Facile one-step catalytic grafting of N-hydroxysuccinimidyl-ester- functionalized methallylsilane onto silica for enzyme immobilization

Chemistry - An Asian Journal

Volumn 6, Issue 2, 2011, Pages 638-645

  Jung, Un Young ^a   Park, Jung Woo ^a   Han, Eun Hee ^a   Kang, Sin Gun ^a   Lee, Sera ^a   Jun, Chul Ho ^a  

^a Yonsei University   (South Korea)

Author keywords

enzymes; immobilization; mesoporous materials; O silylation; organic inorganic hybrids

Indexed keywords

ACID CATALYST; ESTER GROUPS; FUNCTIONALIZED; GRAFTING EFFICIENCY; GRAFTING METHOD; HIGH LOADING RATE; HIGH LOADINGS; IMMOBILIZATION; IMMOBILIZED ENZYME; MESOPOROUS; MESOPOROUS SILICA; MULTI-STEP; ORGANIC-INORGANIC HYBRID; PRECISE MEASUREMENTS; ROOM TEMPERATURE; SILICA SURFACE; SILYLATIONS;

BEARINGS (STRUCTURAL); CATALYSTS; ENZYME IMMOBILIZATION; ENZYMES; ESTERIFICATION; ESTERS; GRAFTING (CHEMICAL); LOADING; SILICA;

MESOPOROUS MATERIALS;

ESTER; GLUCOSE OXIDASE; IMMOBILIZED ENZYME; SILICON DIOXIDE; SUCCINIMIDE DERIVATIVE;

ARTICLE; ASPERGILLUS NIGER; CATALYSIS; CHEMISTRY; ENZYMOLOGY; METABOLISM; POROSITY;

ASPERGILLUS NIGER; CATALYSIS; ENZYMES, IMMOBILIZED; ESTERS; GLUCOSE OXIDASE; POROSITY; SILICON DIOXIDE; SUCCINIMIDES;

EID: 79251477543     PISSN: 18614728     EISSN: 1861471X     Source Type: Journal    
DOI: 10.1002/asia.201000713     Document Type: Article

References (66)

