Abstract
Nanobiocatalysis is a new technique that blends biotechnology with nanotechnology to deliver exciting benefits in bioprocessing applications, such as increased enzyme activity, capacity, stability, and engineering performance. Immobilized enzymes are spatially confined in a particular location where they can keep their catalytic activity and be employed repeatedly. Recent breakthroughs in nano-biotechnology have opened several opportunities for embedding natural biocatalysts into a variety of nanostructures with different features. These nanoparticles (NPs) have additional properties that enzymes do not have in their native condition. Nanomaterials for enzyme delivery and novel catalytic structures with interplaying characteristics and functionality have propelled this field to new heights, with important biotechnological consequences in the coming years. The current review discusses advances in nanostructured materials, such as nanofibers, nanoporous carriers, hybrid nanoflowers, and nanocomposites, as carriers for the immobilization of various enzymes to build nanobiocatalysts with promising stability and activity, as well as current challenges and future trends.
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References
Abdollahi K, Yazdani F, Panahi R, Mokhtarani B (2018) Biotransformation of phenol in synthetic wastewater using the functionalized magnetic nano-biocatalyst particles carrying tyrosinase. 3 Biotech 8(10). https://doi.org/10.1007/s13205-018-1445-2
Ahmed S, Saifullah, Ahmad M, 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
Alswieleh AM (2021) Remediation of cationic and anionic dyes from water by histidine modified mesoporous silica. https://doi.org/10.1080/03067319.2021.1873308
Ansari SA, Husain Q (2012) Potential applications of enzymes immobilized on/in nano materials: A review. Biotechnol Adv 30(3):512–523. https://doi.org/10.1016/J.BIOTECHADV.2011.09.005
Antonio Hernández Martínez S, Melchor-Martínez EM, Rodríguez Hernández A, Parra-Saldívar R, Iqbal HMN (2022) Magnetic nanomaterials assisted nanobiocatalysis systems and their applications in biofuels production. Fuel, 312. https://doi.org/10.1016/j.fuel.2021.122927
Arcus VL, Mulholland AJ (2020) Temperature, Dynamics, and Enzyme-Catalyzed Reaction Rates. https://doi.org/10.1146/annurev-biophys-121219
Ariaeenejad S, Motamedi E, Hosseini Salekdeh G (2020) Stable cellulase immobilized on graphene oxide@CMC-g-poly(AMPS-co-AAm) hydrogel for enhanced enzymatic hydrolysis of lignocellulosic biomass. Carbohydr Polym 230:115661. https://doi.org/10.1016/J.CARBPOL.2019.115661
Ariga K, Ji Q, Mori T, Naito M, Yamauchi Y, Abe H, Hill JP (2013) Enzyme nanoarchitectonics: Organization and device application. Chem Soc Rev 42(15):6322–6345. https://doi.org/10.1039/c2cs35475f
Assa F, Jafarizadeh-Malmiri H, Ajamein H, Vaghari H (2017) Chitosan magnetic nanoparticles for drug delivery systems. Crit Rev Biotechnol 37(4):492–509. https://doi.org/10.1080/07388551.2016.1185389
Azevedo RM, Costa JB, Serp P, Loureiro JM, Faria JL, Silva CG, Tavares AP (2015) A strategy for improving peroxidase stability via immobilization on surface modified multi-walled carbon nanotubes. J Chem Technol Biotechnol 90(9):1570–1578
Berti IR, Castro GR (2022) Nanobiocatalyst for drug delivery. Nanomaterials for Biocatalysis 437–462. https://doi.org/10.1016/B978-0-12-824436-4.00005-8
Bilal M, Ahmad Qamar S, Salman Ashraf S, Rodríguez-Couto S, Iqbal HM (2021) Historical Perspective Robust nanocarriers to engineer nanobiocatalysts for bioprocessing applications. https://doi.org/10.1016/j.cis.2021.102438
Bilal M, Nguyen A, Iqbal HMN (2020) Multifunctional carbon nanotubes and their derived nano-constructs for enzyme immobilization – A paradigm shift in biocatalyst design. Coord Chem Rev 422:213475. https://doi.org/10.1016/J.CCR.2020.213475
Bilal M, Hussain N, Américo-Pinheiro JHP, 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, Iqbal HMN (2019) Chemical, physical, and biological coordination: An interplay between materials and enzymes as potential platforms for immobilization. Coord Chem Rev 388:1–23. https://doi.org/10.1016/J.CCR.2019.02.024
