alzahrani FM, Alsaiari NS, Katubi KM, Rebah FB, Tahoon MA (2021) Magnetic metal organic framework immobilized laccase for wastewater decolorization. Processes 9:774–788. https://doi.org/10.3390/pr9050774
Amirfazli A (2007) Nanomedicine: magnetic nanoparticles hit the target. Nat Nanotechnol 2:467–468. https://doi.org/10.1038/nnano.2007.234
An J, Li G, Zhang Y, Zhang T, Liu X, Gao F, Peng M, He Y, Fan H (2020) Recent advances in enzyme-nanostructure biocatalysts with enhanced activity. Catalysts 10(3):338. https://doi.org/10.3390/catal10030338
Andersson MM, Hatti-Kaul R (1999) Protein stabilising effect of polyethyleneimine. J Biotechnol 72:21–31. https://doi.org/10.1016/S0168-1656(99)00050-4
Ansari SA, Husain Q (2012) Potential applications of enzymes immobilized on/in nano materials: a review. Biotechnol Adv 30:512–523. https://doi.org/10.1016/j.biotechadv.2011.09.005
Anwar A, Imran M, Iqbal HMN (2023) Smart chemistry and applied perceptions of enzyme-coupled nano-engineered assemblies to meet future biocatalytic challenges. Coord Chem Rev 493:215329. https://doi.org/10.1016/j.ccr.2023.215329
Arana-Pena S, Carballares D, Morellon-Sterlling R, Berenguer-Murcia A, Alcantara AR, Rodrigues RC, Fernandez-Lafuente R (2020) Enzyme co-immobilization: always the biocatalyst designers choice…or not? Biotechnol Adv 107584–107621. https://doi.org/10.1016/j.biotechadv.2020.107584
Artyukhov VG, Kovaleva TA, Kholyavka MG, Bityutskaya LA, Grechkina MV (2010) Thermal inactivation of free and immobilized inulinase. Appl Biochem Microbiol 46:385–389. https://doi.org/10.1134/S0003683810040034
Asgher M, Shahid M, Kamal S, Iqbal HMN (2014) Recent trends and valorization of immobilization strategies and ligninolytic enzymes by industrial biotechnology. J Mol Catal B: Enzym 101:56–66. https://doi.org/10.1016/j.molcatb.2013.12.016
Ashmarina LI, Muronetz VI, Nagradova NK (1984) Immobilized glyceraldehyde-3-phosphate dehydrogenase forms a complex with phosphoglycerate kinase. Biochem Int 9:511–521
Assa F, Jafarizadeh-Malmiri H, Ajamein H, Vaghari H, Anarjan N, Ahmadi O, Berenjian A (2017) Crit Rev Biotechnol 37(4):492–509. https://doi.org/10.1080/07388551.2016.1185389
Ayub J, Saeed MU, Hussain N, Zulfiqar I, Mehmood T, Iqbal HMN, Bilal M (2023) Designing robust nano-biocatalysts using nanomaterials as multifunctional carriers - expanding the application scope of bio-enzymes. Top Catal 66:625–648. https://doi.org/10.1007/s11244-022-01657-8
Baluta S, Lesiak A, Cabaj J (2018) Graphene quantum dots-based electrochemical biosensor for catecholamine neurotransmitters detection. Electroanalysis 30(8):1781–1790. https://doi.org/10.1002/elan.201700825
Barbosa O, Ortiz C, Berenguer-Murcia A, Torres R, Rodrigues RC, Fernandez-Lafuente R (2015) Strategies for the one-step immobilization–purification of enzymes as industrial biocatalysts Biotechnol. Adv 33:435–456. https://doi.org/10.1016/j.biotechadv.2015.03.006
Barrat J-L, Joanny F (1995) Theory of Polyelectrolyte Solutions. Wiley-Blackwell, Hoboken, NJ. https://arxiv.org/pdf/cond-mat/9601022.pdf
Batule BS, Park KS, Kim MI, Park HG (2015) Ultrafast sonochemical synthesis of protein-inorganic nanoflowers. Int J Nanomedicine 10:137–142. https://doi.org/10.2147/IJN.S90274
Bekhit AA, Hopkins DL, Geesink G, Bekhit AA, Franks P (2014) Exogenous proteases for meat tenderization. Crit Rev Food Sci Nutr 54:1012–1031. https://doi.org/10.1080/10408398.2011.623247
Besteti MD, Cunha AG, Freire DMG, Pinto JC (2014) Core/Shell polymer particles by semibatch combined suspension/emulsion polymerizations for enzyme immobilization. Macromol Mater Eng 299:135–143. https://doi.org/10.1002/mame.201300023
Bhavsar MD, Amiji MM (2007) Gastrointestinal distribution and in vivo gene transfection studies with nanoparticles-in-microsphere oral system (NiMOS). J Control Release 119:339–348. https://doi.org/10.1016/j.jconrel.2007.03.006
Bie J, Sepodes B, Fernandes PCB, Ribeiro MHL (2022) Enzyme immobilization and co-immobilization: main framework, advances and some applications. Processes 10(3):494–525. https://doi.org/10.3390/pr10030494
Bilal M, Asgher M, Shah SZH, Iqbal HMN (2019) Engineering enzyme-coupled hybrid nanoflowers: the quest for optimum performance to meet biocatalytic challenges and opportunities. Int J Biol Macromol 135:677–690. https://doi.org/10.1016/j.ijbiomac.2019.05.206
Bilal M, Hussain N, Juliana A-P, Almulaiky YQ, Iqbal HMN (2021) Multi-enzyme co-immobilized nano-assemblies: bringing enzymes together for expanding bio-catalysis scope to meet biotechnological challenges. Int J Biol Macromol 186:735–749. https://doi.org/10.1016/j.ijbiomac.2021.07.064
Bilal M, Rashid EU, Munawar J, Iqbal HMN, Cui J, Zdarta J, Ashraf SS, Jesionowski T (2023) Magnetic metal-organic frameworks immobilized enzyme-based nano-biocatalytic systems for sustainable biotechnology. Int J Biol Macromol 237:123968–123986. https://doi.org/10.1016/j.ijbiomac.2023.123968
Biro E, Nemeth AS, Sisak C, Feczko T, Gyenis J (2008) J Biochem Biophys Methods 70:1240–1246. https://doi.org/10.1016/j.jprot.2007.11.005
Blazek T, Gorski W (2020) Oxidases, carbon nanotubes, and direct electron transfer: a cautionary tale. Biosens Bioelectron 163:112260–112266. https://doi.org/10.1016/j.bios.2020.112260
Bolivar JM, Rocha-Martin J, Mateo C, Cava F, Berenguer J, Fernandez-Lafuente R, Guisan JM (2009) Coating of soluble and immobilized enzymes with ionic polymers: full stabilization of the quaternary structure of multimeric enzymes. Biomacromol 10(4):742–747. https://doi.org/10.1021/bm801162e
Boussema F, Gross AJ, Hmida F, Ayed B, Majdoub H, Cosnier S, Maaref A, Holzinger M (2018) Dawson-type polyoxometalate nanoclusters confined in a carbon nanotube matrix as efficient redox mediators for enzymatic glucose biofuel cell anodes and glucose biosensors. Biosens Bioelectron 109:20–26. https://doi.org/10.1016/j.bios.2018.02.060
Brady D, Jordaan J (2009) Advances in enzyme immobilization. Biotechnol Lett 31:1639–1650. https://doi.org/10.1007/s10529-009-0076-4
Brahim FB, Boughzala H (2013) Crystal structure, vibrational spectra and thermal analysis of a new centrosymmetric transition metal phosphate compound, Mn(H2PO4)2·4H2O. J Mol Struct 1034:336–345. https://doi.org/10.1016/j.molstruc.2012.10.050
Britton J, Majumdar S, Weiss GA (2018) Continuous flow biocatalysis. Chem Soc Rev 47:5891–5918. https://doi.org/10.1039/c7cs00906b
Butterworth M, Illum L, Davis S (2001) Preparation of ultrafine silica- and peg-coated magnetite particles. Colloids Surf A Physicochem Eng Asp 179(1):93–102. https://doi.org/10.1016/S0927-7757(00)00633-6
Canevari TC, Cincotto FH, Gomes D, Landers R, Toma HE (2017) Magnetite nanoparticles bonded carbon quantum dots magnetically confined onto screen printed carbon electrodes and their performance as electrochemical sensor for NADH. Electroanalysis 29(8):1968–1975. https://doi.org/10.1002/elan.201700167
Cantone S, Ferrario V, Corici L, Ebert C, Fattor D, Spizzo P, Gardossi L (2013) Efficient immobilization of industrial biocatalysts: criteria and constraints for the selection of organic polymeric carriers and immobilization methods. Chem Soc Rev 42:6262–6276. https://doi.org/10.1039/c3cs35464d
Castelló J, Gallardo M, Busquets MA, Estelrich J (2015) Chitosan (or alginate)-coated iron oxide nanoparticles: a comparative study. Colloids Surf A Physicochem Eng Asp 468:151–158. https://doi.org/10.1016/j.colsurfa.2014.12.031
Castner DG, Ratner BD (2002) Biomedical surface science: foundations to frontiers. Surface Sci 500(1–3):28–60. https://doi.org/10.1016/S0039-6028(01)01587-4
Celik C, Tasdemir D, Demirbas A, Kati A, Gul OT, Cimen B, Ocsoy I (2018) Formation of functional nanobiocatalysts with a novel and encouraging immobilization approach and their versatile bioanalytical applications. RSC Adv 8:25298–25303. https://doi.org/10.1039/c8ra03250e
Chalkias NG, Kahawong P, Giannelis EP (2008) Activity increase of horseradish peroxidase in the presence of magnetic particles. J Am Chem Soc 130:2910–2911. https://doi.org/10.1021/ja7102263
Chastellain M, Petri A, Hofmann H (2004) Particle size investigations of a multistep synthesis of PVA coated superparamagnetic nanoparticles. J Colloid Interface Sci 278:353–360. https://doi.org/10.1016/j.jcis.2004.06.025
Chavali MS, Nikolova MP (2019) Metal oxide nanoparticles and their applications in nanotechnology. SN Appl Sci 1:607–637. https://doi.org/10.1007/s42452-019-0592-3
Chen G, Huang S, Kou X, Zhu F, Ouyang G (2020) Embedding functional biomacromolecules within peptide-directed metal-organic framework (MOF) nanoarchitectures enables activity enhancement. Angew Chem Int Ed 59:13947–13954. https://doi.org/10.1002/anie.202005529
Chen G, Tong L, Huang S, Huang S, Zhu F, Ouyang G (2022) Hydrogen-bonded organic framework biomimetic entrapment allowing non-native biocatalytic activity in enzyme. Nat Commun 13:4816. https://doi.org/10.1038/s41467-022-32454-2
Chen H, Zhang J, Dang Y, Shu G (2014) Optimization for immobilization of β-galactosidase using plackett-burman design and steepest ascent method. J Chem Pharm Res 6(4):612–616. https://doi.org/10.1016/j.enzmictec.2011.06.010
Chen L, Remondetto GE, Subirade M (2006) Food protein-based materials as nutraceutical delivery systems. Trends Food Sci Technol 17:272–283. https://doi.org/10.1016/j.tifs.2005.12.011
Chen SX, Schopfer P (1999) Hydroxyl-radical production in physiological reactions: a novel function of peroxidase. Eur J Biochem 260:726–735. https://doi.org/10.1046/j.1432-1327.1999.00199.x
Cheng C, Chang KC (2013) Development of immobilized cellulase through functionalized gold nano-particles for glucose production by continuous hydrolysis of waste bamboo chopsticks. Enzyme Microb Technol 53:444–451. https://doi.org/10.1016/j.enzmictec.2013.09.010
Cherednikova TV, Muronetz VI, Nagradova NK (1980) Study of subunit interactions in immobilized d-glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta (BBA) - Enzymol 613:292–308. https://doi.org/10.1016/0005-2744(80)90084-4
Ciancaglini P, Simão AMS, Bolean M, Millán JL, Rigos CF, Yoneda JS, Colhone MC, Stabeli RG (2012) Proteoliposomes in nanobiotechnology. Biophys Rev 4:67–81. https://doi.org/10.1007/s12551-011-0065-4
Cipolatti EP, Silva MJA, Klein M, Feddern V, Feltes MMC, Oliveira JV, Ninow JL, de Oliveira D (2014a) Current status and trends in enzymatic nanoimmobilization. J Mol Catal b: Enzym 99:56–67. https://doi.org/10.1016/j.molcatb.2013.10.019
