Artículo

La versión final de este artículo es de uso interno de la institución.
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

A size selective nanorattle was formed by encapsulating soybean peroxidase (SBP) within a ZnS mesoporous hollow sphere. Once encapsulated within the mesoporous hollow sphere, the SBP remained active against molecules smaller than the 3 nm diameter of the mesopores in the shell wall, while molecules larger than the mesopores, which could not pass into the hollow sphere, did not interact with the SBP. Specifically, encapsulated SBP catalyzed the oxidation of Amplex Ultra-Red, a small fluorogen, in the presence of hydrogen peroxide, encapsulated SBP was deactivated by sodium azide, and no reaction was observed between encapsulated SBP and a greater than 3 nm diameter protease. © 2009 American Chemical Society.

Registro:

Documento: Artículo
Título:Mesoporous ZnS nanorattles: Programmed size selected access to encapsulated enzymes
Autor:Gough, D.V.; Wolosiuk, A.; Braun, P.V.
Filiación:Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States
Frederick Seitz Materials Research Laboratory, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States
Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States
Gerencia Quimica, CNEA, CAC Av. Gral Paz 1499, Buenos Aires, B1650KNA, Argentina
DQIAyQF, Pabellon II, Universidad de Buenos Aires, Ciudad Universitaria, Buenos Aires, Argentina
Palabras clave:Encapsulated enzyme; Hollow sphere; Meso-pores; Mesoporous; Shell wall; Size-selective; Sodium azide; Soybean peroxidase; Hydrogen; Hydrogen peroxide; Oxidation; Sodium; Sugar (sucrose); Zinc sulfide; Spheres; amplex red reagent; hydrogen peroxide; immobilized enzyme; nanoparticle; oxazine derivative; peroxidase; sodium azide; sulfide; zinc derivative; zinc sulfide; article; catalysis; chemistry; enzymology; particle size; porosity; soybean; Catalysis; Enzymes, Immobilized; Hydrogen Peroxide; Nanoparticles; Oxazines; Particle Size; Peroxidase; Porosity; Sodium Azide; Soybeans; Sulfides; Zinc Compounds
Año:2009
Volumen:9
Número:5
Página de inicio:1994
Página de fin:1998
DOI: http://dx.doi.org/10.1021/nl900264n
Título revista:Nano Letters
Título revista abreviado:Nano Lett.
ISSN:15306984
CAS:hydrogen peroxide, 7722-84-1; peroxidase, 9003-99-0; sodium azide, 26628-22-8; sulfide, 18496-25-8; zinc sulfide, 12169-28-7, 1314-98-3; Enzymes, Immobilized; Hydrogen Peroxide, 7722-84-1; Oxazines; Peroxidase, 1.11.1.7; Sodium Azide, 26628-22-8; Sulfides; Zinc Compounds; amplex red reagent, 119171-73-2; zinc sulfide, 1314-98-3
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15306984_v9_n5_p1994_Gough

Referencias:

