Facile preparation of Fe3O4@MOF core-shell microspheres for lipase immobilization

Journal of the Taiwan Institute of Chemical Engineers

Volumn 69, Issue , 2016, Pages 139-145

  Wang, Jianzhi ^a,b   Zhao, Guanghui ^b   Yu, Faquan ^a  

^a WUHAN INSTITUTE OF TECHNOLOGY   (China)

^b LANZHOU UNIVERSITY   (China)

Author keywords

Core shell structure; Immobilization; Lipase; Magnetism; MOF

Indexed keywords

CANDIDA; CRYSTALLINE MATERIALS; ENZYMES; JAVA PROGRAMMING LANGUAGE; LIPASES; MAGNETISM; METAL NANOPARTICLES; MICROSPHERES; OLIVE OIL; ORGANOMETALLICS; RADIOACTIVE WASTE VITRIFICATION; SHELLS (STRUCTURES);

COMPOSITE MICROSPHERES; CORE SHELL STRUCTURE; CORE-SHELL MICROSPHERES; HYDROLYSIS OF OLIVE OIL; LARGE SPECIFIC SURFACE AREAS; MAGNETIC CHARACTERISTIC; MAGNETIC COMPOSITE MICROSPHERES; METALORGANIC FRAMEWORKS (MOFS);

ENZYME IMMOBILIZATION;

EID: 85001816364     PISSN: 18761070     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jtice.2016.10.004     Document Type: Article

References (48)