Bilal M, Iqbal HMN, Guo S, Hu H, Wang W, Zhang X (2018) State-of-the-art protein engineering approaches using biological macromolecules: A review from immobilization to implementation view point. Int J Biol Macromol 108:893–901. https://doi.org/10.1016/J.IJBIOMAC.2017.10.182
Bilal M, Qamar SA, Ashraf SS, Rodríguez-Couto S, Iqbal HMN (2021a) Robust nanocarriers to engineer nanobiocatalysts for bioprocessing applications. Adv Colloid Interface Sci 293:102438. https://doi.org/10.1016/J.CIS.2021.102438
Bilal M, Qamar SA, Ashraf SS, Rodríguez-Couto S, Iqbal HMN (2021b) Robust nanocarriers to engineer nanobiocatalysts for bioprocessing applications. Adv Colloid Interface Sci 293:102438. https://doi.org/10.1016/J.CIS.2021.102438
Bilal M, Zhao Y, Noreen S, Zakir S, Shah H, Bharagava RN, Iqbal HMN (2019) Biocatalysis and Biotransformation Modifying bio-catalytic properties of enzymes for efficient biocatalysis: a review from immobilization strategies viewpoint. https://doi.org/10.1080/10242422.2018.1564744
Bilal M, Zhao Y, Noreen S, Shah SZH, Bharagava RN, Iqbal HM (2019) Modifying bio-catalytic properties of enzymes for efficient biocatalysis: A review from immobilization strategies viewpoint. Biocatal Biotransform 37(3):159–182
Borzouee FVJCRA; N. D. P. R. T (2021) A Comparative Analysis of Different Enzyme Immobilization Nanomaterials: Progress, Constraints and Recent Trends. Curr Med Chem 28(20):3980–400324
Carvalho T, Pereira AdaS, Bonomo RCF, Franco M, Finotelli Pv, Amaral PFF (2020) Simple physical adsorption technique to immobilize Yarrowia lipolytica lipase purified by different methods on magnetic nanoparticles: Adsorption isotherms and thermodynamic approach. Int J Biol Macromol 160:889–902. https://doi.org/10.1016/J.IJBIOMAC.2020.05.174
Cai L, Chu Y, Liu X, Qiu Y, Ge Z, Zhang G (2021) A novel all-in-one strategy for purification and immobilization of β-1,3-xylanase directly from cell lysate as active and recyclable nanobiocatalyst. Microb Cell Factories 20:37
Chang RHY, Jang J, Wu KCW (2011) Cellulase immobilized mesoporous silica nanocatalysts for efficient cellulose-to-glucose conversion. Green Chem 13(10):2844–2850. https://doi.org/10.1039/c1gc15563f
Chapman R, Stenzel MH (2019) All Wrapped up: Stabilization of Enzymes within Single Enzyme Nanoparticles. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.8b10338
Cipolatti EP, Silva MJA, Klein M, Feddern V, Feltes MMC, Oliveira JV, Ninow JL, de Oliveira D (2014) Current status and trends in enzymatic nanoimmobilization. J Mol Catal B: Enzymatic 99:56–67. https://doi.org/10.1016/J.MOLCATB.2013.10.019
Cuomo F, Ceglie A, de Leonardis A, Lopez F (2018) catalysts Polymer Capsules for Enzymatic Catalysis in Confined Environments. https://doi.org/10.3390/catal9010001
Cutlan R, de Rose S, Isupov MN, Littlechild JA, Harmer NJ (2020) Using enzyme cascades in biocatalysis: Highlight on transaminases and carboxylic acid reductases. In Biochimica et Biophysica Acta - Proteins and Proteomics (Vol. 1868, Issue 2). Elsevier B.V. https://doi.org/10.1016/j.bbapap.2019.140322
de la Rica R, Aili D, Stevens MM (2012) Enzyme-responsive nanoparticles for drug release and diagnostics. Adv Drug Deliv Rev 64(11):967–978. https://doi.org/10.1016/J.ADDR.2012.01.002
Defaei M, Taheri-Kafrani A, Miroliaei M, Yaghmaei P (2018) Improvement of stability and reusability of α-amylase immobilized on naringin functionalized magnetic nanoparticles: A robust nanobiocatalyst. Int J Biol Macromol 113:354–360. https://doi.org/10.1016/J.IJBIOMAC.2018.02.147
Deshpande A, D’souza SF, Nadkarni GB (1987) Coimmobilization of D-amino acid oxidase and catalase by entrapment of Trigonopsis variabilis in radiation polymerised Polyacrylamide beads. InJ. Biosci(Vol. 11)
Du Y, Jia X, Zhong L, Jiao Y, Zhang Z, Wang Z, Jia S (2022) Metal-organic frameworks with different dimensionalities: An ideal host platform for enzyme@ MOF composites. Coord Chem Rev 454:214327
Dutta N, Mukhopadhyay A, Dasgupta AK, Chakrabarti K (2013) Nanotechnology Enabled Enhancement of Enzyme Activity and Thermostability: Study on Impaired Pectate Lyase from Attenuated Macrophomina phaseolina in Presence of Hydroxyapatite Nanoparticle. PLoS ONE 8(5):63567. https://doi.org/10.1371/journal.pone.0063567
