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Bioprocess and Biosystems Engineering

, Volume 41, Issue 5, pp 739–748 | Cite as

Quick separation and enzymatic performance improvement of lipase by ionic liquid-modified Fe3O4 carrier immobilization

  • Xia Jiaojiao
  • Zou Bin
  • Zhu Gangbin
  • Wei Ping
  • Liu Zhenjiang
Research Paper

Abstract

To promote the activity and stability of immobilized porcine pancreatic lipase (PPL), novel carrier was combined with special immobilization method. Enzymatic activity was enhanced after immobilized onto ionic liquid modified magnetic Fe3O4 by electrostatic adsorption. Activity of immobilized enzyme (PPL-IM/BF4-Fe3O4@CA) reached 596 U/g PPL. Through the combination of electrostatic adsorption and embedding immobilization methods, we improve binding force between the carrier and enzyme, and further enhance the efficiency and stability of immobilized enzyme. The activity of PPL-IM/BF4-Fe3O4@CA after repeated third use was 78%. After storage at room temperature for 5 days, the residual activity was 89%. Enzymatic properties and catalytic kinetics of immobilized enzymes were studied, and the effect mechanism of ionic liquid modified Fe3O4 on PPL was revealed. The effect of ionic liquid on the carrier structure was investigated by characterization of XRD, FT-IR, SEM and TG. The mechanism and enzymatic properties of immobilized PPL via electrostatic adsorption and embedding were analyzed. A novel and efficient immobilized PPL was developed.

Keywords

Immobilization Fe3O4 Ionic liquid Lipase Surface modification 

Notes

Acknowledgements

The work was funded by the National Natural Science Foundation of China (no. 21406093), the Natural Science Foundation of Jiangsu province (BK20140529), Key University Science Research Project of Jiangsu Province (14KJB530001), China Postdoctoral Science Foundation (2014M550271), and the Project Funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions.

