Skip to main content
SpringerLink
Log in

Environmentally Friendly Enzyme Immobilization on MOF Materials

  • Protocol
  • First Online:
Immobilization of Enzymes and Cells

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2100))

Abstract

Metal-organic framework (MOF) materials have revolutionized the applications of nanoporous materials. They can be potentially used in separation, storage, and catalysis, among other applications. Since their discovery in 1999 (Li et al. Nature 402:276–279, 1999; Chui Science 283:1148–1150, 1999), more than 20,000 new structures have been synthesized thanks in part to their high compositional versatility. However, only some of them are really stable in water (both in liquid and vapor phase), which limits their employment in other applications. Furthermore, biocatalysis field has been demanding a “universal support” able to encapsulate/immobilize any type of enzyme in a straightforward methodology and, simultaneously, capable of keeping the enzymatic catalytic activity. This requisite set has been a big challenge considering the drastic synthesis conditions required for most of the MOF materials. Thus, a compromise between the development of a well-formed material support and an acceptable enzymatic activity had to be achieved in order to obtain active biocatalysts, ideally prepared in just one step and under sustainable conditions. In this chapter, we describe the protocols about how to synthesize MOF materials in water, under mild conditions and almost instantaneously in the presence of enzymes. The most successful support of these sustainable MOFs was the semicrystalline Fe-BTC MOF material (like the commercial Basolite F300) allowing the development of efficient active biocatalysts (97% with respect to the free enzyme in the case of CALB lipase). Particularly, this enzyme support improves the benefits given by some other MOF-based supports also described in this chapter, like NH2-MIL-53(Al). Furthermore, we present the post-synthesis immobilization approach, which consists firstly in the synthesis or preparation of the respective MOF material (Fe-BTC or NH2-MIL-53(Al)), followed by an enzyme immobilization protocol. As reported in bibliography, MOFs as enzyme supports combine together more active biocatalysts with lower enzyme leaching when compared to other conventional materials. Moreover, MOFs prepared in non-aqueous media (for instance, N,N-dimethylformamide) can also trap enzymes in an otherwise adverse media. These facts bring these biocatalysts closer to industrial employment in even more demanding applications.

Victoria Gascón and Manuel Sánchez-Sánchez conceived and wrote this chapter.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Protocol
USD 49.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 189.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 249.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 329.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Martinek K, Klibanov AM, Goldmacher VS, Berezin IV (1977) The principles of enzyme stabilization I. Increase in thermostability of enzymes covalently bound to a complementary surface of a polymer support in a multipoint fashion. Biochim Biophys Acta 485(1):1–12. https://doi.org/10.1016/0005-2744(77)90188-7

    Article  CAS  PubMed  Google Scholar 

  2. Martinek K, Klibanov AM, Goldmacher VS, Tchernysheva AV, Mozhaev VV, Berezin IV, Glotov BO (1977) The principles of enzyme stabilization. Biochim Biophys Acta 485(1):13–28. https://doi.org/10.1016/0005-2744(77)90189-9

    Article  CAS  PubMed  Google Scholar 

  3. Halling PJ, Dunnill P (1979) Improved non-porous magnetic supports for immobilized enzymes. Biotechnol Bioeng 21(3):393–416. https://doi.org/10.1002/bit.260210304

    Article  CAS  PubMed  Google Scholar 

  4. Nilsson K, Mosbach K (1981) Immobilization of enzymes and affinity ligands to various hydroxyl group carrying supports using highly reactive sulfonyl chlorides. Biochem Biophys Res Commun 102(1):449–457. https://doi.org/10.1016/0006-291x(81)91541-2

    Article  CAS  PubMed  Google Scholar 

  5. Watanabe K, Royer GP (1983) Polyethylenimine/silica gel as an enzyme support. J Mol Catal 22(2):145–152. https://doi.org/10.1016/0304-5102(83)83020-x

    Article  CAS  Google Scholar 

  6. Dennis KE, Clark DS, Bailey JE, Cho YK, Park YH (1984) Immobilization of enzymes in porous supports: effects of support-enzyme solution contacting. Biotechnol Bioeng 26(8):892–900. https://doi.org/10.1002/bit.260260812