1. U. Hanefeld, L. Gardossi, E. Magner, Chem. Soc. Rev. 2009, 38, 453-468
2. R. A. Sheldon, Adv. Synth. Catal. 2007, 349, 1289-1307
3. U. T. Bornscheuer, Angew. Chem. 2003, 115, 3458-3459
4. Angew. Chem. Int. Ed. 2003, 42, 3336-3337.
5. For a review for immobilization of lipase, see:, V. M. Balcão, A. L. Paiva, F. X. Malcata, Enzyme Microb. Technol. 1996, 18, 392-416.
6. D. Lee, J. Lee, J. Kim, J. Kim, H. B. Na, B. Kim, C. H. Shin, J. H. Kwak, A. Dohnalkova, J. W. Grate, T. Hyeon, H. S. Kim, Adv. Mater. 2005, 17, 2828-2833
7. C. Lei, Y. Shin, J. Liu, E. J. Ackerman, J. Am. Chem. Soc. 2002, 124, 11242-11243
8. For a review:, D. Avnir, S. Braun, O. Lev, M. Ottolenghi, Chem. Mater. 1994, 6, 1605-1614.
9. X. Zhang, R. F. Guan, D. Q. Wu, K. Y. Chan, J. Mol. Catal. B 2005, 33, 43-50
10. Y. Lü, G. Lu, Y. Wang, Y. Guo, Y. Guo, Z. Zhang, Y. Wang, X. Liu, Adv. Funct. Mater. 2007, 17, 2160-2166
11. A. Schlossbauer, D. Schaffert, J. Kecht, E. Wagner, T. Bein, J. Am. Chem. Soc. 2008, 130, 12558-12559
12. S. Libertino, F. Giannazzo, V. Aiello, A. Scandurra, F. Sinatra, M. Renis, M. Fichera, Langmuir 2008, 24, 1965-1972
13. S. Park, J. Pai, E.-H. Han, C.-H. Jun, I. Shin, Bioconjugate Chem. 2010, 21, 1246-1253.
14. S. Hudson, J. Cooney, E. Magner, Angew. Chem. 2008, 120, 8710-8723
15. Angew. Chem. Int. Ed. 2008, 47, 8582-8594
16. H. Takahashi, B. Li, T. Sasaki, C. Miyajaki, T. Kajino, S. Inagaki, Microporous Mesoporous Mater. 2001, 44-45, 755-762. See also Ref. [1a] and [1b].
17. K. B. Yoon, Acc. Chem. Res. 2007, 40, 29-40, and references therein
18. F. Hoffmann, M. Cornelius, J. Morell, M. Fröba, Angew. Chem. 2006, 118, 3290-3328
19. Angew. Chem. Int. Ed. 2006, 45, 3216-3251
20. A. B. Descalzo, R. Martínez-Máñez, F. Sancenõn, K. Hoffmann, K. Rurack, Angew. Chem. 2006, 118, 6068-6093
21. Angew. Chem. Int. Ed. 2006, 45, 5924-5948
22. G. J. A. A. Soler-Illia, P. Innocenzi, Chem. Eur. J. 2006, 12, 4478-4494
23. I. Slowing, B. G. Trewyn, V. S. Y. Lin, J. Am. Chem. Soc. 2006, 128, 14792-14793
24. A. Corma, H. Garcia, Adv. Synth. Catal. 2006, 348, 1391-1412
25. C. M. Crudden, M. Sateesh, R. Lewis, J. Am. Chem. Soc. 2005, 127, 10045-10050
26. E. J. Acosta, C. S. Carr, E. E. Simanek, D. F. Shantz, Adv. Mater. 2004, 16, 985-989
27. Y. Fujimoto, A. Shimojima, K. Kuroda, Chem. Mater. 2003, 15, 4768-4774
28. P. Judeinstein, C. Sanchez, J. Mater. Chem. 1996, 6, 511-525.
29. For special issues on functional hybrid materials, see
30. J. Mater. Chem. 2005, 15, 3541-3988
31. Chem. Mater. 2001, 13, 3059-3809.
32. E. F. Vansant, P. Van Der Voort, K. C. Vranchen, in Studies in Surface Science and Catalysis, Vol. 93, Part II (Eds.:, B. Delmon, T. Yates,), Elsevier, Amsterdam, 1995
33. For applications of trichlorosilanes to SAM, see:, S. Onclin, B. J. Ravoo, D. N. Reinhoudt, Angew. Chem. 2005, 117, 6438-6462
34. Angew. Chem. Int. Ed. 2005, 44, 6282-6304.
35. Y.-R. Yeon, Y. J. Park, J.-S. Lee, J.-W. Park, S.-G. Kang, C.-H. Jun, Angew. Chem. 2008, 120, 115-118
36. Angew. Chem. Int. Ed. 2008, 47, 109-112
37. D. H. Lee, E. A. Jo, J. W. Park, C. H. Jun, Tetrahedron Lett. 2010, 51, 160-163; For the immobilization of organic functional group onto silica using allylsilane, see
38. T. Shimada, K. Aoki, Y. Shinoda, T. Nakamura, N. Tokunaga, S. Inagaki, T. Hayashi, J. Am. Chem. Soc. 2003, 125, 4688-4689
39. K. Aoki, T. Shimada, T. Hayashi, Tetrahedron: Asymmetry 2004, 15, 1771-1777
40. Y. Maegawa, T. Nagano, T. Yabuno, H. Nakagawa, T. Shimada, Tetrahedron 2007, 63, 11467-11474
41. Y. Wang, S. Hu, W. J. Brittain, Macromolecules 2006, 39, 5675-5678.
42. G. T. Hermanson, in Bioconjugate Techniques, Academic Press, London, 1996, pp. 139-140
43. P. Jonkheijm, D. Weinrich, H. Schröder, C. M. Niemeyer, H. Waldmann, Angew. Chem. 2008, 120, 9762-9792
44. Angew. Chem. Int. Ed. 2008, 47, 9618-9647
