Calorimetric studies of thermal denaturation of β-lactoglobulin in the presence of polysaccharides

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-l...

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Autor principal: Baeza, R.I
Otros Autores: Pilosof, A.M.R
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Academic Press 2002
Acceso en línea:Registro en Scopus
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100 1 |a Baeza, R.I. 
245 1 0 |a Calorimetric studies of thermal denaturation of β-lactoglobulin in the presence of polysaccharides 
260 |b Academic Press  |c 2002 
270 1 0 |m Pilosof, A.M.R.; Universidad de Buenos Aires, Departamento de Industrias, Ciudad Universitaria, Buenos Aires (1428), Argentina; email: apilosof@di.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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504 |a Koppel, D., Analysis of macromolecular polydispersity in intensity correlation spectroscopy: The method of cumulants (1972) Journal of Chemistry and Physics, 57, pp. 4814-4819 
504 |a Laemmli, U.K., Cleavage of structural proteins during the assembly of head of bacteriophage T4 (1970) Nature, 227, pp. 680-685 
504 |a 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 
504 |a McKenzie, H.A., Sawyer, W.H., Effect of pH on β-lactoglobulin (1967) Nature, 214, pp. 1101-1104 
504 |a McKenzie, H.A., β-lactoglobulins (1971) Milk Proteins: Chemistry and Molecular Biology, pp. 257-330. , McKenzie, H. A. (Ed.). New York: Academic Press 
504 |a 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 
504 |a 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 
504 |a 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 
504 |a 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 
504 |a Relkin, P., Differential scanning calorimetry: A useful tool for studying protein denaturation (1994) Thermochimica Acta, 246, pp. 371-386 
504 |a 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 
504 |a 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 
504 |a 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 
504 |a 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 
504 |a 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 
504 |a 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 
520 3 |a 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.  |l eng 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: The authors acknowledge the financial support from Universidad de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas y Agencia Nacio- 
593 |a Universidad de Buenos Aires, Departamento de Industrias, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, Buenos Aires (1428), Argentina 
690 1 0 |a DENATURATION 
690 1 0 |a POLYSACCHARIDE 
690 1 0 |a THERMOSTABILITY 
690 1 0 |a Β-LACTOGLOBULIN 
700 1 |a Pilosof, A.M.R. 
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