    Article  CAS  PubMed  Google Scholar 

  7. Nilsson K, Mosbach K (1987) [3] Tresyl chloride-activated supports for enzyme immobilization. Methods Enzymol 135:65–78. https://doi.org/10.1016/0076-6879(87)35064-5

    Article  CAS  PubMed  Google Scholar 

  8. Kennedy JF, Cabral JM (1987) Immobilization of enzymes on transition metal-activated supports. Methods Enzymol 135:117–130

    Article  CAS  Google Scholar 

  9. Serra E, Mayoral Á, Sakamoto Y, Blanco RM, Díaz I (2008) Immobilization of lipase in ordered mesoporous materials: effect of textural and structural parameters. Microporous Mesoporous Mater 114(1-3):201–213. https://doi.org/10.1016/j.micromeso.2008.01.005

    Article  CAS  Google Scholar 

  10. Urrego S, Serra E, Alfredsson V, Blanco RM, Diaz I (2010) Bottle-around-the-ship: a method to encapsulate enzymes in ordered mesoporous materials. Micropor Mesopor Mat 129(1-2):173–178. https://doi.org/10.1016/j.micromeso.2009.09.013

    Article  CAS  Google Scholar 

  11. Gascón V, Márquez-Álvarez C, Blanco RM (2014) Efficient retention of laccase by non-covalent immobilization on amino-functionalized ordered mesoporous silica. Appl Catal, A 482:116–126. https://doi.org/10.1016/j.apcata.2014.05.035

    Article  CAS  Google Scholar 

  12. Gascon V, Diaz I, Marquez-Alvarez C, Blanco RM (2014) Mesoporous silicas with tunable morphology for the immobilization of laccase. Molecules 19(6):7057–7071. https://doi.org/10.3390/molecules19067057

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  13. Gascón V, Díaz I, Blanco RM, Márquez-Álvarez C (2014) Hybrid periodic mesoporous organosilica designed to improve the properties of immobilized enzymes. RSC Adv 4(65):34356–34368. https://doi.org/10.1039/c4ra05362a

    Article  Google Scholar 

  14. Gascón V, Márquez-Álvarez C, Blanco RM (2018) Successful encapsulation of β-glucosidase during the synthesis of siliceous mesostructured materials. J Chem Technol Biotechnol 93:2625–2634. https://doi.org/10.1002/jctb.5616

    Article  CAS  Google Scholar 

  15. Li H, Eddaoudi M, O’Keeffe M, Yaghi OM (1999) Design and synthesis of an exceptionally stable and highly porous metal-organic framework. Nature 402(6759):276–279

    Article  CAS  Google Scholar 

  16. Kitagawa S, Uemura K (2005) Dynamic porous properties of coordination polymers inspired by hydrogen bonds. Chem Soc Rev 34(2):109–119. https://doi.org/10.1039/b313997m

    Article  CAS  PubMed  Google Scholar 

  17. Ferey G (2008) Hybrid porous solids: past, present, future. Chem Soc Rev 37(1):191–214. https://doi.org/10.1039/b618320b

    Article  CAS  PubMed  Google Scholar 

  18. Batten SR, Champness NR, Chen X-M, Garcia-Martinez J, Kitagawa S, Öhrström L, O’Keeffe M, Paik Suh M, Reedijk J (2013) Terminology of metal–organic frameworks and coordination polymers (IUPAC Recommendations 2013). Pure Appl Chem 85(8):1715–1724. https://doi.org/10.1351/pac-rec-12-11-20

    Article  CAS  Google Scholar 

  19. Dinca M, Long JR (2008) Hydrogen storage in microporous metal-organic frameworks with exposed metal sites. Angew Chem Int Ed 47(36):6766–6779. https://doi.org/10.1002/anie.200801163

