Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin
Thermostability and gelation of the main proteins of whey, α-lactalbumin (α-lac) and β-lactoglobulin (β-lg) recovered by selective complexation with carboxymethylcellulose (CMC) was studied to evaluate its functionality in food systems. Their behavior was compared to the non-complexed proteins. Both...
Guardado en:
| Autor principal: | |
|---|---|
| Otros Autores: | , , , |
| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
2007
|
| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
| Aporte de: | Registro referencial: Solicitar el recurso aquí |
| Sumario: | Thermostability and gelation of the main proteins of whey, α-lactalbumin (α-lac) and β-lactoglobulin (β-lg) recovered by selective complexation with carboxymethylcellulose (CMC) was studied to evaluate its functionality in food systems. Their behavior was compared to the non-complexed proteins. Both complexes showed a maximum stability at pH 4, that is close to the pH of obtention of β-lg/CMC coacervate (pH 4) and α-lac/CMC coacervate (pH 3.2). Protein complexation increased the thermostability of β-lg by approximately 6-8 °C and that of α-lac by approximately 26 °C due to immobilization of protein molecules in a complex, mainly by electrostatic interactions and because of different amounts of bound polysaccharide. The denaturation enthalpy of complexed proteins markedly decreased as compared to free proteins. Storage modulus (G′) and loss modulus (G″) were recorded to reflect the structure development during heating β-lg/CMC and α-lac/CMC complexes at different pH values. β-lg/CMC complex at 20 wt% was a viscoelastic liquid at pH values within 2 and 8 but upon heating turned to a particulate viscoelastic gel. However, α-lac/CMC complex formed before heating opaque, large visible white particulate aggregates that sticked together to give a solid viscoelastic structure that was not further modified by thermal processing. © 2006 Elsevier Ltd. All rights reserved. |
|---|---|
| Bibliografía: | Aguilera, J.M., Xiong, Y.L., Kinsella, J.E., Viscoelastic properties of mixed dairy gels (1993) Food Research International, 26, pp. 11-17 Baeza, R.I., Pilosof, A.M.R., Calorimetric studies of thermal denaturation of β-lactoglobulin in the presence of polysaccharides (2002) Lebensmittel Wissenschaft u-Technologie, 35, pp. 393-399 Bernal, V., Jelen, P., Thermal stability of whey proteins-a calorimetric study (1985) Journal of Dairy Science, 68, pp. 2847-2852 Bollag, D.M., Edelstein, S.J., Gel electrophoresis under denaturing conditions (1991) Protein methods, pp. 95-141. , Bollag D.M., and Edelstein S.J. (Eds), Wiley-Liss, Inc, New York Boye, J.I., Alli, I., Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: A differential scanning calorimetric study (2000) Food Research International, 33, pp. 673-682 Boye, J.I., Kalab, M., Alli, I., Ma, Y.C., Microstructural properties of heat-set whey protein gels: Effect of pH (2000) Lebensmittel Wissenschaft u-Technologie, 33, pp. 165-172 Brew, K., Grobler, J.A., α-lactalbumin (1992) Advanced dairy chemistry. Proteins, pp. 191-229. , Fox P.F. (Ed), ElsevierApplied Science, Essex Bungenberg de Jong, H.G., Crystallisation-coacervation-flocculation (1949) Colloid science, 2, pp. 232-258. , Kruyt H.R. (Ed), Elsevier Publishing Company, Amsterdam Burova, T.V., Varfolomeeva, E.P., Grinberg, V.E.P., Haertle, T., Tolstoguzov, V.B., Effect of polysaccharides on the stability and renaturation of soybean trypsin (Kunitz) inhibitor (2002) Macromolecular Bioscience, 2 (6), pp. 286-292 Calvo, S., Leaver, J., Banks, J.M., Influence of other whey proteins on the heat-induced aggregation of α-lactalbumin (1993) International Dairy Journal, 3, pp. 719-727 de