Ee Taek Hwang, & Man Bock Gu (2013) Enzyme stabilization by nano/microsizedhybrid materials. Life Sci 13(1):49–61. https://doi.org/10.1002/elsc.201100225
Fatima A, Waseem Mumtaz M, Mukhtar H, Akram S, Touqeer T, Rashid U, Raza M, Mustafa U, Nehdi IA, Saiman MI (2020) Synthesis of Lipase-Immobilized CeO 2 Nanorods as Heterogeneous Nano-Biocatalyst for Optimized Biodiesel Production from Eruca sativa Seed Oil. 10, 231. https://doi.org/10.3390/catal10020231
Federsel HJ, Moody TS, Taylor S (2021) Recent Trends in Enzyme Immobilization-Concepts for Expanding the Biocatalysis Toolbox. Molecules 26:2822
Fernandez-Lafuente R (2009) Stabilization of multimeric enzymes: Strategies to prevent subunit dissociation. Enzym Microb Technol 45(6–7):405–418. https://doi.org/10.1016/J.ENZMICTEC.2009.08.009
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
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. https://doi.org/10.3390/nano9060808
Fuertes AB, Tartaj P (2007) Monodisperse Carbon-Polymer Mesoporous Spheres with Magnetic Functionality and Adjustable Pore-Size Distribution**. https://doi.org/10.1002/smll.200600487
Ge J, Lei J, Zare RN (2012) Protein-inorganic hybrid nanoflowers. Nat Nanotechnol 7(7):428–432. https://doi.org/10.1038/nnano.2012.80
Ghorbani-Kalhor E (2016) A metal-organic framework nanocomposite made from functionalized magnetite nanoparticles and HKUST-1 (MOF-199) for preconcentration of Cd(II), Pb(II), and Ni(II). https://doi.org/10.1007/s00604-016-1896-2
Giunta CI, Cea-Rama I, Alonso S, Briand ML, Bargiela R, Coscolín C, Corvini F-X, Ferrer P, Sanz-Aparicio M, Shahgaldian P (2020) Tuning the Properties of Natural Promiscuous Enzymes by Engineering Their Nano-environment. ACS Nano 14:17652–17664. https://doi.org/10.1021/acsnano.0c08716
Gößl D, Singer H, Chiu HY, Schmidt A, Lichtnecker M, Engelke H, Bein T (2019) Highly active enzymes immobilized in large pore colloidal mesoporous silica nanoparticles. New J Chem 43(4):1671–1680. https://doi.org/10.1039/c8nj04585b
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, 2018
Grosová Z, Rosenberg M, Rebroš M, Šipocz M, Sedláčková B (2008) Entrapment of β-galactosidase in polyvinylalcohol hydrogel. Biotechnol Lett 30(4):763–767. https://doi.org/10.1007/S10529-007-9606-0
Gupta A, Verma JP (2015) Sustainable bio-ethanol production from agro-residues: A review. Renew Sustain Energy Rev 41:550–567. https://doi.org/10.1016/J.RSER.2014.08.032
Gupta N, Gupta SM, Sharma SK (2019) Carbon nanotubes: synthesis, properties and engineering applications. In Carbon Letters (Vol. 29, Issue 5, pp. 419–447). Springer. https://doi.org/10.1007/s42823-019-00068-2
Holmberg K (2018) Interactions between surfactants and hydrolytic enzymes. Colloids Surf B 168:169–177. https://doi.org/10.1016/J.COLSURFB.2017.12.002
Huang WC, Wang W, Xue C, Mao X (2018) Effective Enzyme Immobilization onto a Magnetic Chitin Nanofiber Composite. ACS Sustainable Chemistry and Engineering 6(7):8118–8124. https://doi.org/10.1021/acssuschemeng.8b01150
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
Johnson BJ, Algar R, Malanoski W, Ancona AP, Medintz IL (2014) Understanding enzymatic acceleration at nanoparticle interfaces: Approaches and challenges. Nano Today 9(1):102–131. https://doi.org/10.1016/J.NANTOD.2014.02.005
Jordan J, Kumar CSSR, Theegala C (2011) Preparation and characterization of cellulase-bound magnetite nanoparticles. J Mol Catal B: Enzymatic 68(2):139–146. https://doi.org/10.1016/J,MOLCATB.2010.09.010
Kaur J, Suri CR (2007) Direct hapten coated ELISA for immunosensing of low molecular weight analytes. Protoc Exch. https://doi.org/10.1038/nprot.2007.508
Khan HA, Shanker R (2015) Editorial Toxicity of Nanomaterials. https://doi.org/10.1155/2015/521014
Khan SU, Shehzad SA (2019) Brownian movement and thermophoretic aspects in third-grade nanofluid over oscillatory moving sheet. Phys Scr 94(9). https://doi.org/10.1088/1402-4896/ab0661
Kharazmi S, Taheri-Kafrani A, Soozanipour A (2020) Efficient immobilization of pectinase on trichlorotriazine-functionalized polyethylene glycol-grafted magnetic nanoparticles: A stable and robust nanobiocatalyst for fruit juice clarification. Food Chem 325:126890. https://doi.org/10.1016/J.FOODCHEM.2020.126890