1. [1] Lee, C, Lin, T, Mou, C., Mesoporous materials for encapsulating enzymes. Nano Today 4 (2009), 165–179.
2. [2] Sheldon, RA, van Pelt, S., Enzyme immobilisation in biocatalysis: why, what and how. Chem Soc Rev 42 (2013), 6223–6235.
3. [3] Yiu, HH, Keane, MA., Enzyme–magnetic nanoparticle hybrids: new effective catalysts for the production of high value chemicals. J Chem Technol Biotechnol 87 (2012), 583–594.
4. [4] Marciello, M, Filice, M, Palomo, JM., Different strategies to enhance the activity of lipase catalysts. Catal Sci Technol 2 (2012), 1531–1543.
5. [5] Ansorge-Schumacher, MB, Thum, O., Immobilised lipases in the cosmetics industry. Chem Soc Rev 42 (2013), 6475–6490.
6. [6] Cantone, S, Ferrario, V, Corici, L, Ebert, C, Fattor, D, Spizzo, P, Gardossi, L., Efficient immobilisation of industrial biocatalysts: criteria and constraints for the selection of organic polymeric carriers and immobilisation methods. Chem Soc Rev 42 (2013), 6262–6276.
7. [7] Zhou, Z, Hartmann, M., Progress in enzyme immobilization in ordered mesoporous materials and related applications. Chem Soc Rev 42 (2013), 3894–3912.
8. [8] Zhu, X, Ma, Y, Zhao, C, Lin, Z., Zhang, L, Chen, R, Yang, W., A mild strategy to encapsulate enzyme into hydrogel layer grafted on oolymeric substrate. Langmuir, 30, 2014, 15229.
9. [9] Liese, A, Hilterhaus, L., Evaluation of immobilized enzymes for industrial applications. Chem Soc Rev, 42, 2013, 6236.
10. [10] Esmaeilnejadahranjani, P, Kazemeini, M, Singh, G, Arpanaei, A., Study of molecular conformation and activity-related properties of lipase immobilized onto core-shell structured polyacrylic acid-coated magnetic silica nanocomposite particles. Langmuir 32 (2016), 3242–3252.
11. [11] Netto, CGCM, Andrade, LH, Toma, HE., Association of pseudomonas putida formaldehyde dehydrogenase with superparamagnetic nanoparticles: an effective way of improving the enzyme stability, performance and recycling. New J Chem 39 (2015), 2162–2167.
12. [12] Barbosa, O, Ortiz, C, Berenguermurcia, A, Torres, R, Rodrigues, RC, Fernandezlafuente, R., Strategies for the one-step immobilization-purification of enzymes as industrial biocatalysts. Biotechnol Adv 33 (2015), 435–456.
13. [13] Adlercreutz, P., Immobilisation and application of lipases in organic media. Chem Soc Rev 42 (2013), 6406–6436.
14. [14] Garciagalan, C, Berenguermurcia, A, Fernandezlafuente, R, Rodrigues, RC., Potential of different enzyme immobilization strategies to improve enzyme performance. Adv Synth Catal 353 (2011), 2885–2904.
15. [15] Mateo, C, Palomo, JM, Fernandezlorente, G, Guisan, JM, Fernandezlafuente, R., Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb Technol 40 (2007), 1451–1463.
16. [16] Bastida, A, Sabuquillo, P, Armisen, P, Fernandezlafuente, R, Huguet, J, Guisan, JM., A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports. Biotechnol Bioeng 58 (1998), 486–493.
17. [17] Wright, A, Morrison, SL., Effect of glycosylation on antibody function: implications for genetic engineering. Trends Biotechnol 15 (1997), 26–32.
18. [18] Faraji, M, Yamini, Y, Rezaee, M., Magnetic nanoparticles: synthesis, stabilization, functionalization, characterization, and applications. J Iran Chem Soc 7 (2010), 1–37.
19. [19] Huang, D, Deng, C, Zhang, X., Functionalized magnetic nanomaterials as solid-phase extraction adsorbents for organic pollutants in environmental analysis. Anal Methods-UK 6 (2014), 7130–7141.
20. 4 microspheres in ethylene glycol. Mater Lett 130 (2014), 101–103.
21. [21] Wang, Y, Sun, Y, Wang, Y, Jiang, C, Yu, X, Gao, Y, Zhang, H, Song, D., Determination of Sudan dyes in environmental water by magnetic mesoporous microsphere-based solid phase extraction ultra fast liquid chromatography. Anal Methods-UK 5 (2013), 1399–1406.
22. [22] Feng, G, Jiang, X, Wei, W, Gong, P, Kang, L, Li, Z, Li, Y, Li, X, Wu, X, Lin, Z., High pressure behaviour and elastic properties of a dense inorganic–organic framework. Dalton T 45 (2016), 4303–4308.
23. 4-MCM-41 nanocomposites as a magnetically recyclable biocatalyst for interesterification of soybean oil and lard. Food Chem 194 (2016), 1283–1292.
24. 4/ZnO core/shell magnetic nanoparticles and catalysis of Michael-type addition to chalcone derivatives. J Mol Catal B: Enzym 100 (2014), 121–128.
