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Review Article

Multi-point enzyme immobilization, surface chemistry, and novel platforms: a paradigm shift in biocatalyst design

ORCID Icon, , , & ORCID Icon
Pages 202-219 | Received 29 Apr 2018, Accepted 06 Sep 2018, Published online: 04 Nov 2018

References

  • Biermann U, Bornscheuer U, Meier MA. Oils and fats as renewable raw materials in chemistry. Angew Chem Int Ed. 2011;50:3854–3871.
  • Kircher M. The emerging bioeconomy: industrial drivers, global impact, and international strategies. Ind Biotechnol. 2014;10:11–18.
  • Santos JCSD, Barbosa O, Ortiz C. Importance of the support properties for immobilization or purification of enzymes. ChemCatChem. 2015;7:2413–2432.
  • Fernandez-Lafuente R. Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme Microb Technol. 2009;45:405–418.
  • Gröger H, Hummel W. Combining the ‘two worlds’ of chemocatalysis and biocatalysis towards multi-step one-pot processes in aqueous media. Curr Opin Chem Biol. 2014;19:171–179.
  • Sheldon RA, van Pelt S. Enzyme immobilisation in biocatalysis: why, what and how. Chem Soc Rev. 2013;42:6223–6235.
  • Wohlgemuth R. Biocatalysis-key to sustainable industrial chemistry. Curr Opin Biotechnol. 2010;21:713–724.
  • Asgher M, Shahid M, Kamal S, et al. Recent trends and valorization of immobilization strategies and ligninolytic enzymes by industrial biotechnology. J Mol Catal B: Enzym. 2014;101:56–66.
  • Amin F, Bhatti HN, Bilal M, et al. Improvement of activity, thermo-stability and fruit juice clarification characteristics of fungal exo-polygalacturonase. Int J Biol Macromol. 2017;95:974–984.
  • Bilal M, Asgher M, Parra-Saldivar R, et al. Immobilized ligninolytic enzymes: an innovative and environmental responsive technology to tackle dye-based industrial pollutants–a review. Sci Total Environ. 2017;576:646–659.
  • Rehman S, Wang P, Bhatti HN, et al. Improved catalytic properties of Penicillium notatum lipase immobilized in nanoscale silicone polymeric films. Int J Biol Macromol. 2017;97:279–286.
  • Bilal M, Iqbal HMN, Shuqi G, et al. State-of-the-art protein engineering approaches using biological macromolecules: a review from immobilization to implementation view point. Int J Biol Macromol. 2018;108:893–901.
  • Bilal M, Rasheed T, Iqbal HMN, et al. Peroxidases-assisted removal of environmentally-related hazardous pollutants with reference to the reaction mechanisms of industrial dyes. Sci Total Environ. 2018;644:1–13.
  • Bilal M, Rasheed T, Zhao Y, et al. Smart chemistry and its application in peroxidase immobilization using different support materials. Int J Biol Macromol. 2018;119:278–290.
  • Tsutsumi M, Tsuse N, Fujieda N, et al. Site-directed mutation at residues near the catalytic site of histamine dehydrogenase from Nocardioides simplex and its effects on substrate inhibition. J Biochem. 2010;147:257–264.
  • Kumar A, Singh S. Directed evolution: tailoring biocatalysts for industrial applications. Crit Rev Biotechnol. 2013;33:365–378.
  • Kumar L, Awasthi G, Singh B. Extremophiles: a novel source of industrially important enzymes. Biotechnology. 2011;10:121–135.
  • Sheldon RA. Enzyme immobilization: the quest for optimum performance. Adv Synth Catal. 2007;349:1289–1307.
  • Hanefeld U, Gardossi L, Magner E. Understanding enzyme immobilisation. Chem Soc Rev. 2009;38:453–468.
  • Tran DN, Balkus KJ. Perspective of recent progress in immobilization of enzymes. ACS Catal. 2011;1:956–968.
  • Mateo C, Palomo JM, Fernandez-Lorente G, et al. Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb Technol. 2007;40:1451–1463.
  • Iyer PV, Ananthanarayan L. Enzyme stability and stabilization—aqueous and non-aqueous environment. Process Biochem. 2008;43:1019–1032.
  • Liese A, Hilterhaus L. Evaluation of immobilized enzymes for industrial applications. Chem Soc Rev. 2013;42:6236–6249.