Khoshnevisan K, Vakhshiteh F, Barkhi M, Baharifar H, Poor-Akbar E, Zari N, Stamatis H, Bordbar AK (2017) Immobilization of cellulase enzyme onto magnetic nanoparticles: Applications and recent advances. In Molecular Catalysis (Vol. 442, pp. 66–73). Elsevier B.V. https://doi.org/10.1016/j.mcat.2017.09.006
Kim HS, Hong S-G, Woo KM, Seijas VT, Kim S, Lee J, Kim J (2018) Precipitation-Based Nanoscale Enzyme Reactor with Improved Loading, Stability, and Mass Transfer for Enzymatic CO 2 Conversion and Utilization. https://doi.org/10.1021/acscatal.8b00606
Kim J, Grate JW, Wang P (2008) Nanobiocatalysis and its potential applications. Trends Biotechnol 26(11):639–646. https://doi.org/10.1016/J.TIBTECH.2008.07.009
Kim J, Kim BC, Lopez-Ferrer D, Petritis K, Smith RD (2010) Nanobiocatalysis for protein digestion in proteomic analysis. https://doi.org/10.1002/pmic.200900519
Kirupa Sankar M, Ravikumar R, Naresh Kumar M, Sivakumar U (2018) Development of co-immobilized tri-enzyme biocatalytic system for one-pot pretreatment of four different perennial lignocellulosic biomass and evaluation of their bioethanol production potential. Bioresour Technol 269:227–236. https://doi.org/10.1016/J.BIORTECH.2018.08.091
Knopp D, Tang D, Niessner R (2009) Review: Bioanalytical applications of biomolecule-functionalized nanometer-sized doped silica particles. Anal Chim Acta 647(1):14–30. https://doi.org/10.1016/J.ACA.2009.05.037
Konwarh R, Karak N, Misra M (2013) Electrospun cellulose acetate nanofibers: The present status and gamut of biotechnological applications. Biotechnol Adv 31(4):421–437. https://doi.org/10.1016/J.BIOTECHADV.2013.01.002
Korschelt K, Muhammad ], Ta N, Tremel W (2018) AStep intot he Future:A pplications of Nanoparticle Enzyme Mimics. InChem. Eur.J(Vol. 24). www.chemeurj.org
Kumar A, Park GD, Patel SKS, Kondaveeti S, Otari S, Anwar MZ, Kalia VC, Singh Y, Kim SC, Cho BK, Sohn JH, Kim DR, Kang YC, Lee JK (2019) SiO2 microparticles with carbon nanotube-derived mesopores as an efficient support for enzyme immobilization. Chem Eng J 359:1252–1264. https://doi.org/10.1016/J.CEJ.2018.11.052
Kumar N, Nar •, Chauhan S (2021) Nano-Biocatalysts: Potential Biotechnological Applications. Indian J Microbiol 61:441–448. https://doi.org/10.1007/s12088-021-00975-x
Lian X, Fang Y, Joseph E, Wang Q, Li J, Banerjee S, Zhou HC (2017) Enzyme–MOF (metal–organic framework) composites. Chem Soc Rev 46(11):3386–3401
Li J, Wen X (2009) Noncovalent immobilization of manganese peroxidases from P. chrysosporium on carbon nanotubes. Front Environ Sci Eng China 3(3):294–299
Li N, Liu L, Wang K, Niu J, Zhang Z, Dou M, Wang F (2021) Gelatin-Derived 1D Carbon Nanofiber Architecture with Simultaneous Decoration of Single Fe – Nx Sites and Fe/Fe3C Nanoparticles for Efficient Oxygen Reduction. Chem---Eur J 27(42):10987–10997. https://doi.org/10.1002/chem.202100996
Li X, Tian L, Ali Z, Wang W, Zhang Q (2018) Design of flexible dendrimer-grafted flower-like magnetic microcarriers for penicillin G acylase immobilization. J Mater Sci 53(2):937–947. https://doi.org/10.1007/s10853-017-1581-9
Li ZL, Cheng L, Zhang LW, Liu W, Ma WQ, Liu L (2017) Preparation of a novel multi-walled-carbon-nanotube/cordierite composite support and its immobilization effect on horseradish peroxidase. Process Saf Environ Prot 107:463–467
Madhavan A, Sindhu R, Binod P, Sukumaran RK, Pandey A (2017a) Strategies for design of improved biocatalysts for industrial applications. Bioresour Technol 245:1304–1313. https://doi.org/10.1016/J.BIORTECH.2017.05.031
Majumdar S, Keller AA (2021) Omics to address the opportunities and challenges of nanotechnology in agriculture. https://doi.org/10.1080/10643389.2020.1785264
Mancin F, Prins LJ, Pengo P, Pasquato L, Tecilla P, Scrimin P, Wei H (n.d.). molecules Hydrolytic Metallo-Nanozymes: From Micelles and Vesicles to Gold Nanoparticles. https://doi.org/10.3390/molecules21081014
Mandal B, Bhattacharjee H, Mittal N, Sah H, Balabathula P, Thoma LA, Wood GC (2013) Core–shell-type lipid–polymer hybrid nanoparticles as a drug delivery platform. Nanomed Nanotechnol Biol Med 9(4):474–491. https://doi.org/10.1016/J.NANO.2012.11.010
Manea F, Houillon FB, Pasquato L, Scrimin P (2004) Nanozymes: Gold-nanoparticle-based transphosphorylation catalysts. Angewandte Chemie - International Edition 43(45):6165–6169. https://doi.org/10.1002/anie.200460649
