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Volumn 10, Issue 4, 2000, Pages 233-240

Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration

Author keywords

Lactoglobulin; Heat induced aggregation; Low pH

Indexed keywords

ANALYTICAL PROCEDURES AND TECHNIQUES; BETA LACTOGLOBULIN; GEL PERMEATION CHROMATOGRAPHY; IONIC STRENGTH; PARTICLE SIZE; PH; REACTION MECHANISM; TEMPERATURE;

EID: 0033846408     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-6946(00)00047-9     Document Type: Article
Times cited : (100)

References (44)
  • 3
    • 0001417865 scopus 로고    scopus 로고
    • Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2
    • Aymard P., Nicolai T., Durand D. Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2. Macromolecules. 32:1999;2542-2552.
    • (1999) Macromolecules , vol.32 , pp. 2542-2552
    • Aymard, P.1    Nicolai, T.2    Durand, D.3
  • 4
    • 0001779640 scopus 로고
    • Hydrogen ion equilibria of the genetic variants of bovine β-lactoglobulin
    • Basch J.J., Timasheff S.N. Hydrogen ion equilibria of the genetic variants of bovine β-lactoglobulin. Archives of Biochemistry and Biophysics. 118:1967;37-47.
    • (1967) Archives of Biochemistry and Biophysics , vol.118 , pp. 37-47
    • Basch, J.J.1    Timasheff, S.N.2
  • 5
    • 0032001691 scopus 로고    scopus 로고
    • Detection of intermediate oligomers, important for the formation of heat aggregates of β-lactoglobulin
    • Bauer R., Hansen S., Øgendal L. Detection of intermediate oligomers, important for the formation of heat aggregates of β-lactoglobulin. International Dairy Journal. 8:1998;105-112.
    • (1998) International Dairy Journal , vol.8 , pp. 105-112
    • Bauer, R.1    Hansen, S.2    Øgendal, L.3
  • 6
    • 0000516475 scopus 로고
    • Light scattering techniques
    • S.B. Ross-Murphy. London: Blackie Academic and Professional
    • Burchard W. Light scattering techniques. Ross-Murphy S.B. Physical techniques for the study of food biopolymers. 1994;151-213 Blackie Academic and Professional, London.
    • (1994) Physical Techniques for the Study of Food Biopolymers , pp. 151-213
    • Burchard, W.1
  • 7
    • 0028290324 scopus 로고
    • Reversible and irreversible modifications of β-lactoglobulin upon exposure to heat
    • Cairoli S., Iametti S., Bonomi F. Reversible and irreversible modifications of β-lactoglobulin upon exposure to heat. Journal of Protein Chemistry. 13:1994;347-354.
    • (1994) Journal of Protein Chemistry , vol.13 , pp. 347-354
    • Cairoli, S.1    Iametti, S.2    Bonomi, F.3
  • 8
    • 0030118518 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin studied by dynamic light scattering
    • Elofsson U.M., Dejmek P., Paulsson M.A. Heat-induced aggregation of β-lactoglobulin studied by dynamic light scattering. International Dairy Journal. 6:1996;343-357.
    • (1996) International Dairy Journal , vol.6 , pp. 343-357
    • Elofsson, U.M.1    Dejmek, P.2    Paulsson, M.A.3
  • 9
    • 85024659041 scopus 로고
    • Factors that determine the fracture properties and microstructure of globular protein gels
    • Foegeding E.A., Bowland E.L., Hardin C.C. Factors that determine the fracture properties and microstructure of globular protein gels. Food Hydrocolloids. 9:1995;237-249.
    • (1995) Food Hydrocolloids , vol.9 , pp. 237-249
    • Foegeding, E.A.1    Bowland, E.L.2    Hardin, C.C.3
  • 10
    • 0028195932 scopus 로고
    • Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins
    • Gimel J.-C., Durand D., Nicolai T. Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins. Macromolecules. 27:1994;583-589.
    • (1994) Macromolecules , vol.27 , pp. 583-589
    • Gimel, J.-C.1    Durand, D.2    Nicolai, T.3
  • 13
    • 0019039524 scopus 로고
    • Measurement of thermal denaturation of β-lactoglobulin at pH 2.5
    • Harwalkar V.R. Measurement of thermal denaturation of β-lactoglobulin at pH 2.5. Journal of Dairy Science. 63:1980;1043-1051.
    • (1980) Journal of Dairy Science , vol.63 , pp. 1043-1051
    • Harwalkar, V.R.1
  • 14
    • 0019039146 scopus 로고
    • Kinetics of thermal denaturation of β-lactoglobulin at pH 2.5
    • Harwalkar V.R. Kinetics of thermal denaturation of β-lactoglobulin at pH 2.5. Journal of Dairy Science. 63:1980;1052-1057.
    • (1980) Journal of Dairy Science , vol.63 , pp. 1052-1057
    • Harwalkar, V.R.1
  • 15
