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Volumn 51, Issue 27, 2003, Pages 8098-8106

Steric Effects Governing Disulfide Bond Interchange during Thermal Aggregation in Solutions of β-Lactoglobulin B and α-Lactalbumin

Author keywords

lactalbumin; lactoglobulin; Cysteine; Disulfide bonds; Heat induced aggregation; Mass spectrometry; Thiol; Whey proteins

Indexed keywords

ALPHA LACTALBUMIN; BETA LACTOGLOBULIN; CYSTEINE; MONOMER; THIOL GROUP;

EID: 0346336103     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf034582q     Document Type: Article
Times cited : (56)

References (36)
  • 1
    • 0032016551 scopus 로고    scopus 로고
    • Nutritional and functional characteristics of whey proteins in food products
    • De Wit, J. N. Nutritional and functional characteristics of whey proteins in food products. J. Dairy Sci. 1998, 81, 597-608.
    • (1998) J. Dairy Sci. , vol.81 , pp. 597-608
    • De Wit, J.N.1
  • 4
    • 0036228989 scopus 로고    scopus 로고
    • Flexibility, functionality and hydrophobicity of bovine β-lactoglobulin
    • Jameson, G. B.; Adams, J. J.; Creamer, L. K. Flexibility, functionality and hydrophobicity of bovine β-lactoglobulin. Int. Dairy J. 2002, 12, 319-329.
    • (2002) Int. Dairy J. , vol.12 , pp. 319-329
    • Jameson, G.B.1    Adams, J.J.2    Creamer, L.K.3
  • 5
    • 0031999034 scopus 로고    scopus 로고
    • β-lactoglobulin: Structural studies, biological clues
    • Sawyer, L.; Brownlow, S.; Polikarpov, I.; Wu, S. Y. β-Lactoglobulin: structural studies, biological clues. Int. Dairy J. 1998, 8, 65-72.
    • (1998) Int. Dairy J. , vol.8 , pp. 65-72
    • Sawyer, L.1    Brownlow, S.2    Polikarpov, I.3    Wu, S.Y.4
  • 6
    • 0030185806 scopus 로고    scopus 로고
    • Thermal unfolding of β-lactoglobulin, α-lactalbumin, and bovine serum albumin. A thermodynamic approach
    • Relkin, P. Thermal unfolding of β-lactoglobulin, α-lactalbumin, and bovine serum albumin. A thermodynamic approach. Crit. Rev. Food Sci. Nutr. 1996, 36, 565-601.
    • (1996) Crit. Rev. Food Sci. Nutr. , vol.36 , pp. 565-601
    • Relkin, P.1
  • 7
    • 0005555237 scopus 로고    scopus 로고
    • Transient modification of the association equilibria in heated β-lactoglobulin
    • Iametti, S.; Bonomi, F. Transient modification of the association equilibria in heated β-lactoglobulin. Int. Dairy Fed. S. 1. 1996, 9602, 341-349.
    • (1996) Int. Dairy Fed. S. 1 , vol.9602 , pp. 341-349
    • Iametti, S.1    Bonomi, F.2
  • 8
    • 0000008540 scopus 로고    scopus 로고
    • Thermal unfolding of β-lactoglobulin: Characterization of initial unfolding events responsible for heat-induced aggregation
    • Prabakaran, S.; Damodaran, S. Thermal unfolding of β-lactoglobulin: characterization of initial unfolding events responsible for heat-induced aggregation. J. Agric. Food Chem. 1997, 45, 4303-4308.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 4303-4308
    • Prabakaran, S.1    Damodaran, S.2
  • 9
    • 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. Eur. J. Biochem. 1994, 226, 883-889.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 883-889
    • Roefs, S.P.F.M.1    De Kruif, K.G.2
  • 10
    • 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. P. J. M. Heat-induced aggregation of β-lactoglobulin: role of the free thiol group and disulfide bonds. J. Agric. Food Chem. 1997, 45, 2942-2948.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 2942-2948
    • Hoffmann, M.A.M.1    Van Mil, P.P.J.M.2
  • 11
    • 0001029710 scopus 로고    scopus 로고
    • Growth and structure of aggregates of heat-denatured β-lactoglobulin
    • Le Bon, C.; Nicolai, T.; Durand, D. Growth and structure of aggregates of heat-denatured β-lactoglobulin. Int. J. Food Sci. Technol. 1999, 34, 451-465.