    Article  CAS  Google Scholar 

  20. Yepez R, García S, Schachat P, Sánchez-Sánchez M, González-Estefan JH, González-Zamora E, Ibarra IA, Aguilar-Pliego J (2015) Catalytic activity of HKUST-1 in the oxidation of trans-ferulic acid to vanillin. New J Chem 39(7):5112–5115. https://doi.org/10.1039/c5nj00247h

    Article  CAS  Google Scholar 

  21. Murdock CR, Hughes BC, Lu Z, Jenkins DM (2014) Approaches for synthesizing breathing MOFs by exploiting dimensional rigidity. Coord Chem Rev 258-259:119–136. https://doi.org/10.1016/j.ccr.2013.09.006

    Article  CAS  Google Scholar 

  22. Alhamami M, Doan H, Cheng CH (2014) A review on breathing behaviors of metal-organic-frameworks (MOFs) for gas adsorption. Materials 7(4):3198–3250. https://doi.org/10.3390/ma7043198

    Article  PubMed  PubMed Central  Google Scholar 

  23. Loiseau T, Serre C, Huguenard C, Fink G, Taulelle F, Henry M, Bataille T, Ferey G (2004) A rationale for the large breathing of the porous aluminum terephthalate (MIL-53) upon hydration. Chemistry 10(6):1373–1382. https://doi.org/10.1002/chem.200305413

    Article  CAS  PubMed  Google Scholar 

  24. Jiang H-L, Makal TA, Zhou H-C (2013) Interpenetration control in metal–organic frameworks for functional applications. Coord Chem Rev 257(15-16):2232–2249. https://doi.org/10.1016/j.ccr.2013.03.017

    Article  CAS  Google Scholar 

  25. Kesanli B, Cui Y, Smith MR, Bittner EW, Bockrath BC, Lin W (2004) Highly interpenetrated metal-organic frameworks for hydrogen storage. Angew Chem Int Ed 44(1):72–75. https://doi.org/10.1002/anie.200461214

    Article  CAS  Google Scholar 

  26. Kitagawa S, Kitaura R, Noro S (2004) Functional porous coordination polymers. Angew Chem Int Ed 43(18):2334–2375. https://doi.org/10.1002/anie.200300610

    Article  CAS  Google Scholar 

  27. Furukawa H, Cordova KE, O'Keeffe M, Yaghi OM (2013) The chemistry and applications of metal-organic frameworks. Science 341(6149):1230444–1230412. https://doi.org/10.1126/science.1230444

    Article  CAS  PubMed  Google Scholar 

  28. Czaja AU, Trukhan N, Muller U (2009) Industrial applications of metal-organic frameworks. Chem Soc Rev 38(5):1284–1293. https://doi.org/10.1039/b804680h

    Article  CAS  PubMed  Google Scholar 

  29. Kuppler RJ, Timmons DJ, Fang Q-R, Li J-R, Makal TA, Young MD, Yuan D, Zhao D, Zhuang W, Zhou H-C (2009) Potential applications of metal-organic frameworks. Coord Chem Rev 253(23-24):3042–3066. https://doi.org/10.1016/j.ccr.2009.05.019

    Article  CAS  Google Scholar 

  30. Sarkisov L (2012) Toward rational design of metal–organic frameworks for sensing applications: efficient calculation of adsorption characteristics in zero loading regime. J Phys Chem C 116(4):3025–3033. https://doi.org/10.1021/jp210633w

    Article  CAS  Google Scholar 

  31. Orcajo G, Calleja G, Botas JA, Wojtas L, Alkordi MH, Sánchez-Sánchez M (2014) Rationally designed nitrogen-rich metal–organic cube material: an efficient CO2 adsorbent and H2 confiner. Cryst Growth Des 14(2):739–746. https://doi.org/10.1021/cg401613w

    Article  CAS  Google Scholar 

  32. Ran J, Zeng H, Cai J, Jiang P, Yan P, Zheng L, Bai Y, Shen X, Shi B, Tong H (2018) Rational design of a stable, effective, and sustained dexamethasone delivery platform on a titanium implant: an innovative application of metal organic frameworks in bone implants. Chem Eng J 333:20–33. https://doi.org/10.1016/j.cej.2017.09.145

