Artículo

Santagapita, P.R.; Brizuela, L.G.; Mazzobre, M.F.; Ramirez, H.L.; Corti, H.R.; Santana, R.V.; Buera, M.P. "Structure/function relationships of several biopolymers as related to invertase stability in dehydrated systems" (2008) Biomacromolecules. 9(2):741-747
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:

Structure/function relationships of different biopolymers (alginate, dextran, or β-cyclodextrin) were analyzed as single excipients or combined with trehalose in relation to their efficiency as enzyme stabilizers in freeze-dried formulations and compared to trehalose. Particularly, a novel synthesized polymer β-cyclodextrin-branched alginate (β-CD-A) was employed as excipient. During freeze-drying, the polymers or their mixtures did not confer better protection to invertase compared to trehalose. β-CD-A (with or without trehalose), β-cyclodextrin (β-CD), or dextran with trehalose were the best protective agents during thermal treatment, while β-CD and algiate showed a negative effect on invertase activity preservation. The β-CD linked alginate combined the physical stability provided by alginate with the stabilization of hydrophobic regions of the enzyme provided by cyclodextrin. β-CD-A was effective even at conditions at which trehalose lost its protective effect. A relatively simple covalent combination of two biopolymers significantly affected their functionalities and, consequently, their interactions with proteins, modifying enzyme stability patterns. © 2008 American Chemical Society.

Registro:

Documento: Artículo
Título:Structure/function relationships of several biopolymers as related to invertase stability in dehydrated systems
Autor:Santagapita, P.R.; Brizuela, L.G.; Mazzobre, M.F.; Ramirez, H.L.; Corti, H.R.; Santana, R.V.; Buera, M.P.
Filiación:Departamentos de Industrias y de Química Orgánica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, 1428 Buenos Aires, Argentina
Centro de Estudios de Tecnología Enzimática, Facultad de Agronomía, Universidad de Matanzas Camilo Cienfuegos, Autopista a Varadero km 3 1/2, 44740 Matanzas, Cuba
Comisión Nacional de Energía Atómica, Centro Atómico Constituyentes, Av. Constituyentes, San Martín, Buenos Aires, Argentina
Departamento de Quimica Inorganica Analitica y Quimica Fisica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, 1428 Buenos Aires, Argentina
Palabras clave:Alginate; Dextran; Enzymes; Mixtures; Polysaccharides; Dehydrated systems; Invertase stability; Trehalose; Biopolymers; alginic acid; beta cyclodextrin; beta fructofuranosidase; biopolymer; dextran; excipient; polymer; protective agent; trehalose; article; chemical analysis; chemical binding; chemical modification; chemical structure; controlled study; covalent bond; dehydration; enzyme stability; freeze drying; hydrophobicity; priority journal; protein interaction; synthesis; thermostability; beta-Fructofuranosidase; Desiccation; Drug Stability; Enzyme Stability; Freeze Drying; Laminaria; Polymers; Structure-Activity Relationship
Año:2008
Volumen:9
Número:2
Página de inicio:741
Página de fin:747
DOI: http://dx.doi.org/10.1021/bm7012108
Título revista:Biomacromolecules
Título revista abreviado:Biomacromolecules
ISSN:15257797
CODEN:BOMAF
CAS:alginic acid, 28961-37-7, 29894-36-8, 9005-32-7, 9005-38-3; beta cyclodextrin, 7585-39-9; beta fructofuranosidase, 9001-57-4; dextran, 87915-38-6, 9014-78-2; trehalose, 99-20-7; beta-Fructofuranosidase, EC 3.2.1.26; Polymers
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15257797_v9_n2_p741_Santagapita

Referencias:

  • Minagawa, H., Kaneko, H., (2000) Biotechnol. Lett, 22, pp. 1131-1133
  • Mateo, C., Abian, O., Fernandez-Lafuente, R., Guisán, J.M., (2000) Enzyme Microb. Technol, 26, pp. 509-515
  • Lozano, P., Combes, D., Iborra, J.L., (1994) J. Biotechnol, 35, pp. 9-18
  • Fernández, M., Fragoso, A., Cao, R., Baños, M., Villalonga, M.L., Villalonga, R., (2002) Biotechnol. Lett, 24, pp. 1455-1459
  • Ferrández, M., Fragoso, A., Cao, R., Baños, M., Villalonga, R., (2002) Enzyme Microb. Technol, 31, pp. 543-548
  • Gómez, L., Villalonga, R., (2000) Biotechnol. Lett, 22, pp. 1191-1195
  • Villalonga, R., Villalonga, A.L., Gómez, L., (2000) J. Mol. Catal. B; Enzym, 10, pp. 483-490
  • Villalonga, R., Fernández, M., Fragoso, A., Cao, R., Di Pierro, P., Mariniello, L., Porta, R., (2003) Biotechnol. Bioeng, 81, pp. 732-737
  • Longo, M.A., Combes, D., (1999) J. Chem. Technol. Biotechnol, 74, pp. 25-32
  • Fernández, M., Villalonga, M.L., Caballero, J., Fragoso, A., Cao, R., Villalonga, R., (2003) Biotechnol. Bioeng, 83, pp. 743-747
  • Koepsell, H.J., Tsuchiya, H.M., (1952) J. Bacteriol, 63, pp. 293-295
  • Shamala, T.R., Prasad, A.S., (1995) Biochemistry, 30, pp. 237-241
  • Gombotz, W.R., Wee, S.F., (1998) Adv. Drug Delivery Rev, 31, pp. 267-285
  • Gómez-Díaz, D., Navaza, J.M., (2002) Electron. J. Environ. Agric. Food Chem, 1, pp. 165-176
  • Van Tomme, S.R., Hennink, W.E., (2007) Expert. Rev. Med. Devices, 4, pp. 147-164
  • Draget, K.I., Smidsrød, O., Skjåk-Bræk, G., (2005) Polysaccharides and Polyamides in the Food Industry. Properties, Production and Patents, pp. 1-30. , Steinbückel, A, Rhee, S. K, Eds, Wiley-VCH Verlag GmbH & Co KGaA: Weinheim
  • De Giulio, B., Orlando, P., Barba, G., Coppola, R., De Rosa, M., Sada, A., De Prisco, P., Nazzaro, F., (2005) World J. Microbiol. Biotechnol, 21, pp. 739-746
  • Lee, S.L., Hafeman, A.E., Debenedetti, P.G., Pethica, B.A., Moore, D.J., (2006) Ind. Eng. Chem. Res, 45, pp. 5134-5147
  • Carpenter, J., Crowe, J., (1988) Cryobiology, 25, pp. 459-470
  • Cardona, S., Schebor, C., Buera, M.P., Chirife, J., (1997) J. Food Sci, 62, pp. 105-112
  • Mazzobre, M.F., Buera, M.P., Chirife, J., (1997) Lebensm.-Wiss. Technol, 30, pp. 324-329
  • Suzuki, T., Imamura, K., Yamamoto, K., Satoh, T., Okazaki, M., (1997) J. Chem. Eng. Jpn, 30, pp. 609-613
  • Sun, W.Q., Davidson, P., (1998) Biochim. Biophys. Acta, 1425, pp. 235-244
  • Berlin, E., Anderson, B., Pallansch, M.J., (1973) Dairy Sci, 56, pp. 685-689
  • Iglesias, H., Chirife, J., (1978) J. Food Technol, 13, pp. 137-144
  • Karmas, R., Buera, M.P., Karel, M., (1992) J. Agric. Food Chem, 40, pp. 873-879
  • Lodato, P., Segovia de Huergo, M., Buera, M.P., (1999) Appl. Microbiol. Biotechnol, 52, pp. 215-220
  • Szejtli, J., (1998) Chem. Rev, 98, pp. 1743-1754
  • Fernández, M., Villalonga, M.L., Fragoso, A., Cao, R., Villalonga, R., (2004) Enzyme Microb. Technol, 34, pp. 78-82
  • Pluemsab, W., Sakairi, N., Furuike, T., (2005) Polymer, 46, pp. 9778-9783
  • Zhong, N., Byun, H.S., Bittman, R., (1998) Tetrahedron Lett, 38, pp. 2919-2920
  • Schneider, H.J., Xiao, F., (1992) J. Chem. Soc., Perkin. Trans, 2, pp. 387-391
  • Smidsrød, O., (1970) Carbohydr. Res, 13, pp. 359-372
  • Grasdalen, H., Larsen, B., Smidsrød, O., (1979) Carbohydr. Res, 68, pp. 23-31
  • Trimble, R.B., Maley, F., (1977) J. Biol. Chem, 252, pp. 4409-4412
  • Greenspan, L., (1977) J. Res. Natl. Bur. Stand., Sect. A, 81, pp. 89-96
  • Bernfeld, P., (1955) Methods Enzymol, 1, pp. 149-158
  • Schebor, C., Burin, L., Buera, M.P., Chirife, J., (2000) Lebensm.-Wiss. Technol, 32, pp. 481-485
  • Mazzobre, M.F., Longinotti, M.P., Corti, H.R., Buera, M.P., (2001) Cryobiology, 43, pp. 199-210
  • Schülke, N., Schmid, F.X., (1988) J. Biol. Chem, 263, pp. 8832-8837
  • Kizilyar, N., Akbulut, U., Toppare, L., Özden, M.Y., Yaǧci, Y., (1999) Synth. Met, 104, pp. 45-50
  • Mazzobre, M.F., Buera, M.P., (1999) Biochim. Biophys. Acta, 1473, pp. 337-344
  • Santagapita, P. R.; Buera, M. P. In Water Properties of Food, Pharmaceutical and Biological Materials; Buera, M. P., Welti-Chanes, J., Lillford, P. Corti, H., Eds.; CRC-Taylor and Francis: Boca Raton. FL, 2006; pp 663-669; Bilensoy, E., Dogan, L., Şen, M., Hincal, A., (2007) J. Incl. Phenom. Macrocycl. Chem, 57, pp. 651-655
  • Mishima, Y., Momma, K., Hashimoto, W., Mikami, B., Murata, K., (2003) J. Biol. Chem, 278, pp. 6552-6559
  • Chan, C., Lori, L., Burrows, L.L., Deber, C.M., (2004) J. Biol. Chem, 279, pp. 38749-38754
  • Basso, A., Maltman, B.A., Flitsch, S.L., Margetts, G., Brazendale, I., Ebert, C., Linda, P., Gardossi, L., (2005) Tetrahedron, 61, pp. 971-976
  • Darias, R., Herrera, I., Fragoso, A., Cao, R., Villalonga, R., (2002) Biotechnol. Lett, 24, pp. 1665-1668
  • Pikal, M.J., (1999) Freeze-Drying/Lyophilization of Pharmaceutical and Biological Products, pp. 161-198. , Rey, L, May, J. C, Eds; Marcel Dekker Inc, New York
  • Hemminga, M. A.; van der Dries, I. J. In Biological Magnetic Resonance, 14: Spin Labeling: The Next Millennium; Berliner, L. J., Ed.; Plenum Press: New York, 1998; pp 339-366; Franks, F., (1994) Biotechnology, 12, pp. 253-256
  • Mazzobre, M.F., Hough, G., Buera, M.P., (2003) Food Sci. Technol. Int, 9, pp. 163-172