Cipolatti EP, Valerio A, Henriques RO, Moritz DE, Ninow JL, Freire DMG, Manoel EA, Fernandez-Lafuente R, de Oliveira D (2016) Nanomaterials for biocatalyst immobilization - state of the art and future trends. RSC Adv 6:104675–104692. https://doi.org/10.1039/c6ra22047a
Cipolatti EP, Valerio A, Nicoletti G, Theilacker E, Araujo PHH, Sayer C, Ninow JL, de Oliveira D (2014b) Immobilization of Candida antarctica lipase B on PEGylated poly(urea-urethane) nanoparticles by step miniemulsion polymerization. J Mol Catal B: Enzym 109:116–121. https://doi.org/10.1016/j.molcatb.2014.08.017
Costa SA, Tzanov T, Carneiro AF, Paar A, Gübitz GM, Cavaco-Paulo A (2002) Studies of stabilization of native catalase using additives. Enzyme Microb Technol 30:387–391. https://doi.org/10.1016/S0141-0229(01)00505-1
Cui J, Feng Y, Lin T, Tan Z, Zhong C, Jia S (2017) Mesoporous metal-organic framework with well-defined cruciate flower-like morphology for enzyme immobilization. ACS Appl Mater Interfaces 9(12):10587–10594. https://doi.org/10.1021/acsami.7b00512
Cui J, Jia S (2017) Organic-inorganic hybrid nanoflowers: a novel host platform for immobilizing biomolecules. Coord Chem Rev 352:249–263. https://doi.org/10.1016/j.ccr.2017.09.008
Cui J, Zhao Y, Liu R, Zhong C, Jia S (2016) Surfactant-activated lipase hybrid nanoflowers with enhanced enzymatic performance. Sci Rep 6:27928–27941. https://doi.org/10.1038/srep27928
Cui L, Li C-C, Tang B, Zhang C-Y (2018) Advances in the integration of quantum dots with various nanomaterials for biomedical and environmental applications. Analyst 143(11):2469–2478. https://doi.org/10.1039/c8an00222c
da Silva AL, Cruz FF, Rocco PRM, Morales MM (2017) New perspectives in nanotherapeutics for chronic respiratory diseases. Biophys Rev 9:793–803. https://doi.org/10.1007/s12551-017-0319-x
Das MC, Pal SC, Chen B (2022) Emerging microporous HOF materials to address global energy challenges. Joule 6:22–27. https://doi.org/10.1016/j.joule.2021.12.005
Dedania SR, Patel VK, Soni SS, Patel DH (2020) Immobilization of Agrobacterium tumefaciens D-psicose 3-epimerase onto 462 titanium dioxide for bioconversion of rare sugar. Enzyme Microb Technol 140:109605. https://doi.org/10.1016/j.enzmictec.2020.109605
Diab R, Jaafar-Maalej C, Fessi H, Maincent Ph (2012) Engineered nanoparticulate drug delivery systems: the next frontier for oral administration? AAPS J 14:688–702. https://doi.org/10.1208/s12248-012-9377-y
Dogan D, Sezer S, Ulu A, Köytepe S, Ateş B (2021) Preparation and characterization of amino-functionalized Zeolite/SiO2 materials for trypsin-chymotrypsin co-immobilization. Catal Lett 151(8):2463–2477. https://doi.org/10.1007/s10562-021-03636-2
Doherty CM, Buso D, Hill AJ, Furukawa S, Kitagawa S, Falcaro P (2014) Using functional nano- and microparticles for the preparation of metal-organic framework composites with novel properties. Acc Chem Res 47:396–405. https://doi.org/10.1021/ar400130a
Donald A (2004) Food for thought. Nat Mater 3:579–581. https://doi.org/10.1038/nmat1207
Doonan C, Ricco R, Liang K, Bradshaw D, Falcaro P (2017) Metal-organic frameworks at the biointerface: synthetic strategies and applications. Acc Chem Res 50:1423–1432. https://doi.org/10.1021/acs.accounts.7b00090
Drifford M, Delsanti M (2001) Polyelectrolyte solutions with multivalent added salts: stability, structure, and dynamics. physical chemistry of polyelectrolytes. Marcel Dekker, New York, pp 135–162. https://www.taylorfrancis.com/chapters/edit/10.1201/9781482270686-6/polyelectrolyte-solutions-multivalent-addedsalts-stability-structure-dynamics-maurice-drifford-michel-delsanti
Du Y, Jia X, Zhong L, Jiao Y, Zhang Z, Wang Z, Feng Y, Bilal M, Cui J, Jia S (2022) Metal-organic frameworks with different dimensionalities: An ideal host platform for enzyme@MOF composites. Coord Chem Rev 454:214327. https://doi.org/10.1016/j.ccr.2021.214327
Egebro Birk S, Boisen A, Hagner NL (2021) Polymeric nano- and microparticulate drug delivery systems for treatment of biofilms. Adv Drug Deliv Rev 174:30–52. https://doi.org/10.1016/j.addr.2021.04.005
Elzoghby AO, Abo El-Fotoh WS, Elgindy NA (2011) Casein-based formulations as promising controlled release drug delivery systems. J Control Release 153:206–216. https://doi.org/10.1016/j.jconrel.2011.02.010
Elzoghby AO, Samy WM, Elgindy NA (2012) Albumin-based nanoparticles as potential controlled release drug delivery systems. J Control Release 167:168–182. https://doi.org/10.1016/j.jconrel.2011.07.031
Emerich DF, Snodgrass P, Lafreniere D, Dean RL, Salzberg H, Marsh J, Perdomo B, Arastu M, Winn SR, Bartus RT (2002) Sustained release chemotherapeutic microspheres provide superior efficacy over systemic therapy and local bolus infusions. Pharm Res 19:1052–1060. https://doi.org/10.1023/a:1016434926649
Escobar S, Velasco-Lozano S, Lu CH, Lin YF, Mesa M, Bernal C, Lopez-Gallego F (2017) Understanding the functional properties of bio-inorganic nanoflowers as biocatalysts by deciphering the metal-binding sites of enzymes. J Mater Chem B 5:4478–4486. https://doi.org/10.1039/x0xx00000x
Fadnis AG, Kulshrestha SK (1982) Kinetics of oxidation of adonitol by manganese (III) pyrophosphate. React Kinet Catal Lett 19:267–269. https://doi.org/10.1007/BF02074043
Faizullin D, Valiullina Y, Salnikov V, Zelenikhin P, Zuev Y, Ilinskaya O (2023) Fibrin-rhamnogalacturonan I composite Gel for therapeutic enzyme delivery to intestinal tumors. Int J Mol Sci 24:926. https://doi.org/10.3390/ijms24020926
Fändrich M, Fletcher MA, Dobson CM (2001) Amyloid fibrils from muscle myoglobin. Nature 410:165. https://doi.org/10.1038/35065514
Faraji AH, Wipf P (2009) Nanoparticles in cellular drug delivery. Bioorg Med Chem 17:2950–2962. https://doi.org/10.1016/j.bmc.2009.02.043
Fathi M, Karim M, Khoigani SR, Mosayebi V (2019) Bioactive molecules in food: use of nanotechnology for immobilization and entrapment of food applicable enzymes. Springer, Cham, pp 2037–2061. https://doi.org/10.1007/978-3-319-78030-652
Feng Y, Du Y, Kuang G, Zhong L, Hu H, Jia S, Cui J (2022) Hierarchical micro- and mesoporous ZIF-8 with core-shell superstructures using colloidal metal sulfates as soft templates for enzyme immobilization. J Colloid Interface Sci 610:709–718. https://doi.org/10.1016/j.jcis.2021.11.123
Feng Y, Hu H, Wang Z, Du Y, Zhong L, Zhang C, Jiang Y, Jia S, Cui J (2021) Three-dimensional ordered magnetic macroporous metal-organic frameworks for enzyme immobilization. J Colloid Interface Sci 590:436–445. https://doi.org/10.1016/j.jcis.2021.01.078
Ferdov S, Lopes AM, Lin Z, Ferreira RAS (2007) New template-free layered manganese (III) phosphate: hydrothermal synthesis, ab initio structural determination, and magnetic properties. Chem Mater 19:6025–6029. https://doi.org/10.1021/Cm701951w
Fotiadou R, Patila M, Hammami MA, Enotiadis A, Moschovas D, Tsirka K, Spyrou K, Giannelis EP, Avgeropoulos A, Paipetis A, Gournis D, Stamatis H (2019) Development of effective lipase-hybrid nanoflowers enriched with carbon and magnetic nanomaterials for biocatalytic transformations. Nanomaterials 9(6):808–825. https://doi.org/10.3390/nano9060808
Fu M, Xing JZ, Ge Z (2019) Preparation of laccase-loaded magnetic nanoflowers and their recycling for efficient degradation of bisphenol A. Sci Total Environ 65:2857–2865. https://doi.org/10.1016/j.scitotenv.2018.10.145
Gao X, Zhai Q, Hu M, Li S, Jiang Y (2021) Hierarchically porous magnetic Fe3O4/Fe-MOF used as an effective platform for enzyme immobilization: a kinetic and thermodynamic study of structure-activity. Catal Sci Technol 11:2446–2455. https://doi.org/10.1039/D0CY02146F
Garcia-Galan C, Barbosa O, Hernandez K, dos Santos JCS, Rodrigues RC, Fernandez-Lafuente R (2014) Evaluation of styrene-divinylbenzene beads as a support to immobilize lipases. Molecules 19:7629–7645. https://doi.org/10.3390/molecules19067629
Ge J, Lei J, Zare RN (2012) Protein–inorganic hybrid nanoflowers. Nat Nanotechnol 7:428–432. https://doi.org/10.1038/nnano.2012.80
Ge MY, Han LY, Wiedwald U, Xu XB, Wang C, Kuepper K, Ziemann P, Jiang JZ (2010) Monodispersed NiO nanoflowers with anomalous magnetic behavior. Nanotechnology 21:425702–425707. https://doi.org/10.1088/0957-4484/21/42/425702
Gentil S, Lalaoui N, Dutta A, Nedellec Y, Cosnier S, Shaw WJ, Artero V, Le Goff A (2017) Carbon-nanotube-supported bio-inspired nickel catalyst and its integration in hybrid hydrogen/air fuel cells. Angew Chem Int Ed 56(7):1845–1849. https://doi.org/10.1002/anie.201611532
Georgakilas V, Tiwari JN, Kemp KC, Perman JA, Bourlinos AB, Kim KS, Zboril R (2016) Noncovalent Functionalization of Graphene and Graphene Oxide for Energy Materials, Biosensing, Catalytic, and Biomedical Applications. Chem Rev 116(9):5464–5519. https://doi.org/10.1021/acs.chemrev.5b00620
Ghosh S, Chaganti SR, Prakasham RS (2012) Polyaniline nanofiber as a novel immobilization matrix for the anti-leukemia enzyme l-asparaginase. J Mol Catal B: Enzym 74:132–137. https://doi.org/10.1016/j.molcatb.2011.09.009
Girigoswami A, Ramalakshmi M, Akhtar N, Metkar SK, Girigoswami K (2019) ZnO Nanoflower petals mediated amyloid degradation-an in vitro electrokinetic potential approach. Mater Sci Eng C 101:169–178. https://doi.org/10.1016/j.msec.2019.03.086
Gkantzou E, Chatzikonstantinou AV, Fotiadou R, Giannakopoulou A, Patila M, Stamatis H (2021) Trends in the development of innovative nanobiocatalysts and their application in biocatalytic transformations. Biotechnol Adv 51:107738–107764. https://doi.org/10.1016/j.biotechadv.2021.107738
Godbey WT, Wu KK, Mikos AG (1999) Poly(ethylenimine) and its role in gene delivery. J Control Release 60:149–160. https://doi.org/10.1016/s0168-3659(99)00090-5
Gokhale AA, Lu J, Lee I (2013) Immobilization of cellulase on magnetoresponsive graphene nano-supports. J Mol Catal b: Enzym 90:76–86. https://doi.org/10.1016/j.molcatb.2013.01.025
Gokhale KM, Walekar C, Manje S (2023) Novel curcumin analogues: synthesis and therapeutic applications. Curr Overview Pharm Sci 5:86–116. https://doi.org/10.9734/bpi/cops/v5/17813D
Goncharova SS, Redko YuA, Lavlinskaya MS, Sorokin AV, Holyavka MG, Kondratyev MS, Artyukhov VG (2023) Biocatalysts based on papain associates with chitosan nanoparticles. Condens Matter Interphases 25:173–181. https://doi.org/10.17308/kcmf.2023.25/11098
Gondwal M, Joshi nee Pant G (2018) Synthesis and catalytic and biological activities of silver and copper nanoparticles using Cassia occidentalis. International Journal of Biomaterials, 2018https://doi.org/10.1155/2018/6735426