References

  1. 1.
    Cazaban D, Wilson L, Betancor L (2017) Lipase immobilization on siliceous supports: application to synthetic reactions. Curr Org Chem 21:96–103CrossRefGoogle Scholar
  2. 2.
    Lustosa de Melo Carvalho AC, Fonseca TDS, de Mattos MC, Ferreira de Oliveira MDC, Gomes de Lemos TL, Molinari F, Romano D, Serra I (2015) Recent advances in lipase-mediated preparation of pharmaceuticals and their intermediates. Int J Mol Sci 16:29682–29716CrossRefGoogle Scholar
  3. 3.
    Sankaran R, Show PL, Chang J-S (2016) Biodiesel production using immobilized lipase: feasibility and challenges. Biofuel Bioprod Bior 10:896–916CrossRefGoogle Scholar
  4. 4.
    Grigoras AG (2017) Catalase immobilization—a review. Biocheml Eng J 117:1–20CrossRefGoogle Scholar
  5. 5.
    Dicosimo R, Mcauliffe J, Poulose AJ, Bohlmann G (2013) Industrial use of immobilized enzymes. Chem Soc Rev 42:6437–6447CrossRefGoogle Scholar
  6. 6.
    Sheldon RA, Van PS (2013) Enzyme immobilisation in biocatalysis: why, what and how. Chem Soc Rev 42:6223–6229CrossRefGoogle Scholar
  7. 7.
    Manoel EA, Santos JCSD., Freire DMG, Rueda N, Fernandez-Lafuente R (2015) Immobilization of lipases on hydrophobic supports involves the open form of the enzyme. Enzyme Microb Technol 71:53–59CrossRefGoogle Scholar
  8. 8.
    Badgujar KC, Bhanage BM (2017) Investigation of deactivation thermodynamics of lipase immobilized on polymeric carrier. Bioproc Biosyst Eng 40:741–757CrossRefGoogle Scholar
  9. 9.
    Tacias-Pascacio VG, Virgen-Ortiz JJ, Jimenez-Perez M, Yates M, Torrestiana-Sanchez B, Rosales-Quintero A, Fernandez-Lafuente R (2017) Evaluation of different lipase biocatalysts in the production of biodiesel from used cooking oil: critical role of the immobilization support. Fuel 200:1–10CrossRefGoogle Scholar
  10. 10.
    Zheng M, Wang S, Xiang X, Shi J, Huang J, Deng Q, Huang F, Xiao J (2017) Facile preparation of magnetic carbon nanotubes-immobilized lipase for highly efficient synthesis of 1,3-dioleoyl-2-palmitoylglycerol-rich human milk fat substitutes. Food Chem 228:476–483CrossRefGoogle Scholar
  11. 11.
    Mendes AA, Oliveira PC, Castro HFD (2012) Properties and biotechnological applications of porcine pancreatic lipase. J Mol Catal B Enzym 78:119–134CrossRefGoogle Scholar
  12. 12.
    Gao J, Kong W, Zhou L, He Y, Ma L, Wang Y, Yin L, Jiang Y (2017) Monodisperse core-shell magnetic organosilica nanoflowers with radial wrinkle for lipase immobilization. Chem Eng J 309:70–79CrossRefGoogle Scholar
  13. 13.
    Mehrasbi MR, Mohammadi J, Peyda M, Mohammadi M (2017) Covalent immobilization of Candida antarctica lipase on core-shell magnetic nanoparticles for production of biodiesel from waste cooking oil. Renew Energy 101:593–602CrossRefGoogle Scholar
  14. 14.
    Kumar-Krishnan S, Hernandez-Rangel A, Pal U, Ceballos-Sanchez O, Flores-Ruiz FJ, Prokhorov E, Arias de Fuentes O, Esparza R, Meyyappan M (2016) Surface functionalized halloysite nanotubes decorated with silver nanoparticles for enzyme immobilization and biosensing. J Mater Chem B 4:2553–2560CrossRefGoogle Scholar
  15. 15.
    Schlipf DM, Rankin SE, Knutson BL (2017) Selective external surface functionalization of large-pore silica materials capable of protein loading. Microporous Mesoporous Mater 244:199–207CrossRefGoogle Scholar
  16. 16.
    Chang M, Lin Y-H, Gabayno JL, Li Q, Liu X (2017) Thrombolysis based on magnetically-controlled surface-functionalized Fe3O4 nanoparticle. Bioengineered 8:29–35CrossRefGoogle Scholar
  17. 17.
    Al-Qodah Z, Al-Shannag M, Ai-Busoul M, Penchev I, Orfali W (2017) Immobilized enzymes bioreactors utilizing a magnetic field: a review. Biochem Eng J 121:94–106CrossRefGoogle Scholar
  18. 18.
    Santos JCSD., Barbosa O, Ortiz C, Berenguer-Murcia A, Rodrigues RC, Fernandez-Lafuente R (2015) Importance of the support properties for immobilization or purification of enzymes. ChemCatChem 7:2413–2432CrossRefGoogle Scholar
  19. 19.
    Alinezhad H, Tajbakhsh M, Ghobadi N (2015) Ionic liquid immobilized on Fe3O4 nanoparticles: a magnetically recyclable heterogeneous catalyst for one-pot three-component synthesis of 1,8-dioxodecahydroacridines. Res Chem Intermed 41:9979–9992CrossRefGoogle Scholar
  20. 20.