    • 0002666893 scopus 로고
    • Thermal denaturation and aggregation of β-lactoglobulin at pH 2.5. Effect of ionic strength and protein concentration
    • Harwalkar V.R., Kalab M. Thermal denaturation and aggregation of β-lactoglobulin at pH 2.5. Effect of ionic strength and protein concentration. Milchwissenschaft. 40:1985;31-34.
    • (1985) Milchwissenschaft , vol.40 , pp. 31-34
    • Harwalkar, V.R.1    Kalab, M.2
  • 16
    • 0002677279 scopus 로고
    • Thermal stability of β-lactoglobulin as a function of pH and the relative concentration of sodium dodecyl sulphate
    • Hegg P.-O. Thermal stability of β-lactoglobulin as a function of pH and the relative concentration of sodium dodecyl sulphate. Acta Agriculturae Scandinavica. 30:1980;401-404.
    • (1980) Acta Agriculturae Scandinavica , vol.30 , pp. 401-404
    • Hegg, P.-O.1
  • 17
    • 0000008542 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin: Role of the free thiol group and disulfide bonds
    • Hoffmann M.A.M., van Mil P.J.J.M. Heat-induced aggregation of β-lactoglobulin. role of the free thiol group and disulfide bonds Journal of Agricultural and Food Chemistry. 45:1997;2942-2948.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 2942-2948
    • Hoffmann, M.A.M.1    Van Mil, P.J.J.M.2
  • 21
    • 0002284922 scopus 로고
    • Modifications of high-order structures upon heating of β-lactoglobulin: Dependence on the protein concentration
    • Iametti S., Cairoli S., De Gregori B., Bonomi F. Modifications of high-order structures upon heating of β-lactoglobulin. dependence on the protein concentration Journal of Agricultural and Food Chemistry. 43:1995;53-58.
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 53-58
    • Iametti, S.1    Cairoli, S.2    De Gregori, B.3    Bonomi, F.4
  • 22
    • 0023765564 scopus 로고
    • Enhanced thermodynamic stability of β-lactoglobulin at low pH. A possible mechanism
    • Kella N.K.D., Kinsella J.E. Enhanced thermodynamic stability of β-lactoglobulin at low pH. A possible mechanism. Biochemical Journal. 255:1988;113-118.
    • (1988) Biochemical Journal , vol.255 , pp. 113-118
    • Kella, N.K.D.1    Kinsella, J.E.2
  • 23
    • 85025567869 scopus 로고
    • Fine-stranded and particulate gels of β-lactoglobulin and whey protein at varying pH
    • Langton M., Hermansson A.-M. Fine-stranded and particulate gels of β-lactoglobulin and whey protein at varying pH. Food Hydrocolloids. 5:1992;523-539.
    • (1992) Food Hydrocolloids , vol.5 , pp. 523-539
    • Langton, M.1    Hermansson, A.-M.2
  • 25
    • 84987300635 scopus 로고
    • Preparation of β-lactoglobulin and β-lactoglobulin-free proteins from whey retentate by NaCl salting out at low pH
    • 752.
    • Mailliart, P., & Ribadeau-Dumas, B. (1988). Preparation of β-lactoglobulin and β-lactoglobulin-free proteins from whey retentate by NaCl salting out at low pH. Journal of Food Science, 53, 743-745, 752.
    • (1988) Journal of Food Science , vol.53 , pp. 743-745
    • Mailliart, P.1    Ribadeau-Dumas, B.2
  • 26
    • 0001205312 scopus 로고    scopus 로고
    • Effect of heat treatment on the conformation and aggregation of β-lactoglobulin A, B, and C
    • Manderson G.A., Hardman M.J., Creamer L.K. Effect of heat treatment on the conformation and aggregation of β-lactoglobulin A, B, and C. Journal of Agricultural and Food Chemistry. 46:1998;5052-5061.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 5052-5061
    • Manderson, G.A.1    Hardman, M.J.2    Creamer, L.K.3
  • 28
    • 85025345712 scopus 로고
    • Thermal aggregation and gelation of bovine β-lactoglobulin
    • McSwiney M., Singh H., Campanella O.H. Thermal aggregation and gelation of bovine β-lactoglobulin. Food Hydrocolloids. 8:1994;441-453.
    • (1994) Food Hydrocolloids , vol.8 , pp. 441-453
    • McSwiney, M.1    Singh, H.2    Campanella, O.H.3
  • 29
    • 0002915720 scopus 로고
    • Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins
    • Monahan F.J., German J.B., Kinsella J.E. Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins. Journal of Agricultural and Food Chemistry. 43:1995;46-52.
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 46-52
    • Monahan, F.J.1    German, J.B.2    Kinsella, J.E.3
  • 31
    • 0001253172 scopus 로고
    • Thermal stability of whey proteins studied by differential scanning calorimetry