25. 4 nanocomposite as a high performance, recyclable environmental superadsorbent. J Mater Chem 22 (2012), 19694–19699.
26. 4@MOF core–shell magnetic microspheres with a designable metal–organic framework shell. J Mater Chem 22 (2012), 9497–9500.
27. [27] Wang, J, Zhao, G, Li, Y, Peng, X, Wang, X., Preparation of amine-functionalized mesoporous magnetic colloidal nanocrystal clusters for glucoamylase immobilization. Chem Eng J 263 (2015), 471–478.
28. [28] Ke, F, Yuan, Y-P, Qiu, L-G, Shen, Y-H, Xie, A-J, Zhu, J-F, Tian, X-Y, Zhang, L-D., Facile fabrication of magnetic metal–organic framework nanocomposites for potential targeted drug delivery. J Mater Chem 21 (2011), 3843–3848.
29. 4@ MIL-100 (Fe) for the decolorization of methylene blue dye. J Mater Chem A 1 (2013), 14329–14334.
30. 4/Chitosan nanoparticles as delivery vehicles for pH-responsive drug delivery and magnetic resonance imaging contrast agents. Chem Asian J 9 (2014), 546–553.
31. [31] Bradford, MM., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976), 248–254.
32. [32] Xie, W, Ma, N., Enzymatic transesterification of soybean oil by using immobilized lipase on magnetic nano-particles. Biomass Bioenergy 34 (2010), 890–896.
33. [33] Deng, H, Li, X, Peng, Q, Wang, X, Chen, J, Li, Y., Monodisperse magnetic single-crystal ferrite microspheres. Angew Chem 117 (2005), 2842–2845.
34. [34] Horcajada, P, Surblé, S, Serre, C, Hong, D-Y, Seo, Y-K, Chang, J-S, Greneche, J-M, Margiolaki, I, Férey, G., Synthesis and catalytic properties of MIL-100 (Fe), an iron (III) carboxylate with large pores. Chem Commun 27 (2007), 2820–2822.
35. [35] Canioni, R, Rochmarchal, C, Secheresse, F, Horcajada, P, Serre, C, Hardidan, M, Ferey, G, Greneche, J, Lefebvre, F, Chang, J., Stable polyoxometalate insertion within the mesoporous metal organic framework MIL-100(Fe). J Mater Chem 21 (2011), 1226–1233.
36. 4 nanoparticles inside a zinc imidazolate framework. Dalton T 44 (2015), 10136–10140.
37. [37] Seo, Y-K, Yoon, JW, Lee, JS, Lee, U-H, Hwang, YK, Jun, C-H, Horcajada, P, Serre, C, Chang, J-S., Large scale fluorine-free synthesis of hierarchically porous iron (III) trimesate MIL-100 (Fe) with a zeolite MTN topology. Microporous Mesoporous Mater 157 (2012), 137–145.
38. 4@ ZIF-8 core–shell heterostructure for adsorption of methylene blue. CrystEngComm 16 (2014), 3960–3964.
39. [39] Sing, KS., Reporting physisorption data for gas/solid systems with special reference to the determination of surface area and porosity (Recommendations 1984). Pure Appl Chem 57 (1985), 603–619.
40. [40] Wang, J, Zhao, G, Li, Y, Zhu, H, Peng, X, Gao, X., One-step fabrication of functionalized magnetic adsorbents with large surface area and their adsorption for dye and heavy metal ions. Dalton T 43 (2014), 11637–11645.
41. 4 nanospheres: preparation, characterization and application for lipase immobilization. CrystEngComm 15 (2013), 4937–4947.
42. 4@ MOF core–shell magnetic microspheres as excellent catalysts for the Claisen–Schmidt condensation reaction. Nanoscale 6 (2014), 1596–1601.
43. [43] Dhakshinamoorthy, A, Alvaro, M, Garcia, H., Commercial metal–organic frameworks as heterogeneous catalysts. Chem Commun 48 (2012), 11275–11288.
44. [44] Wang, J, Zhao, G, Li, Y, Liu, X, Hou, P., Reversible immobilization of glucoamylase onto magnetic chitosan nanocarriers. Appl Microbiol Biotechnol 97 (2013), 681–692.
45. [45] Zhao, G, Wang, J, Li, Y, Huang, H, Chen, X., Reversible immobilization of glucoamylase onto metal–ligand functionalized magnetic FeSBA-15. Biochem Eng J 68 (2012), 159–166.
46. [46] Yakup Arıca, M., Immobilization of polyphenol oxidase on carboxymethylcellulose hydrogel beads: preparation and characterization. Polym Int 49 (2000), 775–781.
47. [47] Pessela, BC, Mateo, C, Carrascosa, AV, Fernandez-Lafuente, R, Guisán, JM., Reversible immobilization of a hexameric α-galactosidase from Thermus sp. strain T2 on polymeric ionic exchangers. Process Biochem 43 (2008), 1142–1146.
48. [48] Yong, Y, Bai, Y-X, Li, Y-F, Lin, L, Cui, Y-J, Xia, C-G., Characterization of candida rugosa lipase immobilized onto magnetic microspheres with hydrophilicity. Process Biochem 43 (2008), 1179–1185.