Abstract:
The thermal denaturation of β-lactoglobulin at pH 6 and 7 in the presence of polysaccharides was studied by differential scanning calorimetry. At neutral pH, the shape of differential scanning calorimetry curves was affected by polysaccharides and an increase of 2-3°C in the onset temperature of β-lactoglobulin denaturation was observed. This tendency was magnified up to 10°C at low water contents. At pH 7, the apparent enthalpy changes and the activation energy (Ea) were larger for β-lactoglobulin + polysaccharides mixtures than for pure β-lactoglobulin. At pH 6 the transition temperatures, denaturation enthalpy and activation energy of pure β-lactoglobulin were highly increased and slight changes were observed with further addition of polysaccharides. The rate constants of conversion of native β-lactoglobulin at pH 7 indicate a lower conversion of β-lactoglobulin when heated in the presence of polysaccharides, in agreement with electrophoretic results. Nevertheless, the formation of larger protein aggregates is promoted. A general analysis of the calorimetric and kinetic data indicates that polysaccharides enhance the thermal stability of β-lactoglobulin at neutral pH due to a limited thermodynamic incompatibility between the biopolymers. At pH 6 this effect is minimised because of the prevailing stabilizing effect of pH and a decreased incompatibility between β-lactoglobulin and polysaccharides.
Registro:
Documento: |
Artículo
|
Título: | Calorimetric studies of thermal denaturation of β-lactoglobulin in the presence of polysaccharides |
Autor: | Baeza, R.I.; Pilosof, A.M.R. |
Filiación: | Universidad de Buenos Aires, Departamento de Industrias, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, Buenos Aires (1428), Argentina
|
Palabras clave: | Denaturation; Polysaccharide; Thermostability; β-lactoglobulin |
Año: | 2002
|
Volumen: | 35
|
Número: | 5
|
Página de inicio: | 393
|
Página de fin: | 399
|
DOI: |
http://dx.doi.org/10.1006/fstl.2001.0862 |
Título revista: | LWT - Food Science and Technology
|
Título revista abreviado: | LWT - Food Sci. Technol.
|
ISSN: | 00236438
|
CODEN: | LBWTA
|
Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00236438_v35_n5_p393_Baeza |
Referencias:
- Baeza, R., Pilosof, A.M., Mixed biopolymer gel systems of β-lactoglobulin and non-gelling gums (2001) Food Colloids - Fundamentals of Formulation, pp. 392-403. , Dickinson, E. and Miller, R. (Eds). Cambridge, UK: The Royal Society of Chemistry
- Borchardt, H.J., Daniels, S.F., Application of differential thermal analysis to study of reaction kinetic (1957) Journal of the American Chemical Society, 79, pp. 41-46
- Cairoli, S., Iametti, S., Bonomi, F., Reversible and irreversible modifications of β-lactoglobulin upon exposure to heat (1994) Journal of Protein Chemistry, 13, pp. 347-354
- Capron, I., Nicolai, T., Durand, D., Heat induced aggregation of β-lactoglobulin in the presence of j-carrageenan (1999) Food Hydrocolloids, 13, pp. 1-5
- De Wit, J.N., Swinkels, G.A.M., A differential scanning calorimetric study of the thermal denaturation of bovine β-lactoblobulin. Thermal behavior at temperatures up to 100°C (1980) Biochimica et Biophysica Acta, 624, pp. 40-50
- Donovan, M., Mulvihill, D.M., Thermal denaturation and aggregation of whey proteins (1987) Irish Journal of Food Science and Technology, 11, pp. 87-100
- Grinberg, V.Ya., Tolstoguzov, V.B., Thermodynamic incompatibility of proteins and polysaccharides in solutions (1997) Food Hydrocolloids, 11, pp. 145-158
- Hoffmann, A.M., Van Mil, P.J., Heat-induced aggregation of β-lactoglobulin as a function of pH (1999) Journal of Agricultural and Food Chemistry, 47, pp. 1898-1905
- Hoffmann, M.A., Van Mil, P., De Kruif, C.G., 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). Cambridge, UK: The Royal Society of Chemistry