  • Hartmann M, Jung D. Biocatalysis with enzymes immobilized on mesoporous hosts: the status quo and future trends. J Mater Chemi. 2010;20:844–857.
  • Cao L. Immobilised enzymes: science or art? Curr Opin Chem Biol. 2005;9:217–226. 2005;
  • Jesionowski T, Zdarta J, Krajewska B. Enzyme immobilization by adsorption: a review. Adsorption. 2014;20:801–821.
  • Hernandez K, Fernandez-Lafuente R. Control of protein immobilization: coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance. Enzyme Microb Technol. 2011;48:107–122.
  • Barbosa O, Torres R, Ortiz C, et al. Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties. Biomacromolecules. 2013;14:2433–2462.
  • Santos JCD, Rueda N, Barbosa O, et al. Characterization of supports activated with divinyl sulfone as a tool to immobilize and stabilize enzymes via multipoint covalent attachment. Application to chymotrypsin. RSC Adv. 2015;5:20639–20649.
  • Cha T, Guo A, Zhu XY. Enzymatic activity on a chip: the critical role of protein orientation. Proteomics. 2005;5:416–419.
  • Seong SY, Choi CY. Current status of protein chip development in terms of fabrication and application. Proteomics. 2003;3:2176–2189.
  • Camarero JA. Recent developments in the site-specific immobilization of proteins onto solid supports . Pept Sci. 2008;90:450–458.
  • Peluso P, Wilson DS, Do D, et al. Optimizing antibody immobilization strategies for the construction of protein microarrays. Anal Biochem. 2003;312:113–124.
  • Soellner MB, Dickson KA, Nilsson BL, et al. Site-specific protein immobilization by Staudinger ligation. J Am Chem Soc. 2003;125:11790–11791.
  • Butterfield DA, Bhattacharyya D, Daunert S, et al. Catalytic biofunctional membranes containing site-specifically immobilized enzyme arrays: a review. J Membr Sci. 2001;181:29–37.
  • Srere PA, Uyeda K. [2] Functional groups on enzymes suitable for binding to matrices. Meth Enzymol. 1976;44:11–19. Academic Press.
  • Brady D, Jordaan J. Advances in enzyme immobilisation. Biotechnol Lett. 2009;31:1639
  • Zucca P, Sanjust E. Inorganic materials as supports for covalent enzyme immobilization: methods and mechanisms. Molecules. 2014;19:14139–14194.
  • Hwang ET, Gu MB. Enzyme stabilization by nano/microsized hybrid materials. Eng Life Sci. 2013;13:49–61.
  • Guisán J. Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes. Enzyme Microb Technol. 1988;10:375–382.
  • Pedroche J, del Mar Yust M, Mateo C, et al. Effect of the support and experimental conditions in the intensity of the multipoint covalent attachment of proteins on glyoxyl-agarose supports: correlation between enzyme–support linkages and thermal stability. Enzyme Microb Technol. 2007;40:1160–1166.
  • Salis A, Pisano M, Monduzzi M, et al. Laccase from Pleurotus sajor-caju on functionalised SBA-15 mesoporous silica: Immobilisation and use for the oxidation of phenolic compounds. J Mol Catal B: Enzym. 2009;58:175–180.
  • Betancor L, López-Gallego F, Hidalgo A, et al. Different mechanisms of protein immobilization on glutaraldehyde activated supports: effect of support activation and immobilization conditions. Enzyme Microb Technol. 2006;39:877–882.
  • Melo RRD, Alnoch RC, Vilela AFL, et al. New heterofunctional supports based on glutaraldehyde-activation: a tool for enzyme immobilization at neutral pH. Molecules. 2017;22:1088.
  • Mateo C, Abian O, Bernedo M, et al. Some special features of glyoxyl supports to immobilize proteins. Enzyme Microb Technol. 2005;37:456–462.
  • Bolivar JM, Mateo C, Godoy C, et al. The co-operative effect of physical and covalent protein adsorption on heterofunctional supports. Process Biochem. 2009;44:757–763.
  • Liu Y, Guo C, Wang F, et al. Preparation of magnetic silica nanoparticles and their application in laccase immobilization. Chinese J Process Eng. 2008;8:583–588.
  • Bryjak J, Kruczkiewicz P, Rekuc A, et al. Laccase immobilization on copolymer of butyl acrylate and ethylene glycol dimethacrylate. Biochem Eng J. 2007;35:325–332.