    Article  CAS  Google Scholar 

  33. Lykourinou V, Chen Y, Wang XS, Meng L, Hoang T, Ming LJ, Musselman RL, Ma S (2011) Immobilization of MP-11 into a mesoporous metal-organic framework, MP-11@mesoMOF: a new platform for enzymatic catalysis. J Am Chem Soc 133(27):10382–10385. https://doi.org/10.1021/ja2038003

    Article  CAS  PubMed  Google Scholar 

  34. Ma S, Ming L-J, Chen Y, Lykourinou V (2012) Polyhedral cage-containing mesoporous metal-organic frameworks as platform for biocatalysis, methods of making these frameworks, and methods of using these frameworks. US Patent,

    Google Scholar 

  35. Chen Y, Lykourinou V, Hoang T, Ming LJ, Ma S (2012) Size-selective biocatalysis of myoglobin immobilized into a mesoporous metal-organic framework with hierarchical pore sizes. Inorg Chem 51(17):9156–9158. https://doi.org/10.1021/ic301280n

    Article  CAS  PubMed  Google Scholar 

  36. Chen Y, Lykourinou V, Vetromile C, Hoang T, Ming LJ, Larsen RW, Ma S (2012) How can proteins enter the interior of a MOF? Investigation of cytochrome c translocation into a MOF consisting of mesoporous cages with microporous windows. J Am Chem Soc 134(32):13188–13191. https://doi.org/10.1021/ja305144x

    Article  CAS  PubMed  Google Scholar 

  37. Deng H, Grunder S, Cordova KE, Valente C, Furukawa H, Hmadeh M, Gandara F, Whalley AC, Liu Z, Asahina S, Kazumori H, O’Keeffe M, Terasaki O, Stoddart JF, Yaghi OM (2012) Large-pore apertures in a series of metal-organic frameworks. Science 336(6084):1018–1023. https://doi.org/10.1126/science.1220131

    Article  CAS  PubMed  Google Scholar 

  38. Wang X, Makal TA, Zhou H-C (2014) Protein immobilization in metal–organic frameworks by covalent binding. Aust J Chem 67(11):1629. https://doi.org/10.1071/ch14104

    Article  CAS  Google Scholar 

  39. Wu X, Hou M, Ge J (2015) Metal–organic frameworks and inorganic nanoflowers: a type of emerging inorganic crystal nanocarrier for enzyme immobilization. Cat Sci Technol 5(12):5077–5085. https://doi.org/10.1039/c5cy01181g

    Article  CAS  Google Scholar 

  40. Feng D, Liu TF, Su J, Bosch M, Wei Z, Wan W, Yuan D, Chen YP, Wang X, Wang K, Lian X, Gu ZY, Park J, Zou X, Zhou HC (2015) Stable metal-organic frameworks containing single-molecule traps for enzyme encapsulation. Nat Commun 6:5979. https://doi.org/10.1038/ncomms6979

    Article  CAS  PubMed  Google Scholar 

  41. Shieh FK, Wang SC, Yen CI, Wu CC, Dutta S, Chou LY, Morabito JV, Hu P, Hsu MH, Wu KC, Tsung CK (2015) Imparting functionality to biocatalysts via embedding enzymes into nanoporous materials by a de novo approach: size-selective sheltering of catalase in metal-organic framework microcrystals. J Am Chem Soc 137(13):4276–4279. https://doi.org/10.1021/ja513058h

    Article  CAS  PubMed  Google Scholar 

  42. Liu WL, Yang NS, Chen YT, Lirio S, Wu CY, Lin CH, Huang HY (2015) Lipase-supported metal-organic framework bioreactor catalyzes warfarin synthesis. Chemistry 21(1):115–119. https://doi.org/10.1002/chem.201405252

    Article  CAS  PubMed  Google Scholar 

  43. Lian X, Chen Y-P, Liu T-F, Zhou H-C (2016) Coupling two enzymes into a tandem nanoreactor utilizing a hierarchically structured MOF. Chem Sci 7:6969–6973. https://doi.org/10.1039/c6sc01438k