González-García I, Solé RV, Costa J (2002) Metapopulation dynamics and spatial heterogeneity in cancer. Proc Natl Acad Sci U S A 99:13085-13089https://doi.org/10.1073/pnas.202139299
Gonzalez-Rabade N, Badillo-Corona JA, Aranda-Barradas JS, Oliver-Salvador MC (2011) Production of plant proteases in vivo and in vitro – a review. Biotechnol 29:983–996. https://doi.org/10.1016/j.biotechadv.2011.08.017
Gruber P, Marques MPC, O’Sullivan B, Baganz F, Wohlgemuth R, Szita N (2017) Conscious coupling: the challenges and opportunities of cascading enzymatic microreactors. Biotechnol J 12(7):1700030–1700043. https://doi.org/10.1002/biot.201700030
Gubaidullin AT, Makarova AO, Derkach SR, Voron’ko NG, Kadyirov AI, Ziganshina SA, Salnikov VV, Zueva OS, Zuev YuF (2022) Modulation of molecular structure and mechanical properties of k-carrageenan-gelatin hydrogel with multi-walled carbon nanotubes. Polymers 14:2346. https://doi.org/10.3390/polym14122346
Gupta N, Gupta SM, Sharma SK (2019) Carbon nanotubes: synthesis, properties and engineering applications. Carbon Lett 29(5):419–447. https://doi.org/10.1007/s42823-019-00068-2
Guzik U, Hupert-Kocurek K, Wojcieszynska D (2014) Immobilization as a strategy for improving enzyme properties-application to oxidoreductases. Molecules 19:8995–9018. https://doi.org/10.3390/molecules19078995
Hainfeld JF, Slatkin DN, Smilowitz HM (2004) The use of gold nanoparticles to enhance radiotherapy in mice. Phys Med Biol 49:309–315. https://doi.org/10.1088/0031-9155/49/18/n03
Han E, Yang H, He Z, Cai J, Zhang X, Dong X (2015) Development of tyrosinase biosensor based on quantum dots/chitosan nanocomposite for detection of phenolic compounds. Anal Biochem 486:102–106. https://doi.org/10.1016/j.ab.2015.07.001
Hartmann M, Kostrov X (2013) Immobilization of enzymes on porous silicas-Benefits and challenges. Chem Chem Soc Rev 42:6277–6289. https://doi.org/10.1039/c3cs60021a
Hermanova S, Zarevúcká M, Bouša D, Pumera M, Sofer Z (2015) Graphene oxide immobilized enzymes show high thermal and solvent stability. Nanoscale 7(13):5852–5858. https://doi.org/10.1039/c5nr00438
Hillyer JF, Albrecht RM (2001) Gastrointestinal persorption and tissue distribution of differently sized colloidal gold nanoparticles. J Pharm Sci 90:1927–1936. https://doi.org/10.1002/jps.1143
Hisaki I, Xin C, Takahashi K, Nakamura T (2019) Designing hydrogen-bonded organic frameworks (HOFs) with permanent porosity. Angew Chem Int Ed 58:11160–11170. https://doi.org/10.1002/anie.201902147
Holyavka MG, Artyukhov VG, Sazykina SM, Nakvasina MA (2017) Physical, chemical, and kinetic properties of trypsin-based heterogeneous biocatalysts immobilized on ion-exchange fiber matrices. Pharm Chem J 51:702–706. https://doi.org/10.1007/s11094-017-1678-0
Holyavka MG, Kondratyev MS, Lukin AN, Agapov BL, Artyukhov VG (2019) Immobilization of inulinase on KU-2 ion-exchange resin matrix. Int J Biol Macromol 138:681–692. https://doi.org/10.1016/j.ijbiomac.2019.07.132
Holyavka MG, Kondratyev MS, Samchenko AA, Kabanov AV, Komarov VM, Artyukhov VG (2016) In silico design of high-affinity ligands for the immobilization of inulinase. Comput Biol Med 71:198–204. https://doi.org/10.1016/j.compbiomed.2016.02.015
Homaei A, Saberi D (2015) Immobilization of α-amylase on gold nanorods: an ideal system for starch processing. Process Biochem 50:1394–1399. https://doi.org/10.1016/j.procbio.2015.06.002
Hu B, Huang Qr (2013) Biopolymer based nano-delivery systems for enhancing bioavailability of nutraceuticals. Chin J Polym Sci 31:1190–1203. https://doi.org/10.1007/s10118-013-1331-7
Hu C, Bai Y, Hou M, Wang Y, Wang L, Cao X, Chan C-W, Sun H, Li W, Ge J, Ren K (2020) Defect-induced activity enhancement of enzyme-encapsulated metal-organic frameworks revealed in microfluidic gradient mixing synthesis. Sci Adv. https://doi.org/10.1126/sciadv.aax5785
Hu H, Li P, Wang Z, Du Y, Kuang G, Feng Y, Jia S, Cui J (2022) glutamate oxidase-integrated biomimetic metal-organic framework hybrids as cascade nanozymes for ultrasensitive glutamate detection. J Agric Food Chem 70(12):3785–3794. https://doi.org/10.1021/acs.jafc.2c01639
Hu M, Giapis KP, Poulikakos D (2011) Interfacial mixing during annealing of zinc oxide nanoparticle junctions. Appl Phys Lett 98:211904–211907. https://doi.org/10.1063/1.3593487
Huang Q, Yu H, Ru Q (2010) Bioavailability and delivery of nutraceuticals using nanotechnology. J Food Sci 75:50–57. https://doi.org/10.1111/j.1750-3841.2009.01457.x
Huang S, Chen G, Ouyang G (2022) Confining enzymes in porous organic frameworks: from synthetic strategy and characterization to healthcare applications. Chem Soc Rev 51:6824–6863. https://doi.org/10.1039/d1cs01011e
Huang S, Kou X, Shen J, Chen G, Ouyang G (2020) Armoring the enzymes with metal-organic frameworks (MOFs). Angew Chem Int Ed 59:8786–8798. https://doi.org/10.1002/anie.201916474
Huang W-C, Wang W, Xue C, Mao X (2018) Effective enzyme immobilization onto a magnetic chitin nanofiber composite. ACS Sustain Chem Eng 6(7):8118–8124. https://doi.org/10.1021/acssuschemeng.8b01150
Huang Y, Zhao M, Han S, Lai Z, Yang J, Tan C, Ma Q, Lu Q, Chen J, Zhang X, Zhang Z, Li B, Chen B, Zong Y, Zhang H (2017) Growth of Au nanoparticles on 2D metalloporphyrinic metal-organic framework nanosheets used as biomimetic catalysts for cascade reactions. Adv Mater 29:1700102. https://doi.org/10.1002/adma.201700102
Huffman MA, Fryszkowska A, Alvizo O, Borra-Garske M, Campos KR, Canada KA, Devine PN, Duan D, Forstater JH, Grosser ST, Halsey HM, Hughes GJ, Jo J, Joyce LA, Kolev JN, Liang J, Maloney KM, Mann BF, Marshall NM, McLaughlin M, Moore JC, Murphy GS, Nawrat CC, Nazor J, Novick S, Patel NR, Rodriguez-Granillo A, Robaire SA, Sherer EC, Truppo MD, Whittaker AM, Verma D, Xiao L, Xu Y, Yang H (2019) Design of an in vitro biocatalytic cascade for the manufacture of islatravir. Science 366:1255–1259. https://doi.org/10.1126/science.aay8484
Husain S, Nandi A, Simnani FZ, Saha U, Ghosh A, Sinha A, Sahay A, Samal SK, Panda PK, Verma SK (2023) Emerging trends in advanced translational applications of silver nanoparticles: a progressing dawn of nanotechnology. J Funct Biomater 14:47–76. https://doi.org/10.3390/jfb14010047
Hwang ET, Gu MB (2013) Enzyme stabilization by nano/microsizedhybrid materials. Life Sci 13(1):49–61. https://doi.org/10.1002/elsc.201100225
Hwang ET, Lee S (2019) Multienzymatic cascade reactions via enzyme complex by immobilization. ACS Catal 9:4402–4425. https://doi.org/10.1021/acscatal.8b04921
Iftikhar FJ, Shah A, Akhter MS, Kurbanoglu S, Ozkan SA (2019) Introduction to nanosensors. In new developments in nanosensors for pharmaceutical analysis, сhapter 1. Cambridge, MA, pp 1–46. https://doi.org/10.1016/B978-0-12-816144-9.00001-8
Iijima S (1991) Helical microtubules of graphitic carbon. Nature 354:56–58. https://doi.org/10.1038/354056a0
Illum L, Farraj NF, Davis SS (1994) Chitosan as a novel nasal delivery system for peptide drugs. Pharm Res 11:1186–1189. https://doi.org/10.1023/a:1018901302450
Issaka E, Amu-Darko JNO, Adams M, Yakubu S, Gyimah E, Ali N, Cui J, Bilal M (2023) Zinc imidazolate metal–organic frameworks-8-encapsulated enzymes/nanoenzymes for biocatalytic and biomedical applications. Catal Lett 153:2083–2106. https://doi.org/10.1007/s10562-022-04140-x
Issaka E, Fapohunda FO, Amu-Darko JNO, Yeboah L, Yakubu S, Varjani S, Ali N, Bilal M (2022) Biocharbased composites for remediation of polluted wastewater and soil environments: challenges and prospects. Chemosphere 297:134163. https://doi.org/10.1016/J.CHEMOSPHERE.2022.134163
Jesionowski T, Zdarta J, Krajewska B (2014) Enzyme immobilization by adsorption: a review. Adsorption 20:801–821. https://doi.org/10.1007/s10450-014-9623-y
Jesorka A, Orwar O (2008) Liposomes: technologies and analytical applications. Annu Rev Anal Chem (Palo Alto Calif) 1:801–832. https://doi.org/10.1146/annurev.anchem.1.031207.112747
Ji P, Tan H, Xu X, Feng W (2010) Lipase covalently attached to multiwalled carbon nanotubes as an efficient catalyst in organic solvent. AIChE J 56(11):3005–3011. https://doi.org/10.1002/aic.12180
Ji Y, Wu Z, Zhang P, Qiao M, Hu Y, Shen B, Li B, Zhang X (2021) Enzyme-functionalized magnetic framework composite fabricated by one-pot encapsulation of lipase and Fe3O4 nanoparticle into metal-organic framework. Biochem Eng J 169:107962–107969. https://doi.org/10.1016/j.bej.2021.107962
Jiang H-L, Xu Q (2011) Porous metal-organic frameworks as platforms for functional applications. Chem Commun 47:3351–3370. https://doi.org/10.1039/c0cc05419d
Jiang J, Oberdörster G, Biswas P (2009) Characterization of size, surface charge, and agglomeration state of nanoparticle dispersions for toxicological studies. J Nanopart Res 11(1):77–89. https://doi.org/10.1007/s11051-008-9446-4
Jiang W, Wang X, Yang J, Han H, Li Q, Tang J (2018) Lipase-inorganic hybrid nanoflower constructed through biomimetic mineralization: a new support for biodiesel synthesis. J Colloid Interface Sci 514:102–107. https://doi.org/10.1016/j.jcis.2017.12.025
Jiang Y, Li Z, Zheng S, Xu H, Zhou YJ, Gao Z, Meng C, Li S (2020) Establishing an enzyme cascade for one-pot production of α-olefins from low-cost triglycerides and oils without exogenous H2O2 addition. Biotechnol Biofuels 13(1):52–63. https://doi.org/10.1186/s13068-020-01684-1
Jiang B, Yang К, Zhang L, Liang Z, Peng X, Zhang Y (2014) Dendrimer-grafted graphene oxide nanosheets as novel support for trypsin immobilization to achieve fast on-plate digestion of proteins. Talanta 122:278–284. https://doi.org/10.1016/j.talanta.2014.01.056
Jin K, Park J, Lee J, Yang KD, Pradhan GK, Sim U, Jeong D, Jang HL, Park S, Kim D, Sung NE, Kim SH, Han S, Nam KT (2014) Hydrated manganese (II) phosphate (Mn3(PO4)2·3H2O) as a water oxidation catalyst. J Am Chem Soc 136:7435–7443. https://doi.org/10.1021/ja5026529
Joshi HM, Bhumkar DR, Joshi K, Pokharkar V, Sastry M (2006) Gold nanoparticlesas carriers for efficient transmucosal insulin delivery. Langmuir 22:300–305. https://doi.org/10.1021/la051982u
Ju J, Li R, Gu S, Leader JK, Wang X, Chen Y, Zheng B, Wu S, Gur D, Sciurba F, Pu J (2014) Impact of emphysema heterogeneity on pulmonary function. PLoS One 9:e113320. https://doi.org/10.1371/journal.pone.0113320
Juang RS, Wu FC, Tseng RL (2001) Solute adsorption and enzyme immobilization on chitosan beads prepared from shrimp shell wastes. Bioresour Technol 80:187–193. https://doi.org/10.1016/s0960-8524(01)00090-6