  • Kumar AK, Goswami P. Dissociation and reconstitution studies of a broad substrate specific multimeric alcohol oxidase protein produced by Aspergillus terreus. J Biochem. 2009;145:259–265.
  • Barzegar A, Moosavi-Movahedi AA, Pedersen JZ, et al. Comparative thermostability of mesophilic and thermophilic alcohol dehydrogenases: stability-determining roles of proline residues and loop conformations. Enzyme Microb Technol. 2009;45:73–79.
  • Poltorak OM, Chukhrai ES, Kozlenkov AA, et al. The putative common mechanism for inactivation of alkaline phosphatase isoenzymes. J Mol Catal B: Enzym. 1999;7:157–163.
  • Pilipenko OS, Atyaksheva LF, Poltorak OM, et al. Dissociation and catalytic activity of oligomer forms of β-galactosidases. Russ J Phys Chem. 2007;81:990–994.
  • Eijsink VG, Bjørk A, Gåseidnes S, et al. Rational engineering of enzyme stability. J Biotechnol. 2004;113:105–120.
  • Balcão VM, Vila MM. Structural and functional stabilization of protein entities: state-of-the-art. Adv Drug Deliv Rev. 2015;93:25–41.
  • López-Gallego F, Betancor L, Hidalgo A, et al. Optimization of an industrial biocatalyst of glutaryl acylase: stabilization of the enzyme by multipoint covalent attachment onto new amino-epoxy Sepabeads. J Biotechnol. 2004;111:219–227.
  • Lopez-Gallego F, Betancor L, Hidalgo A, et al. Stabilization of different alcohol oxidases via immobilization and post immobilization techniques. Enzyme Microb Technol. 2007;40:278–284.
  • Bernal C, Sierra L, Mesa M. Improvement of thermal stability of β-galactosidase from Bacillus circulans by multipoint covalent immobilization in hierarchical macro-mesoporous silica. J Mol Catal B: Enzym. 2012;84:166–172.
  • Grazu V, López-Gallego F, Guisán JM. Tailor-made design of penicillin G acylase surface enables its site-directed immobilization and stabilization onto commercial mono-functional epoxy supports. Process Biochem. 2012;47:2538–2541.
  • Pessela BC, Mateo C, Carrascosa AV, et al. One-step purification, covalent immobilization, and additional stabilization of a thermophilic poly-His-tagged β-galactosidase from Thermus sp. Strain T2 by using novel heterofunctional chelate − epoxy Sepabeads. Biomacromolecules. 2003;4:107–113.
  • Mateo C, Fernández-Lorente G, Abian O, et al. Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage. Biomacromolecules. 2000;1:739–745.
  • Singh V, Srivastava P, Singh A, et al. Polysaccharide-silica hybrids: design and applications. Polym Rev. 2016;56:113–136.
  • Hu C, Wang N, Zhang W, et al. Immobilization of Aspergillus terreus lipase in self-assembled hollow nanospheres for enantioselective hydrolysis of ketoprofen vinyl ester. J Biotechnol. 2015;194:12–18.
  • Cipolatti EP, Valerio A, Henriques RO, et al. Nanomaterials for biocatalyst immobilization–state of the art and future trends. RSC Adv. 2016;6:104675–104692.
  • Cunha MNM, Felgueiras HP, Gouveia I, et al. Synergistically enhanced stability of laccase immobilized on synthesized silver nanoparticles with water-soluble polymers. Colloids Surf B Biointerfaces. 2017;154:210–220.
  • Patel SK, Kalia VC, Choi JH, et al. Immobilization of laccase on SiO2 nanocarriers improves its stability and reusability. J Microbiol Biotechnol. 2014;24:639–647.
  • Ni Y, Li J, Huang Z, et al. Improved activity of immobilized horseradish peroxidase on gold nanoparticles in the presence of bovine serum albumin. J Nanopart Res. 2013;15:2038.
  • Petkova GA, Záruba К, Žvátora P, et al. Gold and silver nanoparticles for biomolecule immobilization and enzymatic catalysis. Nanoscale Res Lett. 2012;7:287.
  • Mahmoud KA, Male KB, Hrapovic S, et al. Cellulose nanocrystal/gold nanoparticle composite as a matrix for enzyme immobilization. ACS Appl Mater Interfaces. 2009;1:1383–1386.