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  44. Castro Miguel E, Gascon V, Diaz Garcia M, Blanco R, Sanchez-Sanchez M (2015) Procedimiento general de obtencion de biocatalizadores que comprende la inmovilizacion de enzimas durante la sintesis de materiales metalo-organicos. Spain Patent WO2016193516A1,

    Google Scholar 

  45. Gkaniatsou E, Sicard C, Ricoux R, Mahy J-P, Steunou N, Serre C (2017) Metal–organic frameworks: a novel host platform for enzymatic catalysis and detection. Mater Horiz 4(1):55–63. https://doi.org/10.1039/c6mh00312e

    Article  CAS  Google Scholar 

  46. Gascón V, Castro-Miguel E, Díaz-García M, Blanco RM, Sanchez-Sanchez M (2017) In situ and post-synthesis immobilization of enzymes on nanocrystalline MOF platforms to yield active biocatalysts. J Chem Technol Biotechnol 92(10):2583–2593. https://doi.org/10.1002/jctb.5274

    Article  CAS  Google Scholar 

  47. Gascón V, Carucci C, Jiménez MB, Blanco RM, Sánchez-Sánchez M, Magner E (2017) Rapid in situ immobilization of enzymes in metal-organic framework supports under mild conditions. ChemCatChem 9:1182–1186. https://doi.org/10.1002/cctc.201601342

    Article  CAS  Google Scholar 

  48. Gascón V, Jiménez MB, Blanco RM, Sanchez-Sanchez M (2018) Semi-crystalline Fe-BTC MOF material as an efficient support for enzyme immobilization. Catal Today 304:119–126. https://doi.org/10.1016/j.cattod.2017.10.022

    Article  CAS  Google Scholar 

  49. Blay V, Bobadilla LF, García AC (eds) (2018) Zeolites and metal-organic frameworks from lab to industry, vol 1. Amsterdam University Press, Amsterdam. https://doi.org/10.5117/9789462985568

    Book  Google Scholar 

  50. Chen Y, Han S, Li X, Zhang Z, Ma S (2014) Why does enzyme not leach from metal-organic frameworks (MOFs)? Unveiling the interactions between an enzyme molecule and a MOF. Inorg Chem 53(19):10006–10008. https://doi.org/10.1021/ic501062r

    Article  CAS  PubMed  Google Scholar 

  51. Serra E, Alfredsson V, Blanco RM, Diaz I (2008) A comprehensive strategy for the immobilization of lipase in ordered mesoporous materials. Stud Surf Sci Catal 174:369–372. https://doi.org/10.1016/s0167-2991(08)80219-4

    Article  Google Scholar 

  52. Mayoral Á, Gascón V, Blanco RM, Márquez-Álvarez C, Díaz I (2014) Location of laccase in ordered mesoporous materials. APL Materials 2(11):113304. https://doi.org/10.1063/1.4897281

    Article  CAS  Google Scholar 

  53. Sanchez Sánchez M, Díaz I, Getachew N, Chebude Y (2012) Procedimiento de preparación de compuestos metalo-orgánicos

    Google Scholar 

  54. Sánchez-Sánchez M, Getachew N, Díaz K, Díaz-García M, Chebude Y, Díaz I (2015) Synthesis of metal–organic frameworks in water at room temperature: salts as linker sources. Green Chem 17(3):1500–1509. https://doi.org/10.1039/c4gc01861c

    Article  Google Scholar 

  55. Stock N, Biswas S (2012) Synthesis of metal-organic frameworks (MOFs): routes to various MOF topologies, morphologies, and composites. Chem Rev 112(2):933–969. https://doi.org/10.1021/cr200304e

    Article  CAS  PubMed  Google Scholar 

  56. Chui SS (1999) A chemically functionalizable nanoporous material [Cu3(TMA)2(H2O)3]n. Science 283(5405):1148–1150. https://doi.org/10.1126/science.283.5405.1148