    Zhu Q, Maeno S, Sasaki M, Miyamoto T, Fukushima M (2015) Monopersulfate oxidation of 2,4,6-tribromophenol using an iron(III)-tetrakis(p-sulfonatephenyl)porphyrin catalyst supported on an ionic liquid functionalized Fe3O4 coated with silica. Appl Catal B Environ 163:459–466CrossRefGoogle Scholar
  21. 21.
    Rodrigues RC, Hernandez K, Barbosa O, Rueda N, Garcia-Galan C, Jose CSDS, Berenguer-Murcia A, Fernandez-Lafuente R (2015) Immobilization of proteins in poly-styrene-divinylbenzene matrices: functional properties and applications. Curr Org Chem 19:1–1CrossRefGoogle Scholar
  22. 22.
    Rios NS, Pinheiro MP, Santos JCSD., Fonseca TDS, Lima LD, Demattos MC, Freire DMG, Júnior IJDS., Rodríguez-Aguado E, Gonçalves LRB (2016) Strategies of covalent immobilization of a recombinant Candida antarctica lipase B on pore-expanded SBA-15 and its application in the kinetic resolution of (R,S)-phenylethyl acetate. J Mol Catal B Enzym 133:246–258CrossRefGoogle Scholar
  23. 23.
    Rueda N, Santos CSD, Rodriguez MD, Albuquerque TL, Barbosa O, Torres R, Ortiz C, Fernandez-Lafuente R (2016) Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization. J Mol Catal B Enzym 128:10–18CrossRefGoogle Scholar
  24. 24.
    Santos JCSD., Rueda N, Gonçalves LRB, Fernandez-Lafuente R (2015) Tuning the catalytic properties of lipases immobilized on divinylsulfone activated agarose by altering its nanoenvironment. Enzyme Microb Technol 77:1–7CrossRefGoogle Scholar
  25. 25.
    DiCosimo R, McAuliffe J, Poulose AJ, Bohlmann G (2013) Industrial use of immobilized enzymes. Chem Soc Rev 42:6437–6474CrossRefGoogle Scholar
  26. 26.
    Bonazza HL, Manzo RM, Santos JCSD, Mammarella EJ (2017) Operational and thermal stability analysis of Thermomyces lanuginosus lipase covalently immobilized onto modified chitosan supports. Appl Biochem Biotechnol 47:1–15Google Scholar
  27. 27.
    Costa-Silva TA, Marques PS, Fernandes Souza CR, Said S, Oliveira WP (2015) Enzyme encapsulation in magnetic chitosan–Fe3O4 microparticles. J Microencapsul 32:16–21CrossRefGoogle Scholar
  28. 28.
    Fang G, Chen H, Zhang Y, Chen A (2016) Immobilization of pectinase onto Fe3O4@SiO2–NH2 and its activity and stability. Int J Biol Macromol 88:189–195CrossRefGoogle Scholar
  29. 29.
    Wang J, Zhao G, Yu F (2016) Facile preparation of Fe3O4@MOF core-shell microspheres for lipase immobilization. J Taiwan Inst Chem 69:139–145CrossRefGoogle Scholar
  30. 30.
    Xu R, Yuan J, Si Y, Li F, Zhang B (2016) Estrone removal by horseradish peroxidase immobilized on a nanofibrous support with Fe3O4 nanoparticles. RSC Adv 6:3927–3933CrossRefGoogle Scholar
  31. 31.
    Liu H, Li Z, Takafuji M, Ihara H, Qiu H (2017) Octadecylimidazolium ionic liquid-modified magnetic materials: preparation, adsorption evaluation and their excellent application for honey and cinnamon. Food Chem 229:208–214CrossRefGoogle Scholar
  32. 32.
    Qian L, Sun J, Hou C, Yang J, Li Y, Lei D, Yang M, Zhang S (2017) Immobilization of BSA on ionic liquid functionalized magnetic Fe3O4 nanoparticles for use in surface imprinting strategy. Talanta 168:174–182CrossRefGoogle Scholar
  33. 33.
    Bahraman F, Alemzadeh I (2017) Optimization of l-asparaginase immobilization onto calcium alginate beads. Chem Eng Commun 204:216–220CrossRefGoogle Scholar
  34. 34.
    Bilal M, Iqbal M, Hu H, Zhang X (2016) Mutagenicity and cytotoxicity assessment of biodegraded textile effluent by Ca-alginate encapsulated manganese peroxidase. Biochem Eng J 109:153–161CrossRefGoogle Scholar
  35. 35.
    Zou B, Hu Y, Yu D, Xia J, Tang S, Liu W, Huang H (2010) Immobilization of porcine pancreatic lipase onto ionic liquid modified mesoporous silica SBA-15. Biochem Eng J 53:150–153CrossRefGoogle Scholar
  36. 36.
    Pereira EB, De Castro HF, De Moraes FF, Zanin GM (2001) Kinetic studies of lipase from Candida rugosa—a comparative study between free and immobilized enzyme onto porous chitosan beads. Appl Biochem Biotechnol 91 – 3:739–752CrossRefGoogle Scholar
  37. 37.
    Sarioglu K, Demir N, Acar J, Mutlu M (2001) The use of commercial pectinase in the fruit juice industry, part 2: determination of the kinetic behaviour of immobilized commercial pectinase. J Food Eng 47:271–274CrossRefGoogle Scholar
  38. 38.
    Urban PL, Goodall DM, Bruce NC (2006) Enzymatic microreactors in chemical analysis and kinetic studies. Biotechnol Adv 24:42–57CrossRefGoogle Scholar
  39. 39.