45. J. H. Yu, S. G. Kang, U. Y. Jung, C. H. Jun, H. Kim, Ann. N. Y. Acad. Sci. 2009, 1171, 359-364
46. H. S. Kim, Y. S. Kye, D. S. Hage, J. Chromatogr. A 2004, 1049, 51-61
47. P. Pandey, S. P. Singh, S. K. Arya, V. Gupta, M. Datta, S. Singh, B. D. Malhotra, Langmuir 2007, 23, 3333-3337.
48. -1; purchased from Sigma) was used. It was reported that the size of glucose oxidase was determined to be 7.0× 5.5× 8.0 nm at most by X-ray crystallography. See:, H. J. Hecht, D. Schomburg, H. Kalisz, R. D. Schmid, Biosens. Bioelectron. 1993, 8, 197-203.
49. H. C. Kolb, M. G. Finn; K. B. Sharpless, Angew. Chem. 2001, 113, 2056-2075
50. K. B. Sharpless, Angew. Chem. 2001, 113, 2056-2075
51. Angew. Chem. Int. Ed. 2001, 40, 2004-2021
52. Q. Wang, T. R. Chan, R. Hilgraf, V. V. Fokin, K. B. Sharpless, M. G. Finn, J. Am. Chem. Soc. 2003, 125, 3192-3193
53. J. E. Moses, A. D. Moorhouse, Chem. Soc. Rev. 2007, 36, 1249-1262
54. See also Ref. [3c].
55. 2,5-Dioxopyrrolidin-1-yl propiolate is so unstable that it readily decomposes to the starting materials. See, G. M. Coppola, R. E. Damon, Synth. Commun. 1993, 23, 2003-2010.
56. -1, pore size: 11.67 nm; which was purchased from Kromasil.
57. The loading rate of the NHS-ester group was determined based on N value of elementary analysis.
58. The corresponding NHS-ester-functionalized alkoxysilane was hard to prepare owing to facile destruction of alkoxysilane during the reaction process.
59. The exact location of immobilized GOx in the silica ball (3) is not clear, but according to references of the detailed dimensions of glucose oxidase and related reference for clear analysis of the structure of this enzyme, the longest axis of the dimeric glucose oxidase is 8.0 nm. In our experiment, the pore size of 2MA-NHS-1step and 2MA-11-NHS-1step were found to be 10.57 nm and 10.04 nm by BET experiments after the reaction of 3 with NHS-ester bound dimethallylsilane 2b and 2d, respectively. From these results, the pore diameter of the NHS-ester functionalized silica ball was thought to be enough for immobilization of the enzyme inside of the pore in silica ball (3). This speculation is supported by other references. For example, Lu et al. reported the covalent-immobilization method of enzyme by using 3- glycidoxypropyltrimethoxysilane (see Ref. [4b]). In this article, Penicillin G Acetylase (size: 7.0 nm× 5.5 nm× 5.5 nm) was immobilized the inside of silica pore (pore diameter: ca. 8 nm). A related reference about the relationship between the pore size of solid supports and the size of Penicillin G Acetylase, see:, Y. Lü, Y. Guo, Y. Wang, X. Liu, Y. Wang, Y. Guo, Z. Zhang, G. Lu, Microporous Mesoporous Mater. 2008, 114, 507-510.
60. A GOx assay kit from Stressgen Biotechnologies was used for enzyme assays according to the manufacturer's instructions, see:, R. G. Thurman, H. G. Ley, R. Scholz, Eur. J. Biochem. 1972, 25, 420-430.
61. Compound 1d was prepared by the reaction of 3- chloropropylethoxydimethylsilane (1e) and sodium azide and purified by distillation. For experimental details, see Experimental Section.
62. Z. Guo, A. Lei, Z. Liang, Q. Xu, Chem. Commun. 2006, 4512-4514.
63. -1, respectively.
64. The Bradford method (Bio-Rad) was used for determination of the amount of immobilized enzyme according to the manufacturer's instructions. From separate experiments of Bradford analyses, the amount of immobilized GOx in 1MA-GO-1step was found to be 1.4 mg, and the amount of immobilized GOx in 2MA-GO-1step was found to be 1.9 mg. These data show the linear correlation between the loading rate of NHS-ester group and the amount of enzyme loaded., M. M. Bradford, Anal. Biochem. 1976, 72, 248-254.
65. For a related reference on the dependence of the binding affinity on the length of linker, see:, S. Park, I. Shin, Angew. Chem. 2002, 114, 3312-3314
66. Angew. Chem. Int. Ed. 2002, 41, 3180-3182.