Kalkan NA, Aksoy S, Aksoy EA, Hasirci N (2012) Preparation of chitosan-coated magnetite nanoparticles and application for immobilization of laccase. J Appl Polym Sci 123:707–716. https://doi.org/10.1002/app.34504
Kazenwadel F, Franzreb M, Rapp B (2015) Synthetic enzyme supercomplexes: coimmobilization of enzyme cascades. Anal Methods 7(10):4030–4037. https://doi.org/10.1039/C5AY00453E
Ke C, Fan Y, Chen Y, Xu L, Yan Y (2016) A new lipase-inorganic hybrid nanoflower with enhanced enzyme activity. RSC Adv 6:19413–19416. https://doi.org/10.1039/x0xx00000x
Khan HA, Shanker R (2015) Editorial Toxicity of Nanomaterialshttps://doi.org/10.1155/2015/521014
Khan IM, Niazi S, Akhtar W, Yue L, Pasha I, Khan MKI, Mohsin A, Iqbal MW, Zhang Y, Wang Z (2023) Surface functionalized AuNCs optical biosensor as an emerging food safety indicator: fundamental mechanism to future prospects. Coord Chem Rev 474:214842. https://doi.org/10.1016/j.ccr.2022.214842
Khorshidi KJ, Lenjannezhadian H, Jamalan M, Zeinali M (2016) Preparation and characterization of nanomagnetic cross-linked cellulase aggregates for cellulose bioconversion. J Chem Technol Biotechnol 91:539–546. https://doi.org/10.1002/jctb.4615
Kilic NM, Singh S, Keles G, Cinti S, Kurbanoglu S, Odaci D (2023) Novel approaches to enzyme-based electrochemical nanobiosensors. Biosensors 13(6):622. https://doi.org/10.3390/bios13060622
Kim K, Kim HJ, Oh DK, Cha SS, Rhee S (2006) Crystal structure of D-psicose 3-epimerase from Agrobacterium tumefaciens and its complex with true substrate D-fructose: a pivotal role of metal in catalysis, an active site for the nonphosphorylated substrate, and its conformational changes. J Mol Biol 361:920–931. https://doi.org/10.1016/j.jmb.2006.06.069
Kim KH, Jeong JM, Lee SJ, Choi BG, Lee KG (2016) Protein-directed assembly of cobalt phosphate hybrid nanoflowers. J Colloid Interface Sci 484:44–50. https://doi.org/10.1016/j.jcis.2016.08.059
Klein MP, Nunes MR, Rodrigues RC, Benvenutti EV, Costa TMH, Hertz PF, Ninow JL (2012) Effect of the support size on the properties of β-galactosidase immobilized on chitosan: advantages and disadvantages of macro and nanoparticles. Biomacromol 13:2456–2464. https://doi.org/10.1021/bm3006984
Kokufuta E, Takahashi K (1986) Adsorption of poly(diallyldimethylammonium chloride) on colloid silica from water and salt solution. Macromolecules 19:351–354. https://doi.org/10.1021/ma00156a019
Kopp W, da Costa TP, Pereira SC, Jr MJ, Giordano RC, Marques RFC, Araujo-Moreira FM, Giordano RLC (2014) Easily handling penicillin g acylase magnetic cross-linked enzymes aggregates: catalytic and morphological studies. Process Biochem 49:38-46.https://doi.org/10.1016/j.procbio.2013.09.024
Kumar A, Sevonkaev I, Goia DV (2014) Synthesis of selenium particles with various morphologies. J Colloid Interface Sci 416:119–123. https://doi.org/10.1016/j.jcis.2013.10.046
Laurienzo P (2010) Marine polysaccharides in pharmaceutical applications: an overview. Mar Drugs 8:2435–2465. https://doi.org/10.3390/md8092435
Lee HR, Chung M, Kim MI, Ha SH (2017) Preparation of glutaraldehyde-treated lipaseinorganic hybrid nanoflowers and their catalytic performance as immobilized enzymes. Enzym Microb Technol 105:24–29. https://doi.org/10.1016/j.enzmictec.2017.06.006
Lee SW, Cheon SA, Kim MI, Park TJ (2015) Organic-inorganic hybrid nanoflowers: types, characteristics, and future prospects. J Nanobiotechnol 13:54. https://doi.org/10.1186/s12951-015-0118-0
Lei Z, Gao C, Chen L, He Y, Ma W, Lin Z (2018) Recent advances in biomolecule immobilization based on self-assembly: organic-inorganic hybrid nanoflowers and metal-organic frameworks as novel substrates. J Mater Chem B 6:1581–1594. https://doi.org/10.1039/c7tb03310a
Leitgeb M, Knez Z, Vasic K (2016) In Micro and Nanotechnologies for Biotechnology: Micro- and nanocarriers for immobilization of enzymes. London, pp 1–38. https://doi.org/10.5772/63129
Li L, Xiang S, Cao S, Zhang J, Ouyang G, Chen L, Su CY (2013) A synthetic route to ultralight hierarchically micro/mesoporous Al(III)-carboxylate metal-organic aerogels. Nat Commun 4:1774-1773. https://doi.org/10.1038/ncomms2757
Li P, Moon SY, Guelta MA, Lin L, Gomez-Gualdron DA, Snurr RQ, Harvey SP, Hupp JT, Farha OK (2016) Nanosizing a metal-organic framework enzyme carrier for accelerating nerve agent hydrolysis. ACS Nano 10:9174–9182. https://doi.org/10.1021/acsnano.6b04996
Li W, Shi J, Chen Y, Liu X, Meng X, Guo Z, Li S, Zhang B, Jiang Z (2023) Nano-sized mesoporous hydrogen-bonded organic frameworks for in situ enzyme immobilization. Chem Eng J 468:143609. https://doi.org/10.1016/j.cej.2023.143609
Li X, Cao Y, Luo K, Sun Y, Xiong J, Wang L, Liu Z, Li J, Ma J, Ge J, Xiao H, Zare RN (2019a) Highly active enzyme–metal nanohybrids synthesized in protein–polymer conjugates. Nat Catal 2(8):718–725. https://doi.org/10.1038/s41929-019-0305-8
Li Y, Wan W (2017) Exploring Polymer Nanofiber Mechanics: a review of the methods for determining their properties. IEEE Nanotechnol Mag 11:16–28. https://doi.org/10.1109/MNANO.2017.2708819
Li Y, Wang Q, Ding Z, Wan D, Nie X, Zhong C (2022) A functionalized magnetic graphene-based MOFs platform as the heterogeneous mimic enzyme sensor for glucose detection. Catal Lett 152:2375–2385. https://doi.org/10.1007/s10562-021-03815-1
Li Y, Wen L, Tan T, Lv Y (2019b) Sequential co-immobilization of enzymes in metal-organic frameworks for efficient biocatalytic conversion of adsorbed CO2 to formate. Front Bioeng Biotechnol 7:394–407. https://doi.org/10.3389/fbioe.2019.00394
Li Z, Zhang Y, Su Y, Ouyang P, Ge J, Liu Z (2014) Spatial co-localization of multienzymes by inorganic nanocrystal-protein complexes. Chem Commun 50:12465–12468. https://doi.org/10.1039/c4cc05478d
Lian X, Fang Y, Joseph E, Wang Q, Li J, Banerjee S, Zhou H-C (2011) Enzyme-MOF (metal-organic framework) composites. Chem Soc Rev 46:3386–3401. https://doi.org/10.1039/c7cs00058h
Lian X, Fang Yu, Joseph E, Wang Q, Li J, Banerjee S, Lollar C, Wanga X, Zhou HC (2017) Enzyme–MOF (metal–organic framework) composites. Chem Soc Rev 46:3386–3401. https://doi.org/10.1039/C7CS00058H
Liang J, Liang K (2020) Multi-enzyme cascade reactions in metal-organic frameworks. Chem Rec 20:1100–1116. https://doi.org/10.1002/TCR.202000067
Liang W, Carraro F, Solomon MB, Bell SG, Amenitsch H, Sumby CJ, White NG, Falcaro P, Doonan CJ (2019) Enzyme encapsulation in a porous hydrogenbonded organic framework. J Am Chem Soc 141:14298–14305. https://doi.org/10.1021/jacs.9b06589
Liao FS, Lo WS, Hsu YS, Wu CC, Wang SC, Shieh FK, Morabito JV, Chou LY, Wu KC, Tsung CK (2017) Shielding against unfolding by embedding enzymes in metal-organic frameworks via a de novo approach. J Am Chem 139:6530–6533. https://doi.org/10.1021/jacs.7b01794
Liao H, Nehl CL, Hafner JH (2006) Biomedical applications of plasmon resonant metal nanoparticles. Nanomedicine (London) 1:201–208. https://doi.org/10.2217/17435889.1.2.201
Lin C, Xu K, Zheng R, Zheng Y (2019) Immobilization of amidase into a magnetic hierarchically porous metal-organic framework for efficient biocatalysis. Chem Commun 55:5697–5700. https://doi.org/10.1039/c9cc02038a
Liu D, Yang F, Xiong F, Gu N (2016) The smart drug delivery system and its clinical potential. Theranostics 6:1306–1323. https://doi.org/10.7150/thno.14858
Liu J, Ma R-T, Shi Y-P (2020) «Recent advances on support materials for lipase immobilization and applicability as biocatalysts in inhibitors screening methods» - a review. Anal Chim Acta 1101–1166:9–22. https://doi.org/10.1016/j.aca.2019.11.073
Liu X, Liu Y, Wang J, Wei T, Dai Z (2019) Mild hyperthermia-enhanced enzyme-mediated tumor cell chemodynamic therapy. ACS Appl Mater Interfaces 11(26):23065–23071. https://doi.org/10.1021/acsami.9b08257
Liu Y, Cao X, Ge J (2021) Antioxidative composites based on multienzyme systems encapsulated in metal-organic frameworks. ACS Appl Mater Interfaces 13:46431–46439. https://doi.org/10.1021/ACSAMI.1C15506/SUPPL_FILE/AM1C15506_SI_001
Liu Y, Chen J, Du M, Wang X, Ji X, He Z (2017a) The preparation of dual-functional hybrid nanoflower and its application in the ultrasensitive detection of diseaserelated biomarker. Biosens Bioelectron 92:68–73. https://doi.org/10.1016/j.bios.2017.02.004
Liu Y, Guo C, Liu CZ (2015) Enhancing the resolution of (R, S)-2-octanol catalyzed by magnetic crosslinked lipase aggregates using an alternating magnetic field. Chem Eng J 280:36–40. https://doi.org/10.1016/j.cej.2015.05.089
Liu Y, Zhang Y, Li X, Yuan Q, Liang H (2017b) Self-repairing metal-organic hybrid complexes for reinforcing immobilized chloroperoxidase reusability. Chem Commun 53:3216–3219. https://doi.org/10.1039/c6cc10319g
Liu Y, Zou P, Huang J, Cai J (2022) Co-immobilization of glucose oxidase and catalase in porous magnetic chitosan microspheres for production of sodium gluconate. Int J Chem React Eng 20:989–1001. https://doi.org/10.1515/ijcre-2021-0237
Long W-J (2023) Design, performance, and mechanism of cement-based materials with 2D nanomaterials. Nanotechnol Civil Infrastructure 127–159. https://doi.org/10.1016/B978-0-12-817832-4.00001-8
López-Gallego F, Yate L (2015) Selective biomineralization of Co3(PO4)2-sponges triggered by His-tagged proteins: efficient heterogeneous biocatalysts for redox processes. Chem Commun 51:8753–8756. https://doi.org/10.1039/C5CC00318K
Lu J, Weerasiri RR, Lee I (2013) Carbon nanotubes tuned foam structures as novel nanostructured biocarriers for lignocellulose hydrolysis. Biotechnol Lett 35:181–188. https://doi.org/10.1007/s10529-012-1066-5
Lu Z, Wu L, Zhang J, Dai W, Mo G, Ye J (2019) Bifunctional and highly sensitive electrochemical non-enzymatic glucose and hydrogen peroxide biosensor based on NiCo2O4 nanoflowers decorated 3D nitrogen doped holey graphene hydrogel. Mater Sci Eng C 102:708–717. https://doi.org/10.1016/j.msec.2019.04.072
Luesakul U, Komenek S, Puthong S, Muangsin N (2016) Shape-controlled synthesis of cubic-like selenium nanoparticles via the self-assembly method. Carbohydr Polym 153:435–444. https://doi.org/10.1016/j.carbpol.2016.08.004
Lundqvist M, Sethson I, Jonsson B-H (2004) Protein adsorption onto silica nanoparticles: conformational changes depend on the particles’ curvature and the protein stability. Langmuir 20(24):10639–10647. https://doi.org/10.1021/la0484725