Citas:

---------- APA ----------
Santagapita, P.R., Brizuela, L.G., Mazzobre, M.F., Ramirez, H.L., Corti, H.R., Santana, R.V. & Buera, M.P. (2008) . Structure/function relationships of several biopolymers as related to invertase stability in dehydrated systems. Biomacromolecules, 9(2), 741-747.
http://dx.doi.org/10.1021/bm7012108
---------- CHICAGO ----------
Santagapita, P.R., Brizuela, L.G., Mazzobre, M.F., Ramirez, H.L., Corti, H.R., Santana, R.V., et al. "Structure/function relationships of several biopolymers as related to invertase stability in dehydrated systems" . Biomacromolecules 9, no. 2 (2008) : 741-747.
http://dx.doi.org/10.1021/bm7012108
---------- MLA ----------
Santagapita, P.R., Brizuela, L.G., Mazzobre, M.F., Ramirez, H.L., Corti, H.R., Santana, R.V., et al. "Structure/function relationships of several biopolymers as related to invertase stability in dehydrated systems" . Biomacromolecules, vol. 9, no. 2, 2008, pp. 741-747.
http://dx.doi.org/10.1021/bm7012108
---------- VANCOUVER ----------
Santagapita, P.R., Brizuela, L.G., Mazzobre, M.F., Ramirez, H.L., Corti, H.R., Santana, R.V., et al. Structure/function relationships of several biopolymers as related to invertase stability in dehydrated systems. Biomacromolecules. 2008;9(2):741-747.
http://dx.doi.org/10.1021/bm7012108