  • Chen YZ, Ching CB, Xu R. Lipase immobilization on modified zirconia nanoparticles: Studies on the effects of modifiers. Process Biochem. 2009;44:1245–1251.
  • Kim MI, Ham HO, Oh SD, et al. Immobilization of Mucor javanicus lipase on effectively functionalized silica nanoparticles. J Mol Catal B: Enzym. 2006;39:62–68.
  • Kotal M, Srivastava SK, Maiti TK. Fabrication of gold nanoparticle assembled polyurethane microsphere template in trypsin immobilization. J Nanosci Nanotechnol. 2011;11:10149–10157.
  • Bolibok P, Wiśniewski M, Roszek K, et al. Controlling enzymatic activity by immobilization on graphene oxide. Naturwissenschaften. 2017;104:36.
  • Hou J, Dong G, Xiao B, et al. Preparation of titania based biocatalytic nanoparticles and membranes for CO2 conversion. J Mater Chem A. 2015;3:3332–3342.
  • Garmroodi M, Mohammadi M, Ramazani A, et al. Covalent binding of hyper-activated Rhizomucor miehei lipase (RML) on hetero-functionalized siliceous supports. Int J Biol Macromol. 2016;86:208–215.
  • Kim J, Jia H, Wang P. Challenges in biocatalysis for enzyme-based biofuel cells. Biotechnol Adv. 2006;24:296–308.
  • Li XS, Zhu GT, Luo YB, et al. Synthesis and applications of functionalized magnetic materials in sample preparation. TrAC, Trends Anal Chem. 2013;45:233–247.
  • Liu DM, Chen J, Shi YP. Advances on methods and easy separated support materials for enzymes immobilization. TrAC, Trends Anal Chem. 2018;102:332–342.
  • Gao J, Wang AR, Jiang XP, et al. Preparation of expoxy-functionalized magnetic nanoparticles for immobilization of glycerol dehydrogenase. J Nanosci Nanotechnol. 2018;18:4852–4857.
  • Hosseini SH, Hosseini SA, Zohreh N, et al. Covalent immobilization of cellulase using magnetic poly(ionic liquid) support: improvement of the enzyme activity and stability. J Agric Food Chem. 2018;66:789–798.
  • Zhou Y, Yuan S, Liu Q, et al. Synchronized purification and immobilization of his-tagged β-glucosidase via Fe3O4/PMG core/shell magnetic nanoparticles. Sci Rep. 2017;7:41741.
  • Mohamed SA, Al-Harbi MH, Almulaiky YQ, et al. Immobilization of horseradish peroxidase on Fe3O4 magnetic nanoparticles. Electron J Biotechnol. 2017;27:84–90.
  • Song C, Sheng L, Zhang X. Immobilization and characterization of a thermostable lipase. Mar Biotechnol. 2013;15:659–667.
  • Kalkan NA, Aksoy S, Aksoy EA, et al. Preparation of chitosan‐coated magnetite nanoparticles and application for immobilization of laccase. J Appl Polym Sci. 2012;123:707–716.
  • Namdeo M, Bajpai SK. Immobilization of α-amylase onto cellulose-coated magnetite (CCM) nanoparticles and preliminary starch degradation study. J Mol Catal B: Enzym. 2009;59:134–139.
  • Huang SH, Liao MH, Chen DH. Direct binding and characterization of lipase onto magnetic nanoparticles. Biotechnol Prog. 2003;19:1095–1100.
  • Zhang Y, Wu C, Guo S, et al. Interactions of graphene and graphene oxide with proteins and peptides. Nanotechnol Rev. 2013;2:27–45.
  • Tseng CW, Liao CY, Sun Y, et al. Immobilization of Clostridium cellulolyticum D-psicose 3-epimerase on artificial oil bodies. J Agric Food Chem. 2014;62:6771–6776.
  • Lee KH, Lee B, Hwang SJ, et al. Large scale production of highly conductive reduced graphene oxide sheets by a solvent-free low temperature reduction. Carbon. 2014;69:327–335.
  • Dedania SR, Patel MJ, Patel DM, et al. Immobilization on graphene oxide improves the thermal stability and bioconversion efficiency of D-psicose 3-epimerase for rare sugar production. Enzyme Microb Technol. 2017;107:49–56.
  • Vineh MB, Saboury AA, Poostchi AA, et al. Stability and activity improvement of horseradish peroxidase by covalent immobilization on functionalized reduced graphene oxide and biodegradation of high phenol concentration. Int J Biol Macromol. 2018;106:1314–1322.