  • Speir, J.A., Munshi, S., Wang, G.J., Baker, T.S., Johnson, J.E., (1995) Structure, 3 (1), pp. 63-78
  • Douglas, T., Strable, E., Willits, D., Aitouchen, A., Libera, M., Young, M., (2002) Adv. Mater, 14 (6), p. 415
  • Douglas, T., Young, M., (1998) Nature (London), 393 (6681), pp. 152-155
  • Donath, E., Sukhorukov, G.B., Caruso, F., Davis, S.A., Mohwald, H., (1998) Angew. Chem., Int. Ed, 37 (16), pp. 2202-2205
  • Lu, Y., McLellan, J., Xia, Y.N., (2004) Lanemuir, 20 (8), pp. 3464-3470
  • Xia, Y.D., Mokaya, R., (2005) J. Mater. Chem, 15 (30), pp. 3126-3131
  • Caruso, F., Caruso, R.A., Mohwald, H., (1998) Science, 282 (5391), pp. 1111-1114
  • Morishita, M., Lowman, A.M., Takayama, K., Nagai, T., Peppas, N.A., (2002) J. Controlled Release, 81 (1-2), pp. 25-32
  • Mauser, T., Dejugnat, C., Sukhorukov, G.B., (2006) J. Phys. Chem. B, 110 (41), pp. 20246-20253
  • Quinn, J.F., Caruso, F., (2004) Lanemuir, 20 (1), pp. 20-22
  • Wang, Y.J., Yu, A.M., Caruso, F., (2005) Angew. Chem., Int. Ed, 44 (19), pp. 2888-2892
  • Mal, N.K., Fujiwara, M., Tanaka, Y., (2003) Nature (London), 421 (6921), pp. 350-353
  • Schuth, F., Schmidt, W., (2002) Adv. Mater, 14 (9), pp. 629-638
  • Hernandez, R., Tseng, H.R., Wong, J.W., Stoddart, J.F., Zink, J.I., (2004) J. Am. Chem. Soc, 126 (11), pp. 3370-3371
  • Kanatzidis, M.G., (2007) Adv. Mater, 19 (9), pp. 1165-1181
  • Kresge, C.T., Leonowicz, M.E., Roth, W.J., Vartuli, J.C., Beck, J.S., (1992) Nature (London), 359 (6397), pp. 710-712
  • Braun, P.V., Osenar, P., Stupp, S.I., (1996) Nature (London), 380 (6572), pp. 325-328
  • Wolosiuk, A., Armagan, O., Braun, P.V., (2005) J. Am. Chem. Soc, 127 (47), pp. 16356-16357
  • Son, D., Wolosiuk, A., Braun, P.V., (2009) Chem. Mater, 21, pp. 628-634
  • Blinkovsky, A.M., Mceldoon, J.P., Arnold, J.M., Dordick, J.S., (1994) Appl. Biochem. Biotechnol, 49 (2), pp. 153-164
  • McEldoon, J.P., Dordick, J.S., (1996) Biotechnol. Prog, 12 (4), pp. 555-558
  • Henriksen, A., Mirza, O., Indiani, C., Teilum, K., Smulevich, G., Welinder, K.G., Gajhede, M., (2001) Protein Sci, 10 (1), pp. 108-115
  • Karajanagi, S.S., Vertegel, A.A., Kane, R.S., Dordick, J.S., (2004) Langmuir, 20 (26), pp. 11594-11599
  • Jain, T.K., Roy, I., De, T.K., Maitra, A., (1998) J. Am. Chem. Soc, 120 (43), pp. 11092-11095
  • Bogush, G.H., Tracy, M.A., Zukoski, C.F., (1988) J. Non-Cryst. Solids, 104 (1), pp. 95-106
  • Vanblaaderen, A., Vrij, A., (1993) J. Colloid Interface Sci, 156 (1), pp. 1-18
  • Kunishima, M., Kawachi, C., Hioki, K., Terao, R., Tani, S., (2001) Tetrahedron, 57 (8), pp. 1551-1558
  • Zhou, M.J., Diwu, Z.J., PanchukVoloshina, N., Haugland, R.P., (1997) Anal. Biochem, 253 (2), pp. 162-168
  • Zhou, M.J., PanchukVoloshina, N., (1997) Anal. Biochem, 253 (2), pp. 169-174
  • Lowe, G., (1970) Philos. Trans. R. Soc. London. Ser. B, 257 (813), pp. 237-248
  • Drenth, J., Jansonius, J.N., Koekoek, R., Sluyterman, L.A.A., Wolthers, B.G., (1970) Philos. Trans. R. Soc. London, Ser. B, 257 (813), pp. 231-236
  • Grzywnowicz, K., Brzyska, M., Lobarzewski, J., Greppin, H., (1992) J. Mol. Catal, 77 (3), pp. 365-376
  • Klein, I.B., Kirsch, J.F., (1969) J. Biol. Chem, 244 (21), pp. 5928-5935
  • Grzywnowicz, K., Brzyska, M., Lobarzewski, J., Greppin, H., (1992) J. Mol. Catal, 77, pp. 365-376

Citas:

---------- APA ----------
Gough, D.V., Wolosiuk, A. & Braun, P.V. (2009) . Mesoporous ZnS nanorattles: Programmed size selected access to encapsulated enzymes. Nano Letters, 9(5), 1994-1998.
http://dx.doi.org/10.1021/nl900264n
---------- CHICAGO ----------
Gough, D.V., Wolosiuk, A., Braun, P.V. "Mesoporous ZnS nanorattles: Programmed size selected access to encapsulated enzymes" . Nano Letters 9, no. 5 (2009) : 1994-1998.
http://dx.doi.org/10.1021/nl900264n
---------- MLA ----------
Gough, D.V., Wolosiuk, A., Braun, P.V. "Mesoporous ZnS nanorattles: Programmed size selected access to encapsulated enzymes" . Nano Letters, vol. 9, no. 5, 2009, pp. 1994-1998.
http://dx.doi.org/10.1021/nl900264n
---------- VANCOUVER ----------
Gough, D.V., Wolosiuk, A., Braun, P.V. Mesoporous ZnS nanorattles: Programmed size selected access to encapsulated enzymes. Nano Lett. 2009;9(5):1994-1998.
http://dx.doi.org/10.1021/nl900264n