    • Paulsson M., Hegg P.O., Castberg H.B. Thermal stability of whey proteins studied by differential scanning calorimetry. Thermochimica Acta. 95:1985;435-440.
    • (1985) Thermochimica Acta , vol.95 , pp. 435-440
    • Paulsson, M.1    Hegg, P.O.2    Castberg, H.B.3
  • 32
    • 0002814094 scopus 로고
    • Rheological properties of heat-induced β-lactoglobulin gels
    • Paulsson M., Dejmek P., van Vliet T. Rheological properties of heat-induced β-lactoglobulin gels. Journal of Dairy Science. 73:1990;45-53.
    • (1990) Journal of Dairy Science , vol.73 , pp. 45-53
    • Paulsson, M.1    Dejmek, P.2    Van Vliet, T.3
  • 34
    • 0028567981 scopus 로고
    • A model for the denaturation and aggregation of β-lactoglobulin
    • Roefs S.P.F.M., de Kruif K.G. A model for the denaturation and aggregation of β-lactoglobulin. European Journal of Biochemistry. 226:1994;883-889.
    • (1994) European Journal of Biochemistry , vol.226 , pp. 883-889
    • Roefs, S.P.F.M.1    De Kruif, K.G.2
  • 35
    • 0033501546 scopus 로고    scopus 로고
    • Characterisation of intermediates formed during heat-induced aggregation of β-lactoglobulin at neutral pH
    • Schokker E.P., Singh H., Pinder D.N., Norris G.E., Creamer L.K. Characterisation of intermediates formed during heat-induced aggregation of β-lactoglobulin at neutral pH. International Dairy Journal. 10:1999;791-800.
    • (1999) International Dairy Journal , vol.10 , pp. 791-800
    • Schokker, E.P.1    Singh, H.2    Pinder, D.N.3    Norris, G.E.4    Creamer, L.K.5
  • 36
    • 0000326329 scopus 로고
    • Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate
    • Shimada K., Cheftel J.C. Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate. Journal of Agricultural and Food Chemistry. 37:1989;161-168.
    • (1989) Journal of Agricultural and Food Chemistry , vol.37 , pp. 161-168
    • Shimada, K.1    Cheftel, J.C.2
  • 37
    • 85025575777 scopus 로고
    • Viscoelastic behaviour of β-lactoglobulin gel structures
    • Stading M., Hermansson A.-M. Viscoelastic behaviour of β-lactoglobulin gel structures. Food Hydrocolloids. 4:1990;121-135.
    • (1990) Food Hydrocolloids , vol.4 , pp. 121-135
    • Stading, M.1    Hermansson, A.-M.2
  • 38
    • 85025567202 scopus 로고
    • Large deformation properties of β-lactoglobulin gel structures
    • Stading M., Hermansson A.-M. Large deformation properties of β-lactoglobulin gel structures. Food Hydrocolloids. 5:1991;339-352.
    • (1991) Food Hydrocolloids , vol.5 , pp. 339-352
    • Stading, M.1    Hermansson, A.-M.2
  • 40
    • 0000819132 scopus 로고
    • Molecular interactions in β-lactoglobulin. IV. The dissociation of β-lactoglobulin below pH 3.5
    • Townend R., Weinberger L., Timasheff S.N. Molecular interactions in β-lactoglobulin. IV. The dissociation of β-lactoglobulin below pH 3.5. Journal of the American Chemical Society. 82:1960;3175-3179.
    • (1960) Journal of the American Chemical Society , vol.82 , pp. 3175-3179
    • Townend, R.1    Weinberger, L.2    Timasheff, S.N.3
  • 42
    • 84974326036 scopus 로고
    • Heat-induced changes in sulphydryl and disulphide levels of β-lactoglobulin A and the formation of polymers
    • Watanabe K., Klostermeyer H. Heat-induced changes in sulphydryl and disulphide levels of β-lactoglobulin A and the formation of polymers. Journal of Dairy Research. 43:1976;411-418.
    • (1976) Journal of Dairy Research , vol.43 , pp. 411-418
    • Watanabe, K.1    Klostermeyer, H.2
  • 43
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions
    • Wen J., Arakawa T., Philo J.S. Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Analytical Biochemistry. 240:1996;155-166.
    • (1996) Analytical Biochemistry , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 44
    • 0002093929 scopus 로고
    • Combined differential light scattering with various liquid chromatographic separation techniques
    • S.E. Harding, D.B. Satelle, & V.A. Bloomfield. Cambridge: Royal Society of Chemistry
    • Wyatt P.J. Combined differential light scattering with various liquid chromatographic separation techniques. Harding S.E., Satelle D.B., Bloomfield V.A. Laser light scattering in biopolymers. 1992;35-58 Royal Society of Chemistry, Cambridge.
    • (1992) Laser Light Scattering in Biopolymers , pp. 35-58
    • Wyatt, P.J.1


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