  • Ormategui N, Veloso A, Leal GP, et al. Design of stable and powerful nanobiocatalysts, based on enzyme laccase immobilized on self-assembled 3D graphene/polymer composite hydrogels. ACS Appl Mater Interfaces. 2015;7:14104–14112.
  • Matuszek K, Chrobok A, Latos P, et al. Silica-supported chlorometallate (III) ionic liquids as recyclable catalysts for Diels–Alder reaction under solventless conditions. Catal Sci Technol. 2016;6:8129–8137.
  • Hartmann M. Ordered mesoporous materials for bioadsorption and biocatalysis. Chem Mater. 2005;17:4577–4593.
  • Yiu HH, Wright PA, Botting NP. Enzyme immobilisation using siliceous mesoporous molecular sieves. Microporous Mesoporous Mater. 2001;44–45:763–768.
  • Moritz M, Geszke-Moritz M. Mesoporous materials as multifunctional tools in biosciences: principles and applications. Mater Sci Eng C. 2015;49:114–151.
  • Cai C, Gao Y, Liu Y, et al. Immobilization of Candida antarctica lipase B onto SBA-15 and their application in glycerolysis for diacylglycerols synthesis. Food Chem. 2016;212:205–212.
  • Zhuang H, Dong S, Zhang T, et al. Study on alkaline protease immobilized on mesoporous materials. Asian J Chem. 2014;26:1139–1144.
  • Mangrulkar PA, Yadav R, Meshram JS, et al. Tyrosinase-immobilized MCM-41 for the detection of phenol. Water Air Soil Pollut. 2012;223:819–825.
  • Chang RHY, Jang J, Wu KCW. Cellulase immobilized mesoporous silica nanocatalysts for efficient cellulose-to-glucose conversion. Green Chem. 2011;13:2844–2850.
  • Pandya PH, Jasra RV, Newalkar BL, et al. Studies on the activity and stability of immobilized α-amylase in ordered mesoporous silicas. Microporous Mesoporous Mater. 2005;77:67–77.
  • Ota S, Miyazaki S, Matsuoka H, et al. High-throughput protein digestion by trypsin-immobilized monolithic silica with pipette-tip formula. J Biochem Biophys Methods. 2007;70:57–62.
  • Caldas EM, Novatzky D, Deon M, et al. Pore size effect in the amount of immobilized enzyme for manufacturing carbon ceramic biosensor. Microporous Mesoporous Mater. 2017;247:95–102.
  • Ebrahimi M, Placido L, Engel L, et al. A novel ceramic membrane reactor system for the continuous enzymatic synthesis of oligosaccharides. Desalination. 2010;250:1105–1108.
  • Wang W, Li Z, Liu W, et al. Horseradish peroxidase immobilized on the silane-modified ceramics for the catalytic oxidation of simulated oily water. Sep Purif Technol. 2012;89:206–211.
  • Wang ZG, Wan LS, Liu ZM, et al. Enzyme immobilization on electrospun polymer nanofibers: an overview. J Mol Catal B: Enzym. 2009;56:189–195.
  • Dai Y, Yao J, Song Y, et al. Enhanced performance of immobilized laccase in electrospun fibrous membranes by carbon nanotubes modification and its application for bisphenol A removal from water. J Hazard Mater. 2016;317:485–493.
  • Bhardwaj N, Kundu SC. Electrospinning: a fascinating fiber fabrication technique. Biotechnol Adv. 2010;28:325–347.
  • Wong DE, Dai M, Talbert JN, et al. Biocatalytic polymer nanofibers for stabilization and delivery of enzymes. J Mol Catal B: Enzym. 2014;110:16–22.
  • Kim J, Grate JW, Wang P. Nanobiocatalysis and its potential applications. Trends Biotechnol. 2008;26:639–646.
  • Saallah S, Naim MN, Lenggoro IW, et al. Immobilisation of cyclodextrin glucanotransferase into polyvinyl alcohol (PVA) nanofibres via electrospinning. Biotechnol Rep. 2016;10:44–48.
  • Feng Q, Zhao Y, Wei A, et al. Immobilization of catalase on electrospun PVA/PA6-Cu(II) nanofibrous membrane for the development of efficient and reusable enzyme membrane reactor. Environ Sci Technol. 2014;48:10390–10397.