    Fernandez-Lopez L, Pedrero SG, Lopez-Carrobles N, Gorines BC, Virgen-Ortíz JJ, Fernandez-Lafuente R (2017) Effect of protein load on stability of immobilized enzymes. Enzyme Microb Technol 98:18–27CrossRefGoogle Scholar
  40. 40.
    Siviello C, Greco F, Larobina D (2016) Analysis of the aging effects on the viscoelasticity of alginate gels. Soft Matter 12:8726–8734CrossRefGoogle Scholar
  41. 41.
    Lee SY, Khoiroh I, Ling TC, Show PL (2017) Enhanced recovery of lipase derived from Burkholderia cepacia from fermentation broth using recyclable ionic liquid/polymer-based aqueous two-phase systems. Sep Purif Technol 179:152–160CrossRefGoogle Scholar
  42. 42.
    Zhao R, Zhang X, Zheng L, Xu H, Li M (2017) Enantioselective esterification of (R,S)-flurbiprofen catalyzed by lipase in ionic liquid. Green Chem 10:23–28Google Scholar
  43. 43.
    Rios N, Pinheiro M, Santos J, Fonseca T, Lima L, Demattos M (2016) Strategies of covalent immobilization of a recombinant Candida antarctica, lipase b on pore-expanded sba-15 and its application in the kinetic resolution of (r,s)-phenylethyl acetate. J Mol Catal B Enzym 133:246–258CrossRefGoogle Scholar
  44. 44.
    Aaron Salazar-Leyva J, Lizardi-Mendoza J, Carlos Ramirez-Suarez J, Elena Lugo-Sanchez M, Miriam Valenzuela-Soto E, Marina Ezquerra-Brauer J, Javier Castillo-Yanez F, Pacheco-Aguilar R (2017) Catalytic and operational stability of acidic proteases from monterey sardine (Sardinops sagax caerulea) immobilized on a partially deacetylated chitin support. J Food Biochem 41:41–49Google Scholar
  45. 45.
    Palomo JM, Muñoz G, Fernández-Lorente G, Mateo C, Fernández-Lafuente R, Guisán JM (2002) Interfacial adsorption of lipases on very hydrophobic support (octadecyl–Sepabeads): immobilization, hyperactivation and stabilization of the open form of lipases. J Mol Catal B Enzym 19–20:279–286CrossRefGoogle Scholar
  46. 46.
    Lage FA, Bassi JJ, Corradini MC, Todero LM, Luiz JH, Mendes AA (2016) Preparation of a biocatalyst via physical adsorption of lipase from Thermomyces lanuginosus on hydrophobic support to catalyze biolubricant synthesis by esterification reaction in a solvent-free system. Enzyme Microb Technol 84:56–64CrossRefGoogle Scholar
  47. 47.
    Manoel EA, Ribeiro MFP, Santos JCSD., Coelho MAZ, Simas ABC, Fernandez-Lafuente R, Freire DMG (2015) Accurel MP 1000 as a support for the immobilization of lipase from Burkholderia cepacia: application to the kinetic resolution of myo-inositol derivatives. Process Biochem 50:1557–1564CrossRefGoogle Scholar
  48. 48.
    Ranjbakhsh E, Bordbar A, Abbasi M, Khosropour A, Shams E (2012) Enhancement of stability and catalytic activity of immobilized lipase on silica-coated modified magnetite nanoparticles. Chem Eng J 179(4):272–276CrossRefGoogle Scholar
  49. 49.
    Peters GH, Olsen OH, Svendsen A, Wade RC (1996) Theoretical investigation of the dynamics of the active site lid in Rhizomucor miehei lipase. Biophys J 71:119–127CrossRefGoogle Scholar
  50. 50.
    Aghazadeh M, Karimzadeh I, Ganjali MR (2017) Ethylenediaminetetraacetic acid capped superparamagnetic iron oxide (Fe3O4) nanoparticles: a novel preparation method and characterization. J Magn Magn Mater 439:312–319CrossRefGoogle Scholar
  51. 51.
    Souza TCD, Fonseca TDS, Costa JAD, Rocha MVP, Mattos MCD, Fernandez-Lafuente R, Gonçalves LRB, Santos JCSD. (2016) Cashew apple bagasse as a support for the immobilization of lipase B from Candida antarctica: application to the chemoenzymatic production of (R)-indanol. J Mol Catal B Enzym 130:58–69CrossRefGoogle Scholar
  52. 52.
    Shirini F, Mazloumi M, Seddighi M (2016) Acidic ionic liquid immobilized on nanoporous Na+-montmorillonite as an efficient and reusable catalyst for the formylation of amines and alcohols. Res Chem Intermedi 42:1759–1776CrossRefGoogle Scholar
  53. 53.
    Xu Z, Wan H, Miao J, Han M, Yang C, Guan G (2010) Reusable and efficient polystyrene-supported acidic ionic liquid catalyst for esterifications. J Mol Catal A Chem 332:152–157CrossRefGoogle Scholar

Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  • Xia Jiaojiao
    • 1
  • Zou Bin
    • 1
  • Zhu Gangbin
    • 1
  • Wei Ping
    • 1
  • Liu Zhenjiang
    • 1
  1. 1.School of Food and Biological EngineeringJiangsu UniversityZhenjiangChina

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