Wit, J.L., Klarenbeek, G., Effects of various heat treatments on structure and solubility of whey proteins (1984) Journal of Dairy Science, 67, pp. 2701-2710 Delben, F., Stefancich, S., Interaction of food proteins with polysaccharides, I. Properties upon mixing (1997) Journal of Food Engineering, 31, pp. 325-346 Gezimati, J., Creamer, L.K., Singh, H., Heat-induced interactions and gelation of mixtures of β-lactoglobulin and α-lactalbumin (1997) Journal of Agriculture Food Chemistry, 45, pp. 1130-1136 Girard, M., Turgeon, S.L., Paquin, P., Emulsifying properties of whey protein-carboxymethylcellulose complexes (2002) Journal of Food Science, 67 (1), pp. 113-119 Hansen, P.M., Hidaldo, J., Gould, I.A., Reclamation of whey protein with carboxymethylcellulose (1971) Journal of Dairy Science, 54, pp. 830-834 Hansen, P.M.T., Black, D.H., Whipping properties of spray-dried complexes from whey protein and carboxymethylcellulose (1972) Journal of Food Science, 37, pp. 452-456 Hattori, M., Aiba, Y., Nagasawa, K., Takashi, K., Functional improvement of alginic acid by conjugating with beta-lactoglobulin (1996) Journal of Food Science, 61 (6), pp. 1171-1176 Hattori, M., Nagasawa, K., Ametani, A., Kaminogawa, S., Functional changes in beta-lactoglobulin by conjugation with carboxymethyl dextran (1994) Journal of Agriculture Food Chemistry, 42, pp. 2120-2125 Hattori, M., Ogino, A., Nakai, H., Functional improvement of β-lactoglobulin by conjugating with alginate lyase-lysate (1997) Journal of Agriculture Food Chemistry, 45, pp. 703-708 Havea, P., Singh, H., Creamer, L.K., Formation of new protein structures in heated mixtures of BSA and α-lactalbumin (2000) Journal of Agriculture Food Chemistry, 48, pp. 1548-1556 Hidalgo, J., Hansen, M.T., Selective precipitation of whey proteins with carboxymethylcellulose (1971) Journal of Dairy Science, 54 (9). , [1270-17-1274] Hoffmann, M.A.M., Van Mil, P.J.J.M., Heat-induced aggregation of β-lactoglobulin: As a function of pH (1999) Journal of Agricultural Food Chemistry, 47, pp. 1898-1905 Hoffmann, M.A.M., Van Mil, P.J.J.M., de Kruif, K., Thermal denaturation and aggregation of β-lactoglobulin studied by differential scanning calorimetry (1995) Food macromolecules and colloids, pp. 171-177. , Dickinson E., and Lorient D. (Eds), The Royal Society of Chemistry, Cambridge Iametti, S., De Gregori, B., Vecchio, G., Bonomi, F., Modifications occur at different structural levels during the heat-denaturation of β-lactoglobulin (1996) European Journal of Biochemistry, 237, pp. 106-112 Ivinova, O., Izumrudov, V.A., Muronetz, V.I., Galaev, I.Y., Mattiasson, B., Influence of compelling polyanions on the thermostability of basic protein (2003) Macromolecular Bioscience, 3 (3-4), pp. 210-215 Kronman, M.J., Cerankow, L., Holmes, L.G., Inter- and intramolecular interactions of α-lactalbumin. 3. Spectral changes at acid pH (1965) Journal of Biochemistry, 4, pp. 518-523 Kuwajima, K., Ikeguchi, M., Sugawara, T., Hiroka, Y., Sugai, S., Kinetics of disulfide bond reduction in α-lactalbumin by dithiotreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond (1990) Biochemistry, 29, pp. 8240-8249 Kuwajima, K., Ogawa, Y., Sugai, S., Role of the interactions between ionizable groups in the folding of bovine α-lactalbumin (1981) Journal of Biochemistry, 89, pp. 759-770 Laemmli, U.K., Cleavage of structural proteins during the assembly of head of bacteriophague T4 (1970) Nature, 227, pp. 680-687 Liu, T., Relkin, P., Launay, B., Thermal denaturation and heat-induced gelation of β-lactoglobulin. Effects of some chemical parameters (1994) Thermochimica Acta, 246, pp. 387-403 Mann, B., Malik, R.C., Studies on some functional characteristics of whey protein-polysaccharide complex (1996) Journal of Food