  • Demirkan E, Avci T, Aykut Y. Protease immobilization on cellulose monoacetate/chitosan-blended nanofibers. J Ind Text. 2018;47:2092–2111.
  • Martrou G, Léonetti M, Gigmes D, et al. One-step preparation of surface modified electrospun microfibers as suitable supports for protein immobilization. Polym Chem. 2017;8:1790–1796.
  • Fazel R, Torabi SF, Naseri-Nosar P, et al. Electrospun polyvinyl alcohol/bovine serum albumin biocomposite membranes for horseradish peroxidase immobilization. Enzyme Microbial Technol. 2016;93-94:1–10.
  • Srbová J, Slováková M, Křípalová Z, et al. Covalent biofunctionalization of chitosan nanofibers with trypsin for high enzyme stability. React Funct Polym. 2016;104:38–44.
  • Pinto SC, Rodrigues AR, Saraiva JA, et al. Catalytic activity of trypsin entrapped in electrospun poly (ϵ-caprolactone) nanofibers. Enzyme Microb Technol. 2015;79-80:8–18.
  • Lee KH, Ki CS, Baek DH, et al. Application of electrospun silk fibroin nanofibers as an immobilization support of enzyme. Fibers Polym. 2005;6:181–185.
  • Xie J, Hsieh YL. Ultra-high surface fibrous membranes from electrospinning of natural proteins: casein and lipase enzyme. J Mater Sci. 2003;38:2125–2133.
  • Nair S, Kim J, Crawford B, et al. Improving biocatalytic activity of enzyme-loaded nanofibers by dispersing entangled nanofiber structure. Biomacromolecules. 2007;8:1266–1270.
  • Sóti PL, Weiser D, Vigh T, et al. Electrospun polylactic acid and polyvinyl alcohol fibers as efficient and stable nanomaterials for immobilization of lipases. Bioprocess Biosyst Eng. 2016;39:449–459.
  • Weiser D, Sóti PL, Bánóczi G, et al. Bioimprinted lipases in PVA nanofibers as efficient immobilized biocatalysts. Tetrahedron. 2016;72:7335–7342.
  • Canbolat MF, Savas HB, Gultekin F. Improved catalytic activity by catalase immobilization using γ‐cyclodextrin and electrospun PCL nanofibers. J Appl Polym Sci. 2017;134:318–326.
  • Yudianti R, Onggo H, Saito Y, et al. Analysis of functional group sited on multi-wall carbon nanotube surface. TOMSJ. 2011;5:242–247.
  • Koster AJ, Ziese U, Verkleij AJ, et al. Three-dimensional transmission electron microscopy: a novel imaging and characterization technique with nanometer scale resolution for materials science. J Phys Chem B. 2000;104:9368–9370.
  • Noureddini H, Gao X. Characterization of sol-gel immobilized lipases. J Sol-Gel Sci Technol. 2007;41:31–41.
  • Rajan A, Sudha JD, Abraham TE. Enzymatic modification of cassava starch by fungal lipase. Ind Crops Prod. 2008;27:50–59.
  • Kumar V, Yadav S, Jahan F, et al. Organic synthesis of maize starch-based polymer using Rhizopus oryzae lipase, scale up, and its characterization. Prep Biochem Biotechnol. 2014;44:321–331.
  • Huang L, Cheng ZM. Immobilization of lipase on chemically modified bimodal ceramic foams for olive oil hydrolysis. Chem Eng J. 2008;144:103–109.
  • Verma ML, Naebe M, Barrow CJ, et al. Enzyme immobilisation on amino-functionalised multi-walled carbon nanotubes: structural and biocatalytic characterisation. PLoS One. 2013;8:e73642.
  • Marcuello C, De Miguel R, Gómez-Moreno C, et al. An efficient method for enzyme immobilization evidenced by atomic force microscopy. Protein Eng Des Sel. 2012;25:715–723.
  • Brundle CR, Conti G, Mack P. XPS and angle resolved XPS, in the semiconductor industry: characterization and metrology control of ultra-thin films. J Electron Spectrosc Relat Phenom. 2010;178–179:433–448.
  • Zhang YW, Prabhu P, Lee JK. Alginate immobilization of recombinant Escherichia coli whole cells harboring L-arabinose isomerase for L-ribulose production. Bioprocess Biosyst Eng. 2010;33:741–748.

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