Martínez SAH, Melchor-Martínez EM, Hernández JAR, Parra-Saldívar R, Iqbal HM (2022) Magnetic nanomaterials assisted nanobiocatalysis systems and their applications in biofuels production. Fuel 312:122927
Mayyadah S, Abed, Zeinab Abbas Jawad (2022) &. Nanotechnology for Defence Applications.Nature to Nanomaterials.,187–205
Memon AH, Ding R, Yuan Q, Wei Y, Liang H (2019) Facile synthesis of alcalase-inorganic hybrid nanoflowers used for soy protein isolate hydrolysis to improve its functional properties. Food Chem 289:568–574
Meryam Sardar RA (2015) Enzyme Immobilization: An Overview on Nanoparticles as Immobilization Matrix. Biochem Anal Biochem 04(02). https://doi.org/10.4172/2161-1009.1000178
Min K, Yoo YJ (2014) Recent progress in nanobiocatalysis for enzyme immobilization and its application. Biotechnol Bioprocess Eng 19(4):553–567
Misson M, Jin B, Chen, Binghui, Zhang • Hu. (n.d.). Enhancing enzyme stability and metabolic functional ability of b-galactosidase through functionalized polymer nanofiber immobilization. Bioprocess and Biosystems Engineering, 38. https://doi.org/10.1007/s00449-015-1432-5
Misson M, Zhang H, Jin B (2015a) Nanobiocatalyst advancements and bioprocessing applications. J Royal Soc Interface 12(102). https://doi.org/10.1098/rsif.2014.0891
Misson M, Zhang H, Jin B (2015b) Nanobiocatalyst advancements and bioprocessing applications. J Royal Soc Interface 12(102). 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
Mohammadi-Mahani H, Badoei-dalfard A, Karami Z (2021) Synthesis and characterization of cross-linked lipase-metal hybrid nanoflowers on graphene oxide with increasing the enzymatic stability and reusability. Biochem Eng J 172:108038. https://doi.org/10.1016/J.BEJ.2021.108038
Mulko L, Pereyra JY, Rivarola CR, Barbero CA, Acevedo DF (2019) Improving the retention and reusability of Alpha-amylase by immobilization in nanoporous polyacrylamide-graphene oxide nanocomposites. Int J Biol Macromol 122:1253–1261. https://doi.org/10.1016/J.IJBIOMAC.2018.09.078
Murugappan G, Sreeram KJ (2021) Nano-biocatalyst: Bi-functionalization of protease and amylase on copper oxide nanoparticles. Colloids Surf B 197:111386. https://doi.org/10.1016/J.COLSURFB.2020.111386
Nadar SS, Rao P, Rathod VK (2018) Enzyme assisted extraction of biomolecules as an approach to novel extraction technology: A review. Food Res Int 108:309–330. https://doi.org/10.1016/J.FOODRES.2018.03.006
Nair S, Kim J, Crawford B, Kim SH (2007) Improving Biocatalytic Activity of Enzyme-Loaded Nanofibers by Dispersing Entangled Nanofiber Structure. https://doi.org/10.1021/bm061004k
Naveed M, Nadeem F, Mehmood T, Bilal M, Anwar Z, Amjad F (2021) Protease—A Versatile and Ecofriendly Biocatalyst with Multi-Industrial Applications: An Updated Review. Catal Lett 151(2):307–323. https://doi.org/10.1007/s10562-020-03316-7
Nasrollah Ahmadifard JHumbertoC, Murueta A, Abedian-Kenari A, Motamedzadegan, Hadi Jamali (2015) Comparison the effect of three commercial enzymes for enzymatic hydrolysis of two substrates (rice bran protein concentrate and soy-been protein) with SDS-PAGE. J Food Sci Technol. https://doi.org/10.1007/s13197-015-2087-6
Nematian T, Salehi Z, Shakeri A (2020) Conversion of bio-oil extracted from Chlorella vulgaris micro algae to biodiesel via modified superparamagnetic nano-biocatalyst. Renewable Energy 146:1796–1804. https://doi.org/10.1016/J.RENENE.2019.08.048
Neri DFM, Balcão VM, Dourado FOQ, Oliveira JMB, Carvalho LB, Teixeira JA (2011) Immobilized β-galactosidase onto magnetic particles coated with polyaniline: Support characterization and galactooligosaccharides production. J Mol Catal B: Enzymatic 70(1–2):74–80. https://doi.org/10.1016/J.MOLCATB.2011.02.007
Ngo TPN, Zhang W, Wang W, Li Z (2012) Reversible clustering of magnetic nanobiocatalysts for high-performance biocatalysis and easy catalyst recycling. Chem Commun 48(38):4585–4587. https://doi.org/10.1039/c2cc30953j
Nisha S, Karthick SA, Gobi N (2012) (2012). A Review on Methods, Application and Properties of Immobilized Enzyme. Chemical Science Review and Letters, 1(3), 148–155