Lyu F, Zhang Y, Zare RN, Ge J, Liu Z (2014) One-pot synthesis of protein-embedded metal-organic frameworks with enhanced biological activities. Nano Lett 14:5761–5765. https://doi.org/10.1021/NL5026419/SUPPL_FILE/NL5026419_SI_001
Ma Y-X, Li Y-F, Zhao G-H, Yang L-Q, Wang J-Z, Shan X, Yan X (2012) Preparation and characterization of graphite nanosheets decorated with Fe3O4 nanoparticles used in the immobilization of glucoamylase. Carbon 50:2976–2986. https://doi.org/10.1016/j.carbon.2012.02.080
Magner E (2013) Immobilisation of enzymes on mesoporous silicate materials Chem. Soc Rev 42:6213–6222. https://doi.org/10.1039/c2cs35450k
Majewski MB, Howarth AJ, Li P, Wasielewski MR, Hupp JT, Farha OK (2017) Enzyme encapsulation in metal-organic frameworks for applications in catalysis. Cryst Eng Comm 19:4082–4091. https://doi.org/10.1039/c7ce00022g
Majumdar S, Keller AA (2021) Omics to address the opportunities and challenges of nanotechnology in agriculture. Crit Rev Environ Sci Technol 51:157. https://doi.org/10.1080/10643389.2020.1785264
Makarova AO, Derkach SR, Kadyirov AI, Ziganshina SA, Kazantseva MA, Zueva OS, Gubaidullin AT, Zuev YuF (2022) Supramolecular structure and mechanical performance of k-carrageenan–gelatin gel. Polymers 14(20):4347. https://doi.org/10.3390/polym14204347
Makarova AO, Derkach SR, Khair T, Kazantseva MA, Zuev YuF, Zueva OS (2023) Ion-induced polysaccharide gelation: peculiarities of alginate egg-box association with different divalent cations. Polymers 15:1243. https://doi.org/10.3390/polym15051243
Makshakova O, Antonova M, Bogdanova L, Faizullin D, Zuev Yu (2023) Regulation of intersubunit interactions in homotetramer of glyceraldehyde-3-phosphate dehydrogenases upon its immobilization in protein-kappa-carrageenan gels. Polymers 15:676. https://doi.org/10.3390/polym15030676
Makshakova ON, Bogdanova LR, Makarova AO, Kusova AM, Ermakova EA, Kazantseva MA, Zuev YuF (2022) k-Carrageenan Hydrogel as a Matrix for Therapeutic Enzyme Immobilization. Polymers 14:4071. https://doi.org/10.3390/polym14194071
Makshakova ON, Zuev YuF (2022) Interaction-induced structural transformations in polysaccharide and protein-polysaccharide gels as functional basis for novel soft-matter: a case of carrageenans. Gels 8:287. https://doi.org/10.3390/gels8050287
Malykhina NV, Olshannikova SS, Holyavka MG, Sorokin AV, Lavlinskaya MS, Artyukhov VG, Faizullin DA, Zuev YuF (2022) Preparation of ficin complexes with carboxymethylchitosan and n-(2-hydroxy)propyl-3-trimethylammoniumchitosan and studies of their structural features. Russ J Bioorganic Chem 48:50–60. https://doi.org/10.1134/S1068162022060176
Manning GS (1969) Limiting laws and counterion condensation in polyelectrolyte solutions I. Colligative Properties. J Chem Phys 51:924–933. https://doi.org/10.1063/1.1672157
Mas-Balleste R, Gomez-Navarro C, Gomez-Herrero J, Zamora F (2011) 2D materials: to graphene and beyond. Nanoscale 3:20–30. https://doi.org/10.1039/c0nr00323a
Mayer KM, Hafner JH (2011) Localized surface plasmon resonance sensors. Chem Rev 111:3828–3857. https://doi.org/10.1021/cr100313v
Mayer SF, Kroutil W, Faber K (2001) Enzyme-initiated domino (cascade) reactions. Chem Soc Rev 30:332–339. https://doi.org/10.1039/B105493G
McClements DJ (2011) Edible nanoemulsions: fabrication, properties, and functional performance. Soft Matter 7:2297–2316. https://doi.org/10.1039/c0sm00549e
McNamara LE, McMurray RJ, Biggs MJP, Kantawong F, Oreffo ROC, Dalby VJ (2010) Nanotopographical control of stem cell differentiation. J Tissue Eng 2010:120623–120636. https://doi.org/10.4061/2010/120623
Mehta J, Bhardwaj N, Bhardwaj SK, Kim K-H, Deep A (2016) Recent advances in enzyme immobilization techniques: metal-organic frameworks as novel substrates. Coord Chem Rev 322:30–40. https://doi.org/10.1016/j.ccr.2016.05.007
Meng XG, Guo Y, Hu CW, Zeng XC (2004) Mimic models of peroxidase-kinetic studies of the catalytic oxidation of hydroquinone by H2O2. J Inorg Biochem 98:2107–2113. https://doi.org/10.1016/j.jinorgbio.2004.09.019
Menzies KL, Jones L (2010) The impact of contact angle on the biocompatibility of biomaterials. Optom Vis Sci 87:387–399. https://doi.org/10.1097/OPX.0b013e3181da863e
Mezzenga R, Schurtenberger P, Burbidge A, Michel M (2005) Understanding foods as soft materials. Nat Mater 4:729–740. https://doi.org/10.1038/nmat1496
Misson M, Zhang H, Jin B (2015) Nanobiocatalyst advancements and bioprocessing applications. J R Soc Interface 12(102):20140891. https://doi.org/10.1098/rsif.2014.0891
Mohajerani A, Burnett L, Smith J, Kurmus H, Milas J, Arulrajah A, Horpibulsuk S, Kadir AA (2019) Materials review nanoparticles in construction materials and other applications, and implications of nanoparticle use. https://doi.org/10.3390/ma12193052
Mora-Huertas CE, Fessi H, Elaissari A (2010) Polymer-based nanocapsules for drug delivery. Int J Pharm 385:113–142. https://doi.org/10.1016/j.ijpharm.2009.10.018
Morris W, Briley WE, Auyeung E, Cabezas MD, Mirkin CA (2014) Nucleic acid-metal organic framework (MOF) nanoparticle conjugates. J Am Chem Soc 136:7261–7264. https://doi.org/10.1021/ja503215w
Morshedi M, Thomas M, Tarzia A, Doonan CJ, White NG (2017) Supramolecular anion recognition in water: synthesis of hydrogen-bonded supramolecular frameworks. Chem Sci 8:3019–3025. https://doi.org/10.1039/c7sc00201g
Motamedi N, Barani M, Lohrasbi-Nejad A, Mortazavi M, Riahi-Medvar A, Varma RS, Torkzadeh-Mahani M (2021) Enhancement of thermostability of Aspergillus flavus urate oxidase by immobilization on the Ni-based magnetic metal-organic framework. Nanomaterials 11:1759–1779. https://doi.org/10.3390/nano11071759
Moyano DF, Rotello VM (2011) Nano meets biology: structure and function at the nanoparticle interface. Langmuir 27:10376–10385. https://doi.org/10.1021/la2004535
Muley AB, Thorat AS, Singhal RS, Babu KH (2018) A tri-enzyme co-immobilized magnetic complex: process details, kinetics, thermodynamics and applications. Int J Biol Macromol 118:1781–1795. https://doi.org/10.1016/j.ijbiomac.2018.07.022
Müller RH, Mäder K, Gohla S (2000) Solid lipid nanoparticles (SLN) for controlled drug delivery-a review of the state of the art. Eur J Pharm Biopharm 50:161–177. https://doi.org/10.1016/s0939-6411(00)00087-4
Munyemana JC, He H, Ding S, Yin J, Xi P, Xiao J (2018) Synthesis of manganese phosphate hybrid nanoflowers by collagen-templated biomineralization. RSC Adv 8:2708–2713. https://doi.org/10.1039/c7ra12628j
Nadar SS, Gawas SD, Rathod VK (2016) Self-assembled organic-inorganic hybrid glucoamylase nanoflowers with enhanced activity and stability. Int J Biol Macromol 92:660–669. https://doi.org/10.1016/j.ijbiomac.2016.06.071
Naha A, Antony S, Nath S, Sharma D, Mishra A, Biju DT, Madhavan A, Binod P, Varjani S, Sindhu R (2023) A hypothetical model of multi-layered cost-effective wastewater treatment plant integrating microbial fuel cell and nanofiltration technology: a comprehensive review on wastewater treatment and sustainable remediation. Environ Pollut 121274. https://doi.org/10.1016/j.envpol.2023.121274
Negahdary M, Heli H (2018) Applications of nanoflowers in biomedicine. Recent Pat Nanotechnol 12:22–33. https://doi.org/10.2174/1872210511666170911153428
Nematian T, Shakeri A, Salehi Z, Saboury AA (2020) lipase immobilized on functionalized superparamagnetic few-layer graphene oxide as an efficient nanobiocatalyst for biodiesel production from Chlorella vulgaris bio-oil. Biotechnol Biofuels 13:57–72. https://doi.org/10.1186/s13068-020-01688-x
Netto CGCM, Toma HE, Andrade LH (2013) Superparamagnetic nanoparticles as versatile carriers and supporting materials for enzymes. J Mol Catal B: Enzym 85–86:71–92. https://doi.org/10.1016/j.molcatb.2012.08.010
Neupane S, Patnode K, Li H, Baryeh K, Liu G, Hu J, Chen B, Pan Y, Yang Z (2019) Enhancing enzyme immobilization on carbon nanotubes via metal-organic frameworks for large-substrate biocatalysis. ACS Appl Mater Interfaces 11(12):12133–12141. https://doi.org/10.1021/acsami.9b01077
Nguyen MM, Carlini AS, Chien MP, Sonnenberg S, Luo C, Braden RL, Osborn KG, Li Y, Gianneschi NC, Christman KL (2015) Enzyme-responsive nanoparticles for targeted accumulation and prolonged retention in heart tissue after myocardial infarction. Adv Mater 27:5547–5552. https://doi.org/10.1002/adma.201502003
Ni W, Zhang P, Long L, Ding S (2022) Engineering and linker-mediated co-immobilization of carotenoid cleavage oxygenase with phenolic acid decarboxylase for efficiently converting ferulic acid into vanillin. Process Biochem 122:67–77. https://doi.org/10.1016/j.procbio.2022.08.020
Nicoletti G, Cipolatti EP, Valerio A, Carbonera NTG, Soares NS, Theilacker E, Ninow JL, de Oliveira D (2015) Evaluation of different methods for immobilization of Candida antarctica lipase B (CalB lipase) in polyurethane foam and its application in the production of geranyl propionate. Bioprocess Biosyst Eng 38:1739–1748. https://doi.org/10.1007/s00449-015-1415-6
Nonsuwan P, Puthong S, Palaga T, Muangsin N (2018) Novel organic/inorganic hybrid flower-like structure of selenium nanoparticles stabilized by pullulan derivatives. Carbohydr Polym 184:9–19. https://doi.org/10.1016/j.carbpol.2017.12.029
Novoselov KS, Geim AK, Morozov SV, Jiang D, Katsnelson MI, Grigorieva IV, Dubonos SV, Firsov AA (2005) Two-dimensional gas of massless Dirac fermions in graphene. Nature 438:197–200. https://doi.org/10.1038/nature04233
Novoselov KS, Geim AK, Morozov SV, Jiang D, Zhang Y, Dubonos SV, Grigorieva IV, Firsov AA (2004) Electric field effect in atomically thin carbon films. Science 306:666–669. https://doi.org/10.1126/science.1102896
Obayomi KS, Lau SY, Danquah M, Chiong T, Takeo M (2022) Advances in graphene oxide based nanobiocatalytic technology for wastewater treatment. Environmental Nanotechnology, Monitoring & Management 17:100647. https://doi.org/10.1016/j.enmm.2022.100647
Ó’Fágáin C (2003) Enzyme stabilization-recent experimental progress. Enzyme Microb Technol 33(2–3):137–149. https://doi.org/10.1016/S0141-0229(03)00160-1
Ocsoy I, Dogru E, Usta S (2015) A new generation of flowerlike horseradish peroxides as a nanobiocatalyst for superior enzymatic activity. Enzym Microb Technol 75:25–29. https://doi.org/10.1016/j.enzmictec.2015.04.010
Olshannikova SS, Redko YuA, Lavlinskaya MS, Sorokin AV, Holyavka MG, Yudin NE, Artyukhov VG (2022) Study of the proteolytic activity of ficin associates with chitosan nanoparticles. Condensed Matter and Interphases 24:523–528. https://doi.org/10.17308/kcmf.2022.24/10556