    Article  CAS  PubMed  Google Scholar 

  57. Serre C, Millange F, Thouvenot C, Noguès M, Marsolier G, Louër D, Férey G (2002) Very large breathing effect in the first nanoporous chromium(III)-based solids: MIL-53 or CrIII(OH)·{O2C−C6H4−CO2}·{HO2C−C6H4−CO2H}x·H2Oy. J Am Chem Soc 124(45):13519–13526. https://doi.org/10.1021/ja0276974

    Article  CAS  PubMed  Google Scholar 

  58. Surble S, Serre C, Mellot-Draznieks C, Millange F, Ferey G (2006) A new isoreticular class of metal-organic-frameworks with the MIL-88 topology. Chem Commun (Camb) 3:284–286. https://doi.org/10.1039/b512169h

    Article  CAS  Google Scholar 

  59. Sanchez-Sanchez M, de Asua I, Ruano D, Diaz K (2015) Direct synthesis, structural features, and enhanced catalytic activity of the basolite F300-like semiamorphous Fe-BTC framework. Cryst Growth Des 15(9):4498–4506. https://doi.org/10.1021/acs.cgd.5b00755

    Article  CAS  Google Scholar 

  60. Guesh K, Caiuby CAD, Mayoral Á, Díaz-García M, Díaz I, Sanchez-Sanchez M (2017) Sustainable preparation of MIL-100(Fe) and its photocatalytic behavior in the degradation of methyl orange in water. Cryst Growth Des 17(4):1806–1813. https://doi.org/10.1021/acs.cgd.6b01776

    Article  CAS  Google Scholar 

  61. Tranchemontagne DJ, Hunt JR, Yaghi OM (2008) Room temperature synthesis of metal-organic frameworks: MOF-5, MOF-74, MOF-177, MOF-199, and IRMOF-0. Tetrahedron 64(36):8553–8557. https://doi.org/10.1016/j.tet.2008.06.036

    Article  CAS  Google Scholar 

  62. Calleja G, Botas JA, Orcajo MG, Sánchez-Sánchez M (2009) Differences between the isostructural IRMOF-1 and MOCP-L porous adsorbents. J Porous Mat 17(1):91–97. https://doi.org/10.1007/s10934-009-9268-5

    Article  CAS  Google Scholar 

  63. Getachew N, Chebude Y, Diaz I, Sanchez-Sanchez M (2014) Room temperature synthesis of metal organic framework MOF-2. J Porous Mat 21(5):769–773. https://doi.org/10.1007/s10934-014-9823-6

    Article  CAS  Google Scholar 

  64. Díaz-García M, Mayoral Á, Díaz I, Sánchez-Sánchez M (2014) Nanoscaled M-MOF-74 materials prepared at room temperature. Cryst Growth Des 14(5):2479–2487. https://doi.org/10.1021/cg500190h

    Article  CAS  Google Scholar 

  65. Ruano D, Díaz-García M, Alfayate A, Sánchez-Sánchez M (2015) Nanocrystalline M-MOF-74 as heterogeneous catalysts in the oxidation of cyclohexene: correlation of the activity and redox potential. ChemCatChem 7(4):674–681. https://doi.org/10.1002/cctc.201402927

    Article  CAS  Google Scholar 

  66. Flores JG, Sanchez-Gonzalez E, Gutierrez-Alejandre A, Aguilar-Pliego J, Martinez A, Jurado-Vazquez T, Lima E, Gonzalez-Zamora E, Diaz-Garcia M, Sanchez-Sanchez M, Ibarra IA (2018) Greener synthesis of Cu-MOF-74 and its catalytic use for the generation of vanillin. Dalton Trans 47(13):4639–4645. https://doi.org/10.1039/c7dt04701k

    Article  CAS  PubMed  Google Scholar 

  67. Seo Y-K, Yoon JW, Lee JS, Lee UH, Hwang YK, Jun C-H, Horcajada P, Serre C, Chang J-S (2012) Large scale fluorine-free synthesis of hierarchically porous iron(III) trimesate MIL-100(Fe) with a zeolite MTN topology. Microporous Mesoporous Mater 157:137–145. https://doi.org/10.1016/j.micromeso.2012.02.027