Olariu CI, Yiu HHP, Bouffier L, Nedjadi T, Costello E, Williams SR, Halloran CM, Rosseinsky MJ (2011) Multifunctional Fe3O4 nanoparticles for targeted bi-modal imaging of pancreatic cancer. J Mater Chem 21(34):12650–12659. https://doi.org/10.1039/c1jm11370d
Oliveira SF, da Luz JMR, Kasuya MCM, Ladeira LO, Junior AC (2018) Enzymatic extract containing lignin peroxidase immobilized on carbon nanotubes: Potential biocatalyst in dye decolourization. Saudi J Biol Sci 25(4):651–659
Pan C, Hu B, Li W, Sun Y, Ye H, Zeng X (2009) Novel and efficient method for immobilization and stabilization of β-d-galactosidase by covalent attachment onto magnetic Fe3O4–chitosan nanoparticles. J Mol Catal B: Enzymatic 61(3–4):208–215. https://doi.org/10.1016/J.MOLCATB.2009.07.003
Patel SN, Sharma M, Lata K, Singh U, Kumar V, Sangwan RS, Singh SP (2016) Improved operational stability of d-psicose 3-epimerase by a novel protein engineering strategy, and d-psicose production from fruit and vegetable residues. Bioresour Technol 216:121–127. https://doi.org/10.1016/J.BIORTECH.2016.05.053
Pavlidis Iv, Patila M, Bornscheuer UT, Gournis D, Stamatis H (2014) Graphene-based nanobiocatalytic systems: recent advances and future prospects. Trends Biotechnol 32(6):312–320. https://doi.org/10.1016/J.TIBTECH.2014.04.004
Pavlidis Iv, Vorhaben T, Tsoufis T, Rudolf P, Bornscheuer UT, Gournis D, Stamatis H (2012) Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials. Bioresour Technol 115:164–171. https://doi.org/10.1016/J.BIORTECH.2011.11.007
Poorakbar E, Shafiee A, Saboury AA, Rad BL, Khoshnevisan K, Ma’mani L, Derakhshankhah H, Ganjali MR, Hosseini M (2018) Synthesis of magnetic gold mesoporous silica nanoparticles core shell for cellulase enzyme immobilization: Improvement of enzymatic activity and thermal stability. Process Biochem 71:92–100. https://doi.org/10.1016/J.PROCBIO.2018.05.012
Prabhu S, Tizazu BZ (2021) A novel approach to biodiesel production and its function attribute improvement: nano-immobilized biocatalysts, nanoadditives, and risk management. Nanomaterials, 425–443. https://doi.org/10.1016/B978-0-12-822401-4.00025-8
Prlainović NZ, Bezbradica DI, Rogan JR, Uskoković PS, Mijin D, Marinković AD (2016) Surface functionalization of oxidized multi-walled carbon nanotubes: Candida rugosa lipase immobilization. C R Chim 19(3):363–370. https://doi.org/10.1016/J.CRCI.2015.10.008
Qiu H, Xu C, Huang X, Ding Y, Qu Y, Gao P (2009) Immobilization of Laccase on Nanoporous Gold: Comparative Studies on the Immobilization Strategies and the Particle Size Effects. https://doi.org/10.1021/jp8090304
Qu Z, Wang Y, Wang W, Yu D (2021) Three-dimensional network structure Co/CNT derived from bimetal MOFs toward efficient electromagnetic wave absorber. Adv Powder Technol 32(12):4599–4608. https://doi.org/10.1016/J.APT.2021.10.010
Reshmy R, Philip E, Sirohi R, Tarafdar A, Arun KB, Madhavan A, Binod P, Kumar Awasthi M, Varjani S, Szakacs G, Sindhu R (2021) Nanobiocatalysts: Advancements and applications in enzyme technology. Bioresour Technol 337:125491. https://doi.org/10.1016/J.BIORTECH.2021.125491
Rodrigues RC, Berenguer-Murcia Á, Carballares D, Morellon-Sterling R, Fernandez-Lafuente R (2021) Stabilization of enzymes via immobilization: Multipoint covalent attachment and other stabilization strategies. Biotechnol Adv 52:107821. https://doi.org/10.1016/J.BIOTECHADV.2021.107821
Ros TG, Van Dillen AJ, Geus JW, Koningsberger DC (2002) Surface oxidation of carbon nanofibres. Chemistry–A Eur J 8(5):1151–1162. https://doi.org/10.1002/1521-3765(20020301)8:5%3C1151::AID-CHEM1151%3E3.0.CO;2-%23
Şahin S (2020) A simple and sensitive hydrogen peroxide detection with horseradish peroxidase immobilized on pyrene modified acid-treated single‐walled carbon nanotubes. J Chem Technol Biotechnol 95(4):1093–1099
Salwan R, Sharma A, Sharma V (2020) Nanomaterial-Immobilized Biocatalysts for Biofuel Production from Lignocellulose Biomass (pp. 213–250). https://doi.org/10.1007/978-981-13-9333-4_9
Silva C, Martins M, Jing S, Fu J, Cavaco-Paulo A (2018) Practical insights on enzyme stabilization. Crit Rev Biotechnol 38:335–350
Sampaio LMP, Padrão J, Faria J, Silva JP, Silva CJ, Dourado F, Zille A (2016) Laccase immobilization on bacterial nanocellulose membranes: Antimicrobial, kinetic and stability properties. Carbohydr Polym 145:1–12. https://doi.org/10.1016/J.CARBPOL.2016.03.009