Padilla-Martínez SG, Martínez-Jothar L, Sampedro JG, Tristan F, Pérez 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
Pakchin PS, Ghanbari H, Saber R, Omidi Y (2018) Electrochemical immunosensor based on chitosan-gold nanoparticle/carbon nanotube as a platform and lactate oxidase as a label for detection of CA125 oncomarker. Biosens Bioelectron 122:68–74. https://doi.org/10.1016/j.bios.2018.09.016
Palanisamy S, Ramaraj SK, Chen S-M, Yang TCK, Yi-Fan P, Chen T-W, Velusamy V, Selvam S (2017) A novel laccase biosensor based on laccase immobilized graphene-cellulose microfiber composite modified screen-printed carbon electrode for sensitive determination of catechol. Sci Rep 7(1):1–12. https://doi.org/10.1038/srep41214
Patel SK, Otari SV, Li J, Kim DR, Kim SC, Cho BK, Kalia VC, Kang YC, Lee JK (2018) Synthesis of crosslinked protein-metal hybrid nanoflowers and its application in repeated batch decolorization of synthetic dyes. J Hazard Mater 347:442–450. https://doi.org/10.1016/j.jhazmat.2018.01.003
Paukov M, Kramberger C, Begichev I, Kharlamova M, Burdanova M (2023) Functionalized fullerenes and their applications in electrochemistry, solar cells, and nanoelectronics. Materials 16:1276–1297. https://doi.org/10.3390/ma16031276
Pavlidis IV, Patila M, Bornscheuer UT, Gournis D, Stamatis H (2014) Graphene-based nanobiocatalytic systems: recent advances and future prospects. Trends in Biotechnol 32:312–320. https://doi.org/10.1016/j.tibtech.2014.04.004
Peng M, Li H, Luo Z, Kong J, Wan Y, Zheng L, Zhang Q, Niu H, Vermorken A, Van de Ven W, Chen C, Zhang X, Li F, Guo L, Cui Y (2015) Dextran-coated superparamagnetic nanoparticles as potential cancer drug carriers in vivo. Nanoscale 7:11155–11162. https://doi.org/10.1039/c5nr01382h
Pospiskova K, Safarik I (2015) Magnetically responsive enzyme powders. Magn Magn Mater 380:197–200. https://doi.org/10.1016/j.jmmm.2014.10.037
Pourmadadi M, Rahmani E, Rajabzadeh-Khosroshahi M, Samadi A, Behzadmehr R, Rahdar A, Ferreira LFR (2023) Properties and application of carbon quantum dots (CQDs) in biosensors for disease detection: a comprehensive review. J Drug Delivery Sci Technol 80:104156–104170. https://doi.org/10.1016/j.jddst.2023.104156
Povedano E, Cincotto FH, Parrado C, Díez P, Sánchez A, Canevari TC, Machado SAS, Pingarrón JM, Villalonga R (2017) Decoration of reduced graphene oxide with rhodium nanoparticles for the design of a sensitive electrochemical enzyme biosensor for 17β-estradiol. Biosens Bioelectron 89:343–351. https://doi.org/10.1016/j.bios.2016.07.018
Qiu H, Li Y, Ji G, Zhou G, Huang X, Qu Y, Gao P (2009) Immobilization of lignin peroxidase on nanoporous gold: enzymatic properties and in situ release of H2O2 by co-immobilized glucose oxidase. Bioresour Technol 100:3837–3842. https://doi.org/10.1016/j.biortech.2009.03.016
Quin MB, Wallin KK, Zhang G, Schmidt-Dannert C (2017) Spatial organization of multi-enzyme biocatalytic cascades. Org Biomol Chem 15(20):4260–4271. https://doi.org/10.1039/c7ob00391a
Rai SK, Narnoliya LK, Sangwan RS, Yadav SK (2018) Self-assembled hybrid nanoflowers of manganese phosphate and L-arabinose isomerase: a stable and recyclable nanobiocatalyst for equilibrium level conversion of D-galactose to Dtagatose. ACS Sustain Chem Eng 6:6296–6304. https://doi.org/10.1021/acssuschemeng.8b00091
Raita M, Arnthong J, Champreda V, Laosiripojana N (2015) Modification of magnetic nanoparticle lipase designs for biodiesel production from palm oil. Fuel Process Technol 134:189–197. https://doi.org/10.1016/j.fuproc.2015.01.032
Ramos AP, Cruz MAE, Tovani CB, Ciancaglini P (2017) Biomedical applications of nanotechnology. Biophys Rev 9:79–89. https://doi.org/10.1007/s12551-016-0246-2
Razumovsky SD, Efremenko EN, Makhlis TA, Senko OV, Bikhovsky MY, Podmasterev VV, Varfolomeev SD (2008) Effect of immobilization on the main dynamic characteristics of the enzymatic oxidation of methane to methanol by bacteria Methylosinus sporium B-2121. Russ Chem Bull, Int Ed 57:1633–1636. https://doi.org/10.1007/s11172-008-0211-8
Redko YuA, Olshannikova SS, Holyavka MG, Lavlinskaya MS, Sorokin AV, Artyukhov VG (2022) Development of a method for obtaining bromelain associates with chitosan micro- and nanoparticles. Pharm Chem J 56:984–988. https://doi.org/10.1007/s11094-022-02737-5
Reis CLB, de Sousa EYA, de Franca SJ, Oliveira RC, dos Santos JCS (2019) Design of immobilized enzyme biocatalysts: drawbacks and opportunities. Quim Nova 42:768–783. https://doi.org/10.21577/0100-4042.20170381
Ren S, Wang Z, Bilal M, Feng Y, Jiang Y, Jia S, Cui J (2020) Co-immobilization multienzyme nanoreactor with co-factor regeneration for conversion of CO2. Int J Biol Macromol 155:110–118. https://doi.org/10.1016/j.ijbiomac.2020.03.177
Ren SZ, Li CH, Jiao XB, Jia SR, Jiang YJ, Bilal M, Cui J (2019) Recent progress in multienzymes co-immobilization and multienzyme system applications. Chem Eng J 373:1254–1278. https://doi.org/10.1016/j.cej.2019.05.141
Rezaei B, Shoushtari AM, Rabiee M, Uzun L, Mak WC, Turner APF (2018) An electrochemical immunosensor for cardiac Troponin I using electrospun carboxylated multi-walled carbon nanotube-whiskered nanofibres. Talanta 182:178–186. https://doi.org/10.1016/j.talanta.2018.01.046
Rouhani S, Azizi S, Kibechu RW, Mamba BB, Msagati TAM (2020) Laccase immobilized Fe3O4-graphene oxide nanobiocatalyst improves stability and immobilization efficiency in the green preparation of sulfa drugs. Catalysts 10(4):459–474. https://doi.org/10.3390/catal10040459
Rulı́šek L, Vondrášek J (1998) Coordination geometries of selected transition metal ions (Co2+, Ni2+, Cu2+, Zn2+, Cd2+, and Hg2+) in metalloproteins. J Inorg Biochem 71:115–127. https://doi.org/10.1016/s0162-0134(98)10042-9
Sahoo B, Sahu SK, Pramanik P (2011) A novel method for the immobilization of urease on phosphonate grafted iron oxide nanoparticle. J Mol Catal B: Enzym 69:95–102. https://doi.org/10.1016/j.molcatb.2011.01.001
Saji VS, Choe HC, Young KWK (2010) Nanotechnology in biomedical applications-a review. Int J Nano Biomater 3:119–139. https://doi.org/10.1504/IJNBM.2010.037801
Sargazi G, Afzali D, Ebrahimi AK, Badoei-Dalfard A, Malekabadi S, Karami Z (2018) Ultrasound assisted reverse micelle efficient synthesis of new Ta-MOF@Fe3O4 core/shell nanostructures as a novel candidate for lipase immobilization. Mater Sci Eng C 93:768–775. https://doi.org/10.1016/j.msec.2018.08.041
Senko O, Gladchenko M, Maslova O, Efremenko E (2019) Long-term storage and use of artificially immobilized anaerobic sludge as a powerful biocatalyst for conversion of various wastes including those containing xenobiotics to biogas. Catalysts 9:326–346. https://doi.org/10.3390/catal9040326
Shaarani S, Jahim J, Rahman RA, Idris A, Munir A, Murad IR (2016) Silanized maghemite for cross-linked enzyme aggregates of recombinant xylanase from Trichoderma reesei. J Mol Catal B: Enzym 133:65–76. https://doi.org/10.1016/j.molcatb.2016.07.006
Shahedi M, Habibi Z, Yousefi M, Brask J, Mohammadi M (2021) Improvement of biodiesel production from palm oil by coimmobilization of Thermomyces lanuginosa lipase and Candida antarctica lipase B: optimization using response surface methodology. Int J Biol Macromol 170:490–502. https://doi.org/10.1016/j.ijbiomac.2020.12.181
Shalova IN, Naletova IN, Saso L, Muronetz VI, Izumrudov VA (2007) Interaction of polyelectrolytes with proteins, 3 influence of complexing polycations on the thermoaggregation of oligomeric enzymes. Macromol Biosci 7:929–939. https://doi.org/10.1002/mabi.200700052
Shanta AS, Al Mamun KA, Islam SK, McFarlane N, Hensley DK (2017) Carbon nanotubes, nanofibers and nanospikes for electrochemical sensing: A review. Int J High Speed Electron Syst 26(3):1740008. https://doi.org/10.1142/S0129156417400080
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
Sheldon RA (2010) Cross-linked enzyme aggregates as industrial biocatalysts. Org Process Res Dev 15:213–223. https://doi.org/10.1021/op100289f
Sheldon RA, Basso A, Brady D (2021) New frontiers in enzyme immobilisation: robust biocatalysts for a circular bio-based economy. Chem Soc Rev 50:5850–5862. https://doi.org/10.1039/d1cs00015b
Sheldon RA, Woodley JM (2018) Role of biocatalysis in sustainable chemistry. Chem Rev 118:801–838. https://doi.org/10.1021/acs.chemrev.7b00203
Shende P, Kasture P, Gaud RS (2018) Nanoflowers: the future trend of nanotechnology for multi-applications. Artif Cells Nanomed Biotechnol 46:413–422. https://doi.org/10.1080/21691401.2018.1428812
Shikama Y, Kitazawa JI, Yagihashi N, Uehara O, Murata Y, Yajima N, Wada R, Yagihashi S (2010) Localized amyloidosis at the site of repeated insulin injection in a diabetic patient. Intern Med 49:397–401. https://doi.org/10.2169/internalmedicine.49.2633
Shola OK, Yon JLS, Danquah M, Chiong T, Takeo M (2022) Advances in graphene oxide based nanobiocatalytic technology for wastewater treatment. Environ Nanotechnol Monit Manage 17:100647. https://doi.org/10.1016/j.enmm.2022.100647
Shukla SK, Mishra AK, Arotiba OA, Mamba BB (2013) Chitosan-based nanomaterials: a state-of-the-art review. Int J Biol Macromol 59:46–58. https://doi.org/10.1016/j.ijbiomac.2013.04.043
Singh V, Kaul S, Singla P, Kumar V, Sandhir R, Chung JH, Garg P, Singhal NK (2018) Xylanase immobilization on magnetite and magnetite core/shell nanocomposites using two different flexible alkyl length organophosphonates: linker length and shell effect on enzyme catalytic activity. Int J Biol Macromol 115:590–599. https://doi.org/10.1016/j.ijbiomac.2018.04.097
Somturk B, Hancer M, Ocsoy I, Özdemir N (2015) Synthesis of copper ion incorporated horseradish peroxidase-based hybrid nanoflowers for enhanced catalytic activity and stability. Dalton Trans 44:13845–13852. https://doi.org/10.1039/c5dt01250c
Soozanipour A, Taheri-Kafrani A, Isfahani AL (2015) Covalent attachment of xylanase on functionalized magnetic nanoparticles and determination of its activity and stability. Chem Eng J 270:235–243. https://doi.org/10.1016/j.cej.2015.02.032
Souto EB, Müller RH (2007) Lipid nanoparticles (solid lipid nanoparticles and nanostructured lipid carriers) for cosmetic, dermal, and transdermal applications. drugs and the pharmaceutical sciences. a series of textbooks and monographs. Executive Editor James Swarbrick. PharmaceuTech, Inc. Pinehurst, North Carolina. https://doi.org/10.1201/9781420008449.ch14