- 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
- Koppel, D., Analysis of macromolecular polydispersity in intensity correlation spectroscopy: The method of cumulants (1972) Journal of Chemistry and Physics, 57, pp. 4814-4819
- Laemmli, U.K., Cleavage of structural proteins during the assembly of head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
- Liu, T.X., Relkin, P., Launay, B., Thermal denaturation and heat induced gelation properties of β-lactoglobulin. Effects of some chemical parameters (1994) Thermochimica Acta, 246, pp. 387-403
- McKenzie, H.A., Sawyer, W.H., Effect of pH on β-lactoglobulin (1967) Nature, 214, pp. 1101-1104
- McKenzie, H.A., β-lactoglobulins (1971) Milk Proteins: Chemistry and Molecular Biology, pp. 257-330. , McKenzie, H. A. (Ed.). New York: Academic Press
- 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
- Pavlovskaya, G.E., Semenova, M.G., Thzapkina, E.N., Tolstoguzov, V.B., The influence of dextran on the interfacial pressure of absorbing layers of 11S globulin vicia faba at the planar n-decane/aqueous solution interface (1993) Food Hydrocolloids, 7, pp. 1-10
- Qi, X.L., Brownlow, S., Holt, C., Sellers, P., Thermal denaturation of β-lactoglobulin: Effect of protein concentration at pH 6.75 and 8.05 (1995) Biochimica et Biophysica Acta, 1248, pp. 43-49
- Qi, X.L., Holt, C., McNulty, D., Clarke, D.T., Brownlows, S., Jones, G.R., Effect of temperature on the secondary structure of b-lactoglobulin at pH 6.7, as determined by CD and ID spectroscopy: A test of the molten globule hypothesis (1997) Biochemistry Journal, 324, pp. 341-346
- 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 serum albumin. A thermodynamic approach (1996) Critical Reviews in Food Science and Nutrition, 36, pp. 565-601
- Relkin, P., Meylheuc, T., Launay, B., Raynal, K., Heat-and cold-setting gels of β-lactoglobulin solutions. A DSC and TEM study (1998) Thermochimica Acta, 308, pp. 69-74
- Sanchez, V.E., Bartholomai, G.B., Pilosof, A.M., Rheological properties of food gums as related to their water binding capacity and to soy protein interaction (1995) Lebensmittel-Wissenschaft und-Technologie, 28, pp. 380-385
- Tolstoguzov, V.B., Protein-polysaccharide interactions (1997) Food Proteins and their Applications, pp. 171-198. , Damodaran, S. and Paraf, A. (Eds). New York: Marcel Dekker Inc
- Van Mil, P.J., Roefs, S., Denaturation of whey proteins studied by thermal analysis and chromatography (1993) Food Colloids and Polymers: Stability and Mechanical Properties, pp. 45-54. , Dickinson, E. and Walstra, P. (Eds). Cambridge, UK: The Royal Society of Chemistry
- Verheul, M., Roefs, S., De Kruif, K., Kinetics of heat-induced aggregation of β-lactoglobulin (1998) Journal of Agricultural and Food Chemistry, 46, pp. 896-903
Citas:
---------- APA ----------
Baeza, R.I. & Pilosof, A.M.R.
(2002)
. Calorimetric studies of thermal denaturation of β-lactoglobulin in the presence of polysaccharides. LWT - Food Science and Technology, 35(5), 393-399.
http://dx.doi.org/10.1006/fstl.2001.0862---------- CHICAGO ----------
Baeza, R.I., Pilosof, A.M.R.
"Calorimetric studies of thermal denaturation of β-lactoglobulin in the presence of polysaccharides"
. LWT - Food Science and Technology 35, no. 5
(2002) : 393-399.
http://dx.doi.org/10.1006/fstl.2001.0862---------- MLA ----------
Baeza, R.I., Pilosof, A.M.R.
"Calorimetric studies of thermal denaturation of β-lactoglobulin in the presence of polysaccharides"
. LWT - Food Science and Technology, vol. 35, no. 5, 2002, pp. 393-399.
http://dx.doi.org/10.1006/fstl.2001.0862---------- VANCOUVER ----------
Baeza, R.I., Pilosof, A.M.R. Calorimetric studies of thermal denaturation of β-lactoglobulin in the presence of polysaccharides. LWT - Food Sci. Technol. 2002;35(5):393-399.
http://dx.doi.org/10.1006/fstl.2001.0862