Seo M-J, Schmidt-Dannert C, Daniellou R (2021) Organizing Multi-Enzyme Systems into Programmable Materials for Biocatalysis. https://doi.org/10.3390/catal11040409
Sharma A, Thatai KS, Kuthiala T, Singh G, Arya SK (2021) Employment of polysaccharides in enzyme immobilization. Reactive and Functional Polymers 167:105005. https://doi.org/10.1016/J.REACTFUNCTPOLYM.2021.105005
Sheldon RA, Brady D, Bode ML (2020) The Hitchhiker’s guide to biocatalysis: recent advances in the use of enzymes in organic synthesis. https://doi.org/10.1039/c9sc05746c
Sheldon RA, Woodley JM (2018) Role of Biocatalysis in Sustainable Chemistry. In Chemical Reviews (Vol. 118, Issue 2, pp. 801–838). American Chemical Society. https://doi.org/10.1021/acs.chemrev.7b00203
Shrestha BK, Shrestha S, Tiwari AP, Kim JI, Ko SW, Kim HJ, Park CH, Kim CS (2017) Bio-inspired hybrid scaffold of zinc oxide-functionalized multi-wall carbon nanotubes reinforced polyurethane nanofibers for bone tissue engineering. Mater Design 133:69–81. https://doi.org/10.1016/J.MATDES.2017.07.049
Simić S, Jeremic S, Djokic L, Božić N, Vujčić Z, Lončar N, Senthamaraikannan R, Babu R, Opsenica IM, Nikodinovic-Runic J (2020) Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines. Enzym Microb Technol 132:109411. https://doi.org/10.1016/J.ENZMICTEC.2019.109411
Singh N, Dhanya BS, Verma ML (2020) Nano-immobilized biocatalysts and their potential biotechnological applications in bioenergy production. Mater Sci Energy Technol 3:808–824. https://doi.org/10.1016/J.MSET.2020.09.006
Singh SB (2018) Enzyme catalysis and its role in food processing industries. In Enzymes in Food Technology: Improvements and Innovations (pp. 143–165). Springer Singapore. https://doi.org/10.1007/978-981-13-1933-4_8
Song N, Ma F, Zhu Y, Chen S, Wang C, Lu X (2018) Fe 3 C/Nitrogen-Doped Carbon Nanofibers as Highly Efficient Biocatalyst with Oxidase-Mimicking Activity for Colorimetric Sensing. https://doi.org/10.1021/acssuschemeng.8b04036
Soni S, Dwivedee BP, Banerjee UC (2020) Tailoring a stable and recyclable nanobiocatalyst by immobilization of surfactant treated Burkholderia cepacia lipase on polyaniline nanofibers for biocatalytic application. Int J Biol Macromol 161:573–586. https://doi.org/10.1016/J.IJBIOMAC.2020.06.002
Su H, Tian Q, Hurd Price CA, Xu L, Qian K, Liu J (2020) Nanoporous core@shell particles: Design, preparation, applications in bioadsorption and biocatalysis. Nano Today 31:100834. https://doi.org/10.1016/J.NANTOD.2019.100834
Suma Y, Kang CS, Kim HS (n.d.). SELECTED PAPERS FROM THE 2ND CONTAMINATED LAND, ECOLOGICAL ASSESSMENT AND REMEDIATION (CLEAR 2014) CONFERENCE: ENVIRONMENTAL POLLUTION AND REMEDIATION Noncovalent and covalent immobilization of oxygenase on single-walled carbon nanotube for enzymatic decomposition of aromatic hydrocarbon intermediates. https://doi.org/10.1007/s11356-015-4168-5
Syed F, Ali K, Asad MJ, Fraz MG, Khan Z, Imran M, 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
Tacias-Pascacio VG, Morellon-Sterling R, Siar EH, Tavano O, Berenguer-Murcia Á, Fernandez-Lafuente R (2020) Use of Alcalase in the production of bioactive peptides: A review. Int J Biol Macromol (Vol 165:2143–2196. https://doi.org/10.1016/j.ijbiomac.2020.10.060. Elsevier B.V
Tai Duc Tran & Moon Il Kim (2018) Organic-Inorganic Hybrid Nanoflowers as Potent Materials for Biosensing and Biocatalytic Applications. BioChip 12:268–279. https://doi.org/10.1007/s13206-018-2409-7
Tapdigov SZ (2021) The bonding nature of the chemical interaction between trypsin and chitosan based carriers in immobilization process depend on entrapped method: A review. Int J Biol Macromol 183:1676–1696. https://doi.org/10.1016/J.IJBIOMAC.2021.05.059
Unsworth LD, van der Oost J, Koutsopoulos S (2007) Hyperthermophilic enzymes) stability, activity and implementation strategies for high temperature applications. https://doi.org/10.1111/j.1742-4658.2007.05954.x
Verma ML, Abraham RE, Puri M (2020) Nanobiocatalyst designing strategies and their applications in food industry. Biomass Biofuels Biochemicals 171–189. https://doi.org/10.1016/B978-0-12-819820-9.00010-7