Stefani M, Dobson CM (2003) Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 81:678–699. https://doi.org/10.1007/s00109-003-0464-5
Stern A, Rotem D, Popov I, Porath D (2012) Quasi 3D imaging of DNA-gold nanoparticle tetrahedral structures. J Phys Condens Matter 24:164203–164209. https://doi.org/10.1088/0953-8984/24/16/164203
Stine KJ (2017) Enzyme immobilization on nanoporous gold: A review. Biochem Insights 10:1178626417748607. https://doi.org/10.1177/1178626417748607
Stocke NA, Arnold SM, Hilt JZ (2015) Responsive hydrogel nanoparticles for pulmonary delivery. J Drug Deliv Sci Technol 29:143–151. https://doi.org/10.1016/j.jddst.2015.06.013
Su Y, Zhou X, Long Y, Li W (2018) Immobilization of horseradish peroxidase on amino-functionalized carbon dots for the sensitive detection of hydrogen peroxide. Microchim Acta 185(2):1–8. https://doi.org/10.1007/s00604-017-2629-x
Sun J, Ge J, Liu W, Lan M, Zhang H, Wang P, Wang Y, Niu Z (2014) Multi-enzyme coembedded organic-inorganic hybrid nanoflowers: synthesis and application as a colorimetric sensor. Nanoscale 6:255–262. https://doi.org/10.1039/c3nr04425d
Sur S, Rathore A, Dave V, Reddy KR, Chouhan RS, Sadhu V (2019) Recent developments in functionalized polymer nanoparticles for efficient drug delivery system. Nano-Struct & Nano-Objects 20:100397–100418. https://doi.org/10.1016/j.nanoso.2019.100397
Syed F, Ali K, Asad MJ, Fraz MG, Khan Z, Imran M, Taj R, Ahmad A (2016) Preparation and characterization of a green nano-support for the covalent immobilization of glucoamylase from Neurospora sitophila. J Photochem Photobiol B 162:309–317. https://doi.org/10.1016/j.jphotobiol.2016.07.002
Takimoto A, Shiomi T, Ino K, Tsunoda T, Kawai A, Mizukami F, Sakaguchi K (2008) Encapsulation of cellulase with mesoporous silica (SBA-15). Microporous Mesoporous Mater 116:601–606. https://doi.org/10.1016/j.micromeso.2008.05.046
Talekar S, Ghodake V, Ghotage T, Rathod P, Deshmukh P, Nadar S, Mulla M, Ladole M (2012) Novel magnetic cross-linked enzyme aggregates (magnetic CLEAs) of alpha amylase. Bioresour Technol 123:542–547. https://doi.org/10.1016/j.biortech.2012.07.044
Tan H, Feng W, Ji P (2012) Lipase immobilized on magnetic multi-walled carbon nanotubes. Bioresour Technol 115:172–176. https://doi.org/10.1016/j.biortech.2011.10.066
Tan WY, Gopinath SCB, Anbu P, Yaakub ARW, Subramaniam S, Chen Y, Sasidharan S (2023) Bio-enzyme hybrid with nanomaterials: a potential cargo as sustainable biocatalyst. Sustainability 15(9):7511. https://doi.org/10.3390/su15097511
Tang J, Liu J, Zheng Q, Li W, Sheng J, Mao L, Wang M (2021a) In-situ encapsulation of protein into nanoscale hydrogen-bonded organic frameworks for intracellular biocatalysis. Angew Chem Int Ed 60:22315–22321. https://doi.org/10.1002/anie.202105634
Tang Z, Li X, Tong L, Yang H, Wu J, Zhang X, Song T, Huang S, Zhu F, Chen G, Ouyang G (2021b) A biocatalytic cascade in an ultrastable mesoporous hydrogenbonded organic framework for point-of-care biosensing. Angew Chem Int Ed 60:23608–23613. https://doi.org/10.1002/anie.202110351
Tang ZX, Qian JQ, Shi LE (2007) Characterizations of immobilized neutral lipase on chitosan nano-particles. Mater Lett 61:37–40. https://doi.org/10.1016/j.matlet.2006.04.048
Thakur K, Attri C, Seth A (2011) Nanocarriers-based immobilization of enzymes for industrial application. Biotech 11:1–12. https://doi.org/10.1007/s13205-021-02953-y
Thandavan K, Gandhi S, Sethuraman S, Rayappan JBB, Krishnan UM (2013) A novel nano-interfaced superoxide biosensor. Sens Actuators, B 176:884–892. https://doi.org/10.1016/j.snb.2012.09.031
Tran DT, Chen CL, Chang JS (2012) Immobilization of Burkholderia sp. lipase on a ferric silica nanocomposite for biodiesel production. J Biotechnol 158:112–119. https://doi.org/10.1016/j.jbiotec.2012.01.018
Ubbink J, Burbidge A, Mezzenga R (2008) Food structure and functionality: a soft matter perspective. Soft Mater 4:1569–1581. https://doi.org/10.1039/b802183j
Uddin MJ, Werfel TA, Crews BC, Gupta MK, Kavanaugh TE, Kingsley PhJ, Boyd K, Marnett LJ, Duvall CL (2016) Fluorocoxib a loaded nanoparticles enable targeted visualization of cyclooxygenase-2 in inflammation and cancer. Biomaterials 92:71–80. https://doi.org/10.1016/j.biomaterials.2016.03.028
Valerio A, Nicoletti G, Cipolatti EP, Ninow JL, Araujo PHH, Sayer C, de Oliveira D (2015) Kinetic study of Candida antarctica lipase b immobilization using poly (methyl methacrylate) nanoparticles obtained by miniemulsion polymerization as support. Appl Biochem Biotechnol 175:2961–2971. https://doi.org/10.1007/s12010-015-1478-5
Valls-Chivas Á, Gómez J, Garcia-Peiro JI, Hornos F, Hueso JL (2017) Enzyme-iron oxide nanoassemblies: a review of immobilization and biocatalytic applications. Catalysts 13(6):980. https://doi.org/10.3390/catal13060980
Vashist SK, Luong JHT (2015) Recent advances in electrochemical biosensing schemes using graphene and graphene-based nanocomposites. Carbon 84:519–550. https://doi.org/10.1016/j.carbon.2014.12.052
Vauthier C, Bouchemal K (2009) Methods for the preparation and manufacture of polymeric nanoparticles. Pharm Res 26:1025–1058. https://doi.org/10.1007/s11095-008-9800-3
Velasco-Lozano S (2020) Co-immobilization and colocalization of multi-enzyme systems for the cell-free biosynthesis of aminoalcohols. ChemCatChem 12(11):3030–3041. https://doi.org/10.1002/cctc.201902404
Verma ML, Puri M, Barrow CJ (2016) Recent trends in nanomaterials immobilised enzymes for biofuel production. Crit Rev Biotechnol 36:108–119. https://doi.org/10.3109/07388551.2014.928811
Vertegel AA, Richard W, Siegel A, Dordick JS (2004) Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme. Langmuir 20(16):6800–6807. https://doi.org/10.1021/la0497200
Virgen-Ortíz JJ, Dos Santos JCS, Berenguer-Murcia Á, 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 5:7461–7490. https://doi.org/10.1039/c7tb01639e
Visakh PM, Bayraktar O, Picó G (2014) Polyelectrolyte: Thermodynamics and Rheology. 1–17. https://doi.org/10.1007/978-3-319-01680-1
Wahab RA, Elias N, Abdullaha F, Ghoshal SK (2020) On the taught new tricks of enzymes immobilization: An allinclusive overview. React Funct Polym 152:104613–104639. https://doi.org/10.1016/j.reactfunctpolym.2020.104613
Wahajuddin AS (2012) Superparamagnetic iron oxide nanoparticles: magnetic nanoplatforms as drug carriers. Int J Nanomedicine 7:3445–3471. https://doi.org/10.2147/IJN.S30320
Wan G-Z, Ma X-H, Jin L, Chen J (2021) α-Glucosidase immobilization on magnetic core-shell metal-organic frameworks for inhibitor screening from traditional Chinese medicines. Colloids Surf B: Biointerfaces 205:111847–111856. https://doi.org/10.1016/j.colsurfb.2021.111847
Wang B, Lin RB, Zhang Z, Xiang S, Chen B (2020) Hydrogen-bonded organic frameworks as a tunable platform for functional materials. J Am Chem Soc 142:14399–14416. https://doi.org/10.1021/jacs.0c06473
Wang C, Liao K (2021) Recent advances in emerging metal- and covalent-organic frameworks for enzyme encapsulation. ACS Appl Mater Inter 13:56752–56776. https://doi.org/10.1021/acsami.1c13408
Wang J, Chen Y, Chen B, Ding J, Xia G, Gao C, Cheng J, Jin N, Zhou Y, Li X, Tang M, Wang XM (2010) Pharmacokinetic parameters and tissue distribution of magnetic Fe3O4 nanoparticles in mice. Int J Nanomedicine 5:861–866. https://doi.org/10.2147/IJN.S13662
Wang L, Jiang R (2011) Reversible his-tagged enzyme immobilization on functionalized carbon nanotubes as nanoscale biocatalyst. Methods Mol Biol 743:95–106. https://doi.org/10.1007/978-1-61779-132-1_8
Wang L, Zhi W, Lian D, Wang Y, Han J, Wang Y (2019) HRP@ZIF-8/DNA Hybrids: Functionality Integration of ZIF-8 via Biomineralization and Surface Absorption. ACS Sustainable Chem Eng 7:14611–14620. https://doi.org/10.1021/ACSSUSCHEMENG.9B02348
Wang LB, Wang YC, He R, Zhuang A, Wang X, Zeng J, Hou JG (2013) A new nanobiocatalytic system based on allosteric effect with dramatically enhanced enzymatic performance. J Am Chem Soc 135:1272–1275. https://doi.org/10.1021/ja3120136
Wang X, Shi J, Li Z, Zhang S, Wu H, Jiang Z, Yang C, Tian C (2014) Facile one-pot preparation of chitosan/calcium pyrophosphate hybrid microflowers. ACS Appl Mater Interfaces 6:14522–14532. https://doi.org/10.1021/am503787h
Wang Z, Liu Y, Li J, Meng G, Zhu D, Cui J, Jia S (2022) Efficient immobilization of enzymes on amino functionalized MIL-125-NH2 metal organic framework. Biotechnol Bioprocess Eng 27:135–144. https://doi.org/10.1007/s12257-020-0393-y
Wei B, Xu H, Cheng L, Yuan Q, Liu C, Gao H, Liang H (2021) Highly selective entrapment of his-tagged enzymes on superparamagnetic zirconium-based MOFs with robust renewability to enhance pH and thermal stability. ACS Biomater Sci Eng 7:3727–3736. https://doi.org/10.1021/acsbiomaterials.1c00780
Wei W, Yi Y, Song J, Chen X, Li J, Li J (2022) Tunable graphene/nitrocellulose temperature alarm sensors. ACS Appl Mater Interfaces 14:13790–13800. https://doi.org/10.1021/acsami.2c02340
White NG (2021) Amidiniumcdots, three dots, centeredcarboxylate frameworks: predictable, robust, water-stable hydrogen bonded materials. Chem Commun 57:10998–11008. https://doi.org/10.1039/d1cc04782e
Wick P, Louw-Gaume AE, Kucki M, Krug HF, Kostarelos K, Fadeel B, Dawson KA, Salvati A, Vázquez E, Ballerini L, Tretiach M, Benfenati F, Flahaut E, Gauthier L, Prato M, Bianco A (2014) Classification framework for graphene-based materials. Angew Chem Int Ed 53(30):7714–7718. https://doi.org/10.1002/anie.201403335
Wied P, Carraro F, Bolivar JM, Doonan CJ, Falcaro P, Nidetzky B (2022) Combining a genetically engineered oxidase with hydrogen-bonded organic frameworks (HOFs) for highly efficient biocomposites. Angew Chem Int Ed 61:16. https://doi.org/10.1002/anie.202117345
Williams L, Adams W (2007) Nanotechnology demystified. New York, U.S.A. https://doi.org/10.1036/0071460233
Wu H, Li X, Liu W, Chen T, Li Y, Zheng W, Man CWY, Wong MK, Wong KH (2012) Surface decoration of selenium nanoparticles by mushroom polysaccharides-protein complexes to achieve enhanced cellular uptake and antiproliferative activity. J Mater Chem 22:9602–9610. https://doi.org/10.1039/C2JM16828F
Wu Z, Shan H, Jiao Y, Huang S, Wang X, Liang K, Shi J (2022) Covalent organic networks for in situ entrapment of enzymes with superior robustness and durability. Chem Eng J 450:138446. https://doi.org/10.1016/j.cej.2022.138446