    Article  CAS  Google Scholar 

  68. Dhakshinamoorthy A, Alvaro M, Garcia H (2012) Commercial metal-organic frameworks as heterogeneous catalysts. Chem Commun (Camb) 48(92):11275–11288. https://doi.org/10.1039/c2cc34329k

    Article  CAS  Google Scholar 

  69. Dhakshinamoorthy A, Alvaro M, Horcajada P, Gibson E, Vishnuvarthan M, Vimont A, Grenèche J-M, Serre C, Daturi M, Garcia H (2012) Comparison of porous iron trimesates Basolite F300 and MIL-100(Fe) as heterogeneous catalysts for Lewis acid and oxidation reactions: roles of sructural defects and stability. ACS Catal 2(10):2060–2065. https://doi.org/10.1021/cs300345b

    Article  CAS  Google Scholar 

  70. Martínez F, Leo P, Orcajo G, Díaz-García M, Sanchez-Sanchez M, Calleja G (2017) Sustainable Fe-BTC catalyst for efficient removal of mehylene blue by advanced fenton oxidation. Catal Today 313:6–11. https://doi.org/10.1016/j.cattod.2017.10.002

    Article  CAS  Google Scholar 

  71. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72(1-2):248–254. https://doi.org/10.1016/0003-2697(76)90527-3

    Article  CAS  Google Scholar 

Download references

Acknowledgments

Authors greatly appreciate the contribution of Dr. Rosa M Blanco during the initial design and the early stages of drafting this Chapter. Financial support from the Irish Research Council under The Government of Ireland Postdoctoral Fellowship-2015 GOIPD/2015/287, the Spanish State Research Agency (Agencia Española de Investigación, AEI) and the European Regional Development Fund (Fondo Europeo de Desarrollo Regional, FEDER) through the Project MAT2016-77496-R (AEI/FEDER, UE) are gratefully acknowledged. The authors thank Mr. Ramiro Martínez (Novozymes, Spain) for the CALB lipase extract sample, Mrs. Elsa Castro-Miguel and Mrs. Mayra B. Jimenez for their contribution to this research area during their respective Bachelor's Degree Final Project, and Mr. Carlos Isam Bachour Sirerol for his writing comments during the review and editing of this Chapter and his suggestions for a more sophisticated English style.

Author information

Authors and Affiliations

  1. Department of Chemical Sciences, Bernal Institute, University of Limerick, Limerick, Ireland

    Victoria Gascón Pérez

  2. Instituto de Catálisis y Petroleoquímica (ICP), CSIC, Madrid, Spain

    Manuel Sánchez-Sánchez

Authors
  1. Victoria Gascón Pérez
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Manuel Sánchez-Sánchez
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Victoria Gascón Pérez .

Editor information

Editors and Affiliations

  1. CSIC Campus Cantoblanco, Instituto de Catalisis, Madrid, Spain

    Jose M. Guisan

  2. Institute of Biotech and Biochemical Engineering, Graz University of Technology, Graz, Austria

    Juan M. Bolivar

  3. CIC biomaGUNE, Donostia-San Sebastian, Spain

    Fernando López-Gallego

  4. Campus UAM-CSIC, Institute of Catatalysis, Madrid, Spain

    Javier Rocha-Martín

Rights and permissions

Reprints and permissions

Copyright information

© 2020 Springer Science+Business Media, LLC, part of Springer Nature

About this protocol

Check for updates. Verify currency and authenticity via CrossMark

Cite this protocol

Gascón Pérez, V., Sánchez-Sánchez, M. (2020). Environmentally Friendly Enzyme Immobilization on MOF Materials. In: Guisan, J., Bolivar, J., López-Gallego, F., Rocha-Martín, J. (eds) Immobilization of Enzymes and Cells. Methods in Molecular Biology, vol 2100. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0215-7_18

Download citation

  • DOI: https://doi.org/10.1007/978-1-0716-0215-7_18

  • Published:

  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-0214-0

  • Online ISBN: 978-1-0716-0215-7

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics

Search

Navigation