Verma ML, Puri M, Barrow CJ (2016) Recent trends in nanomaterials immobilised enzymes for biofuel production. Critical Reviews in Biotechnology, vol 36. Taylor and Francis Ltd, pp 108–119. 1 https://doi.org/10.3109/07388551.2014.928811
Wang H-L, Yeh H, Chen Y-C, Lai Y-C, Lin C-Y, Lu K-Y, Ho R-M, Li B-H, Lin C-H, Tsai D-H (2018) Thermal Stability of Metal – Organic Frameworks and Encapsulation of CuO Nanocrystals for Highly Active Catalysis. https://doi.org/10.1021/acsami.7b17389
Wang X, Liu X, Zhao C, Ding Y, Xu P (2011) Biodiesel production in packed-bed reactors using lipase–nanoparticle biocomposite. Bioresour Technol 102(10):6352–6355. https://doi.org/10.1016/J.BIORTECH.2011.03.003
Wani TU, Rather AH, Khan S, Beigh R, Park MA, Pant M, Sheikh FA (2021) catalysts Strategies to Use Nanofiber Scaffolds as Enzyme-Based Biocatalysts in Tissue Engineering Applications. https://doi.org/10.3390/catal11050536
Wehaidy HR, Abdel-Naby MA, El-Hennawi HM, Youssef HF (2019) Nanoporous Zeolite-X as a new carrier for laccase immobilization and its application in dyes decolorization. Biocatal Agric Biotechnol 19:101135. https://doi.org/10.1016/J.BCAB.2019.101135
Wei S, Zhang J, Li S, Ma X (2021) “Ship-in-a-Bottle” Strategy for Immobilization of 9-Amino(9-deoxy)epi-Cinchona Alkaloid into Molecularly Imprinted Solid Acid: Acetal Hydrolysis/Asymmetric Aldol Tandem Reaction. ChemCatChem 13(2):627–636. https://doi.org/10.1002/cctc.202001402
Wu L, Wu S, Xu Z, Qiu Y, Li S, Xu H (2016) Modified nanoporous titanium dioxide as a novel carrier for enzyme immobilization. Biosens Bioelectron 80:59–66. https://doi.org/10.1016/J.BIOS.2016.01.045
Xue R, Woodley JM (2012) Process technology for multi-enzymatic reaction systems. Bioresour Technol 115:183–195. https://doi.org/10.1016/J.BIORTECH.2012.03.033
Yang M, Li H, Javadi A, Gong S (2010) Multifunctional mesoporous silica nanoparticles as labels for the preparation of ultrasensitive electrochemical immunosensors. Biomaterials 31(12):3281–3286. https://doi.org/10.1016/J.BIOMATERIALS.2010.01.033
Ye R, Zhao J, Wickemeyer BB, Toste FD, Somorjai GA (2018) Foundations and strategies of the construction of hybrid catalysts for optimized performances. In Nature Catalysis (Vol. 1, Issue 5, pp. 318–325). Nature Publishing Group. https://doi.org/10.1038/s41929-018-0052-2
Yiu HHP, Keane MA (2012) Enzyme-magnetic nanoparticle hybrids: new effective catalysts for the production of high value chemicals. https://doi.org/10.1002/jctb.3735
Yuan H, Chen L, Cao Z, Hong FF (2020) Enhanced decolourization efficiency of textile dye Reactive Blue 19 in a horizontal rotating reactor using strips of BNC-immobilized laccase: Optimization of conditions and comparison of decolourization efficiency. Biochem Eng J 156:107501. https://doi.org/10.1016/J.BEJ.2020.107501
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 Engineering: C 103:109789. https://doi.org/10.1016/J.MSEC.2019.109789
Zhai R, Zhang B, Wan Y, Li C, Wang J, Liu J (2013) Chitosan–halloysite hybrid-nanotubes: Horseradish peroxidase immobilization and applications in phenol removal. Chem Eng J 214:304–309
Zhang H, Misson M, Jin B (2015) Nanobiocatalyst advancements and bioprocessing applications. https://doi.org/10.1098/rsif.2014.0891
Zhang C, Cai X (2019) Immobilization of horseradish peroxidase on Fe3O4/nanotubes composites for Biocatalysis-degradation of phenol. Compos Interfaces 26(5):379–396
Zhong L, Jiao X, Hu H, Shen X, Zhao J, Feng Y, Jia S (2021) Activated magnetic lipase-inorganic hybrid nanoflowers: A highly active and recyclable nanobiocatalyst for biodiesel production. Renewable Energy 171:825–832
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Consejo Nacional de Ciencia y Tecnología (CONACyT) Mexico is thankfully acknowledged for partially supporting this work under Sistema Nacional de Investigadores (SNI) program awarded to Hafiz M. N. Iqbal (CVU: 735340).
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Ayub, J., Saeed, M.U., Hussain, N. et al. Designing robust nano-biocatalysts using nanomaterials as multifunctional carriers - expanding the application scope of bio-enzymes. Top Catal 66, 625–648 (2023). https://doi.org/10.1007/s11244-022-01657-8
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DOI: https://doi.org/10.1007/s11244-022-01657-8