Wu ZF, Wang Z, Zhang Y, Ma YL, He CY, Li H, Chen L, Huo QS, Wang L, Li ZQ (2016) Amino acids-incorporated nanoflowers with an intrinsic peroxidase-like activity. Sci Rep 6:22412–22418. https://doi.org/10.1038/srep22412
Wu ZL, Liu ZX, Yuan YH (2017) Carbon dots: materials, synthesis, properties and approaches to long-wavelength and multicolor emission. J Mater Chem B 5(21):3794–3809. https://doi.org/10.1039/C7TB00363C
Wu X, Hou M, Ge J (2015) Metal-organic frameworks and inorganic nanoflowers: a type of emerging inorganic crystal nanocarriers for enzyme immobilization. Catal Sci Technol 5:5077–5508. https://doi.org/10.1039/C5CY01181G
Xie J, Huang J, Li X, Sun S, Chen X (2009) Iron oxide nanoparticle platform for biomedical applications. Curr Med Chem 16:1278–1294. https://doi.org/10.2174/092986709787846604
Xie W, Ma N (2010) Enzymatic transesterification of soybean oil by using immobilized lipase on magnetic nano-particles. Biomass Bioenergy 34:890–896. https://doi.org/10.1016/j.biombioe.2010.01.034
Xu J, Cao P, Fan Z, Luo X, Yang G, Qu T, Gao J (2022) Rapid screening of lipase inhibitors in Scutellaria baicalensis by using porcine pancreatic lipase immobilized on magnetic core-shell metal-organic frameworks. Molecules 27:3475–3489. https://doi.org/10.3390/molecules27113475
Xu W, Jiao L, Wu Y, Hu L, Gu W, Zhu C (2021) Metal-organic frameworks enhance biomimetic cascade catalysis for biosensing. Adv Mater 33:2005172. https://doi.org/10.1002/ADMA.202005172
Yaari Z, Cheung JM, Baker HA, Frederiksen RS, Jena PV, Horoszko CP, Jiao F, Scheuring S, Luo M, Heller DA (2020) Nanoreporter of an enzymatic suicide inactivation pathway. Nano Lett 20(11):7819–7827. https://doi.org/10.1021/acs.nanolett.0c01858
Yan S, Chen X, Wu J, Wang P (2012) Ethanol production from concentrated food waste hydrolysates with yeast cells immobilized on corn stalk. Appl Microbiol Biotechnol 94:829–838. https://doi.org/10.1007/s00253-012-3990-7
Yang F, Tang Q, Zhong X, Bai Y, Chen T, Zhang Y, Li Y, Zheng W (2012) Surface decoration by Spirulina polysaccharide enhances the cellular uptake and anticancer efficacy of selenium nanoparticles. Int J Nanomedicine 7:835–844. https://doi.org/10.2147/IJN.S28278
Yang J, Wang J, Hou B, Huang X, Wang T, Bao Y, Hao H (2020) Porous hydrogenbonded organic frameworks (HOFs): From design to potential applications. Chem Eng J 399:125873–125938. https://doi.org/10.1016/j.cej.2020.125873
Yang J, Zhang T, Tian C, Zhu Y, Zeng Y, Men Y, Chen P, Sun Y, Ma Y (2019) Multi-enzyme systems and recombinant cells for synthesis of valuable saccharides: advances and perspectives. Biotechnol Adv 37:107406–107430. https://doi.org/10.1016/j.biotechadv.2019.06.005
Ye R, Zhu C, Song Y, Song J, Fu S, Lu Q, Yang X, Zhu MJ, Du D, Li H, Lin Y (2016) One-pot bioinspired synthesis of all-inclusive protein-protein nanoflowers for point-of-care bioassay: detection of E. coli O157: H7 from milk. Nanoscale 8:18980–18986. https://doi.org/10.1039/c6nr06870g
Yim EKF, Darling EM, Kulangara K et al (2010) Nanotopographyinduced changes in focal adhesions, cytoskeletal organization, and mechanical properties of human mesenchymal stem cells. Biomaterials 31:1299–1306. https://doi.org/10.1016/j.biomaterials.2009.10.037
Yin H, Xu Z, Bao H, Bai J, Zheng Y (2004) Single crystal trigonal selenium nanoplates converted from selenium nanoparticles. Chem Lett 34:122–123. https://doi.org/10.1246/cl.2005.122
Yin Q, Zhao P, Sa RJ, Chen GC, Lu J, Liu TE, Cao R (2018) An ultra-robust and crystalline redeemable hydrogen-bonded organic framework for synergistic chemo-photodynamic therapy. Angew Chem Int Ed 57:7691–7696. https://doi.org/10.1002/anie.201800354
Yin Y, Xiao Y, Lin G, Xiao Q, Lin Z, Cai Z (2015) An enzyme-inorganic hybrid nanoflower based immobilized enzyme reactor with enhanced enzymatic activity. J Mater Chem B 3:2295–2300. https://doi.org/10.1039/C4TB01697A
Yu B, Zhou Y, Song M, Xue Y, Cai N, Luo X, Yu F (2016) Synthesis of selenium nanoparticles with mesoporous silica drug-carrier shell for programmed responsive tumor targeted synergistic therapy. RSC Adv 6:2171–2175. https://doi.org/10.1039/C5RA21460B
Yu Z, Ji N, Li X, Zhang R, Qiao Y, Xiong J, Liu J, Lu X (2023) Kinetics driven by hollow nanoreactors: an opportunity for controllable catalysis. Angew Chem Int Ed 62(3):e202213612. https://doi.org/10.1002/anie.202213612
Zang L, Qiu J, Wu X, Zhang W, Sakai E, Wei Y (2014) Preparation of magnetic chitosan nanoparticles as support for cellulase immobilization. Ind Eng Chem Res 53:3448–3454. https://doi.org/10.1021/ie404072s
Zdarta J, Jankowska K, Wyszowska M, Kijeńska-Gawrońska E, Zgoła-Grześkowiak A, Pinelo M, Meyer AS, Moszyński D, Jesionowski T (2019) Robust biodegradation of naproxen and diclofenac by laccase immobilized using electrospun nanofibers with enhanced stability and reusability. Mater Sci Eng: C 103:109789. https://doi.org/10.1016/J.MSEC.2019.109789
Zeng J, Xia Y (2012) Hybrid nanomaterials: not just a pretty flower. Nat Nanotechnol 7:415–416. https://doi.org/10.1038/nnano.2012.105
Zeng Y, Zhu Z, Du D, Lin Y (2016) Nanomaterial-based electrochemical biosensors for food safety. J Electroanal Chem 781:147–154. https://doi.org/10.1016/j.jelechem.2016.10.030
Zhang B, Chen J, Wang J, Huyan Y, Zhang H, Zhang Q (2018) Flowerlike BSA/Zn3(PO4)2/Fe3O4 magnetic hybrid particles: preparation and application to adsorption of copper ions. J Chem Eng Data 63:3913–3922. https://doi.org/10.1021/acs.jced.8b00544
Zhang B, Li P, Zhang H, Fan L, Wang H, Li X, Tian L, Chen X, Ali N, Ali Z, Zhang Q (2016a) Papain/ Zn3(PO4)2 hybrid nanoflower: preparation, characterization and its enhanced catalytic activity as an immobilized enzyme. RSC Adv 6:46702–46710. https://doi.org/10.1039/C6RA05308D
Zhang B, Li P, Zhang H, Li X, Tian L, Wang H, Ali N, Ali Z, Zhang Q (2016b) Red-blood-cell-like BSA/Zn3(PO4)2 hybrid particles: preparation and application to adsorption of heavy metal ions. Appl Surf Sci 366:328–338. https://doi.org/10.1016/j.apsusc.2016.01.074
Zhang B, Li P, Zhang H, Wang H, Li X, Tian L, Ali N, Ali Z, Zhang Q (2016c) Preparation of lipase/ Zn3(PO4)2 hybrid nanoflower and its catalytic performance as an immobilized enzyme. Chem Eng J 291:287–297. https://doi.org/10.1016/j.cej.2016.01.104
Zhang L, Liu Z, Xie Q, Li Y, Ying Y, Fu Y (2019) Bioinspired assembly of reduced graphene oxide by fibrin fiber to prepare multi-functional conductive bionanocomposites as versatile electrochemical platforms. Carbon 153:504–512. https://doi.org/10.1016/j.carbon.2019.06.101
Zhang W-W, Yang X-L, Jia J-Q, Wang N, Hu C-L, Yu X-Q (2015a) Surfactant-activated magnetic cross-linked enzyme aggregates (magnetic CLEAs) of Thermomyces lanuginosus lipase for biodiesel production. J Mol Catal B: Enzym 115:83–89. https://doi.org/10.1016/j.molcatb.2015.02.003
Zhang Y, Ge J, Liu Z (2015b) Enhanced activity of immobilized or chemically modified enzymes. ACS Catal 5:4503–4513. https://doi.org/10.1021/acscatal.5b00996
Zhang Y, Xu L, Ge J (2022) Multienzyme system in amorphous metal-organic frameworks for intracellular lactate detection. Nano Lett. https://doi.org/10.1021/ACS.NANOLETT.2C01154
Zhang Z, Zhang Y, He L, Yang Y, Liu S, Wangab M, Fand S, Fu G (2015c) A feasible synthesis of Mn3(PO4)2@ BSA nanoflowers and its application as the support nanomaterial for Pt catalyst. J Power Sources 284:170–177. https://doi.org/10.1016/j.jpowsour.2015.03.011
Zhao XS, Bao XY, Guo W, Lee FY (2006) Immobilizing catalysts on porous materials. Mater Today 9(3):32–39. https://doi.org/10.1016/S1369-7021(06)71388-8
Zhao Z, Tian J, Wu Z, Liu J, Zhao D, Shen W, He L (2013) Enhancing enzymatic stability of bioactive papers by implanting enzyme-immobilized mesoporous silicananorods into paper. Mater J Chem B 1:4719–4722. https://doi.org/10.1039/C3TB20953A
Zheng L, Sun Y, Wang J, Huang H, Geng X, Tong Y, Wang Z (2018) Preparation of a flower-like immobilized D-psicose 3-epimerase with enhanced catalytic performance. Catalysts 8:468–478. https://doi.org/10.3390/catal8100468
Zhong L, Feng Y, Hu H, Xu J, Wang Z, Du Y, Cui J, Jia S (2021) Enhanced enzymatic performance of immobilized lipase on metal organic frameworks with superhydrophobic coating for biodiesel production. J Colloid Interface Sci 602:426–436. https://doi.org/10.1016/j.jcis.2021.06.017
Zhong C, Lei Z, Huang H, Zhang M, Cai Z, Lin Z (2020) One-pot synthesis of trypsin-based magnetic metal-organic frameworks for highly efficient proteolysis. J Mater Chem B 8:4642–4647. https://doi.org/10.1039/c9tb02315a
Zhou Z, Hartmann M (2013) Progress in enzyme immobilization in ordered mesoporous materials and related applications. Chem Soc Rev 42:3894–3912. https://doi.org/10.1039/c3cs60059a
Zhu J, Sun G (2012) Lipase immobilization on glutaraldehyde-activated nanofibrous membranes for improved enzyme stabilities and activities. React Funct Polym 72:839–845. https://doi.org/10.1016/j.reactfunctpolym.2012.08.001
Zhu J, Wen M, Wen W, Du D, Zhang X, Wang S, Lin Y (2018) Recent progress in biosensors based on organic-inorganic hybrid nanoflowers. Biosens Bioelectron 120:175–187. https://doi.org/10.1016/j.bios.2018.08.058
Zhu L, Yang R, Zhai J, Tian C (2007a) Bienzymatic glucose biosensor based on coimmobilization of peroxidase and glucose oxidase on a carbon nanotubes electrode. Biosens Bioelectron 23:528–535. https://doi.org/10.1016/j.bios.2007.07.002
Zhu X, Yuri I, Gan X, Suzuki I, Li G (2007b) Electrochemical study of the effect of nano-zinc oxide on microperoxidase and its application to more sensitive hydrogen peroxide biosensor preparation. Biosens Bioelectron 22:1600–1604. https://doi.org/10.1016/j.bios.2006.07.007
Zielinska A, Carreiro F, Oliveira AM, Neves A, Pires B, Venkatesh DN, Durazzo A, Lucarini M, Eder P, Silva AM, Santini A, Souto EB (2020) Polymeric nanoparticles: production, characterization, toxicology and ecotoxicology. Molecules 25:3731–3751. https://doi.org/10.3390/molecules25163731
Zueva OS, Khair T, Derkach SR, Kazantseva MA, Zuev YuF (2023) Strontium-induced gelation of sodium alginate in the presence of carbon nanotubes: Elemental analysis and gel structure. J Compos Sci 7(7):286. https://doi.org/10.3390/jcs7070286
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Holyavka, M.G., Goncharova, S.S., Redko, Y.A. et al. Novel biocatalysts based on enzymes in complexes with nano- and micromaterials. Biophys Rev 15, 1127–1158 (2023). https://doi.org/10.1007/s12551-023-01146-6
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DOI: https://doi.org/10.1007/s12551-023-01146-6