    • (1999) Int. J. Food Sci. Technol. , vol.34 , pp. 451-465
    • Le Bon, C.1    Nicolai, T.2    Durand, D.3
  • 12
    • 0033501546 scopus 로고    scopus 로고
    • Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH
    • Schokker, E. P.; Singh, H.; Pinder, D. N.; Norris, G. E.; Creamer, L. K. Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH. Int. Dairy J. 2000, 9, 791-800.
    • (2000) Int. Dairy J. , vol.9 , pp. 791-800
    • Schokker, E.P.1    Singh, H.2    Pinder, D.N.3    Norris, G.E.4    Creamer, L.K.5
  • 13
    • 0342374989 scopus 로고    scopus 로고
    • Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation
    • Le Bon, C.; Nicolai, T.; Durand, D. Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation. Macromolecules 1999, 32, 6120-6127.
    • (1999) Macromolecules , vol.32 , pp. 6120-6127
    • Le Bon, C.1    Nicolai, T.2    Durand, D.3
  • 14
    • 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 1994, 8, 441-453.
    • (1994) Food Hydrocolloids , vol.8 , pp. 441-453
    • McSwiney, M.1    Singh, H.2    Campanella, O.H.3
  • 15
    • 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. J. Agric. Food Chem. 1989, 37, 161-168.
    • (1989) J. Agric. Food Chem. , vol.37 , pp. 161-168
    • Shimada, K.1    Cheftel, J.C.2
  • 16
    • 0000295322 scopus 로고    scopus 로고
    • Kinetics of heat-induced aggregation of β-Lactoglobulin
    • Verheul, M.; Roefs, S. P. F. M.; De Kruif, K. G. Kinetics of heat-induced aggregation of β-Lactoglobulin. J. Agric. Food Chem. 1998, 46, 896-903.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 896-903
    • Verheul, M.1    Roefs, S.P.F.M.2    De Kruif, K.G.3
  • 17
    • 0000706426 scopus 로고    scopus 로고
    • Heat-induced denaturation and aggregation of β-lactoglobulin: Kinetics of formation of hydrophobic and disulphide-linked aggregates
    • Galani, D.; Apenten, R. K. O. Heat-induced denaturation and aggregation of β-lactoglobulin: kinetics of formation of hydrophobic and disulphide-linked aggregates. Int. J. Food Sci. Technol. 1999, 34, 467-476.
    • (1999) Int. J. Food Sci. Technol. , vol.34 , pp. 467-476
    • Galani, D.1    Apenten, R.K.O.2
  • 18
    • 0037423721 scopus 로고    scopus 로고
    • Stable monomeric intermediate with exposed Cys-119 is formed during heat denaturation of β-lactoglobulin
    • Croguennec, T.; Bouhallab, S.; Mollé, D.; O'Kennedy, B. T.; Mehra, R. Stable monomeric intermediate with exposed Cys-119 is formed during heat denaturation of β-lactoglobulin. Biochem. Biophys. Res. Comum. 2003, 301, 465-471.
    • (2003) Biochem. Biophys. Res. Comum. , vol.301 , pp. 465-471
    • Croguennec, T.1    Bouhallab, S.2    Mollé, D.3    O'Kennedy, B.T.4    Mehra, R.5
  • 19
    • 0037073089 scopus 로고    scopus 로고
    • Towards the understanding of molecular mechanisms in the early stages of heat-induced aggregation of β-lactoglobulin AB
    • Surroca, Y.; Haverkamp, J.; Heck, A. J. R. Towards the understanding of molecular mechanisms in the early stages of heat-induced aggregation of β-lactoglobulin AB. J. Chromatogr. A 2002, 970, 275-285.
    • (2002) J. Chromatogr. A , vol.970 , pp. 275-285
    • Surroca, Y.1    Haverkamp, J.2    Heck, A.J.R.3
  • 20
    • 0001447396 scopus 로고
    • α-lactalbumin
    • Fox, P. F., Ed.; Elsevier Applied Science: London, U.K.
    • Brew, K.; Grobler, J. A. α-Lactalbumin. In Advanced Dairy Chemistry-1: Proteins; Fox, P. F., Ed.; Elsevier Applied Science: London, U.K., 1992; pp 191-229.
    • (1992) Advanced Dairy Chemistry-1: Proteins , pp. 191-229
    • Brew, K.1    Grobler, J.A.2
  • 21
    • 0034711229 scopus 로고    scopus 로고
    • Crystal structures of apo- and holo-bovine α-lactalbumin at 2.2-Å resolution reveal an effect of calcium on inter-lobe interactions