Science and Technology, 33 (3), pp. 202-206 Mc Kenzie, H.A., Sawyer, W.H., Effect of pH on β-lactoglobulin (1967) Nature, 214, pp. 1101-1104 Mulvihill, D.M., Donovan, M., Whey proteins and their thermal denaturation. A review (1987) Irish Journal of Food Science and Technology, 11, pp. 43-75 Nagasawa, K., Ohgata, K., Takahashi, K., Hattori, M., Role of the polysaccharide content and net charge on the emulsifying properties of β-lactoglobulin-carboxymethyldextran conjugates (1996) Journal of Agriculture Food Chemistry, 44, pp. 2538-2543 Nagasawa, K., Takahashi, K., Hattori, M., Improved emulsifying properties of β-lactoglobulin by conjugating with carboxymethyl dextran (1996) Food Hydrocolloids, 10, pp. 63-67 Paulsson, M., Hegg, P.O., Castberg, H.B., Thermal stability of whey proteins studied by differential scanning calorimetry (1985) Thermochimica Acta, 95 (2), pp. 435-440 Relkin, P., Differential scanning calorimetry: A useful tool for studying protein denaturation (1994) Thermochimica Acta, 246, pp. 371-386 Relkin, P., Thermal unfolding of β-lactoglobulin, α-lactalbumin and bovine sero-albumin. A thermodynamic approach (1996) Critical Reviews in Food Science and Nutrition, 36, pp. 565-601 Relkin, P., Launay, B., Eynard, L., Effect of sodium and calcium addition on thermal denaturation of apo α-lactalbumin: A differential scanning calorimetric study (1993) Journal of Dairy Science, 76, pp. 36-47 Rojas, A.S., Goff, H.D., Senaratne, V., Dalgliesh, D.G., Flores, A., Gelation of commercial fractions of β-lactoglobulin and α-lactalbumin (1997) International Dairy Journal, 7, pp. 79-85 Ross, Y., Karel, M., Phase transitions of mixtures of amorphous polysaccharides and sugars (1991) Biotechnology Progress, 7, pp. 49-53 Ruegg, M., Moor, V., Blanc, B., A calorimetric study of thermal denaturation of whey proteins in simulated milk ultrafiltrate (1977) Journal of Dairy Research, 44, pp. 500-520 Schmitt, C., Sanchez, C., Desobry-Banon, S., Hardy, J., Structure and technofunctional properties of protein-polisaccharides complexes: A review (1998) Critical Reviews in Food Science and Nutrition, 38 (8), pp. 689-753 Schokker, E.P., Singh, H., Creamer, L.K., Heat-induced aggregation of β-lactoglobulin a and b with α-lactalbumin (2000) International Dairy Journal, 10, pp. 843-853 Serov, A.V., Antonov, Y., Tolstoguzov, V.B., Isolation of lactic whey proteins in the form of complexes with apple pectin (1985) Nahrung, 1, pp. 19-30 Shukla, T.P., Chemistry and biological function of α-lactalbumin (1973) CRC Press Critical Reviews in Food Technology, 3, pp. 241-312 Stading, M., Hermansson, A.M., Viscoelastic behaviour of β-lactoglobulin gel structure (1990) Food Hydrocolloids, 4, pp. 121-153 Takahashi, K., Lou, X.F., Ishii, Y., Hattori, M., Lysozyme-glucose stearic acid monoester conjugate formed through the Maillard reaction as an antibacterial emulsifier (2000) Journal of Agriculture Food Chemistry, 48, pp. 2044-2049 Tolstoguzov, V.B., Functional properties of protein-polysaccharide mixtures (1998) Functional properties of food macromolecules. 2nd ed., pp. 252-277. , Hill S.E., Ledward D.A., and Mitchell J.R. (Eds), Aspen Publishers Inc., Maryland Tolstoguzov, V.B., Grinberg, V.Y., Gurov, A.N., Some physicochemical approaches to the problem of protein texturization (1985) Journal of Agriculture Food Chemistry, 33, pp. 151-159 Verheul, M., Roefs, S., de Kruif, K., Kinetics of heat induced aggregation of β-lactoglobulin (1998) Journal of Agriculture Food Chemistry, 46, pp. 896-903 Vikelouda, M., Kiosseoglou, V., The use of carboxymethylcellulose to recover potato proteins and control their functional properties (2004) Food Hydrocolloids, 18, pp. 21-27 |
| ISSN: | 0268005X |
| DOI: | 10.1016/j.foodhyd.2006.10.022 |