    • Chrysina, E. D.; Brew, K.; Acharya, K. R. Crystal structures of apo- and holo-bovine α-lactalbumin at 2.2-Å resolution reveal an effect of calcium on inter-lobe interactions. J. Biol. Chem. 2000, 275, 37021-37029.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37021-37029
    • Chrysina, E.D.1    Brew, K.2    Acharya, K.R.3
  • 22
    • 0000318442 scopus 로고
    • Irreversible heat denaturation of bovine α-lactalbumin
    • Chaplin, L. C.; Lyster, R. L. J. Irreversible heat denaturation of bovine α-lactalbumin. J. Dairy Res. 1986, 53, 249-258.
    • (1986) J. Dairy Res. , vol.53 , pp. 249-258
    • Chaplin, L.C.1    Lyster, R.L.J.2
  • 23
    • 0001701660 scopus 로고    scopus 로고
    • The conformation of α-lactalbumin as a function of pH, heat treatment and adsorption at hydrophobic surfaces studied by FTIR
    • Fang, Y.; Dalgleish, D. G. The conformation of α-lactalbumin as a function of pH, heat treatment and adsorption at hydrophobic surfaces studied by FTIR. Food Hydrocolloids 1998, 12, 121-126.
    • (1998) Food Hydrocolloids , vol.12 , pp. 121-126
    • Fang, Y.1    Dalgleish, D.G.2
  • 24
    • 0038403043 scopus 로고
    • Chromatographic evidence for heat-induced interaction of α-lactalbumin and β-lactoglobulin
    • Hunziker, H. G.; Tarassuk, N. P. Chromatographic evidence for heat-induced interaction of α-lactalbumin and β-lactoglobulin. J. Dairy Sci. 1965, 48, 733-734.
    • (1965) J. Dairy Sci. , vol.48 , pp. 733-734
    • Hunziker, H.G.1    Tarassuk, N.P.2
  • 25
    • 0000053442 scopus 로고
    • Influence of other whey proteins on the heat-induced aggregation of α-lactalbumin
    • Calvo, M. M.; Leaver, J.; Banks, J. M. Influence of other whey proteins on the heat-induced aggregation of α-lactalbumin. Int. Dairy J. 1993, 3, 719-727.
    • (1993) Int. Dairy J. , vol.3 , pp. 719-727
    • Calvo, M.M.1    Leaver, J.2    Banks, J.M.3
  • 26
    • 0001406422 scopus 로고    scopus 로고
    • Interactions between α-lactalbumin and β-lactoglobulin in the early stages of heat denaturation
    • Dalgleish, D. G.; Senaratne, V.; Francois, S. Interactions between α-lactalbumin and β-lactoglobulin in the early stages of heat denaturation. J. Agric. Food Chem. 1997, 45, 3459-3464.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 3459-3464
    • Dalgleish, D.G.1    Senaratne, V.2    Francois, S.3
  • 27
    • 0034462997 scopus 로고    scopus 로고
    • Heat-induced aggregation of α-lactoglobulin A and B with α-lactalbumin
    • Schokker, E. P.; Singh, H.; Creamer, L. K. Heat-induced aggregation of α-lactoglobulin A and B with α-lactalbumin. Int. Dairy J. 2000, 10, 843-853.
    • (2000) Int. Dairy J. , vol.10 , pp. 843-853
    • Schokker, E.P.1    Singh, H.2    Creamer, L.K.3
  • 28
    • 0034768130 scopus 로고    scopus 로고
    • Characterization of heat-induced aggregates of β-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment
    • Havea, P.; Singh, H.; Creamer, L. K. Characterization of heat-induced aggregates of β-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment. J. Dairy Res. 2003, 68, 483-497.
    • (2003) J. Dairy Res. , vol.68 , pp. 483-497
    • Havea, P.1    Singh, H.2    Creamer, L.K.3
  • 29
    • 0036230909 scopus 로고    scopus 로고
    • Changed protein structures of bovine fi-lactoglobulin B and α-lactalbumin as a consequence of heat treatment
    • Hong, Y. H.; Creamer, L. K. Changed protein structures of bovine fi-lactoglobulin B and α-lactalbumin as a consequence of heat treatment. Int. Dairy J. 2002, 12, 345-359.
    • (2002) Int. Dairy J. , vol.12 , pp. 345-359
    • Hong, Y.H.1    Creamer, L.K.2
  • 30
    • 0033858518 scopus 로고    scopus 로고
    • Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: A differential scanning calorimetric study
    • Boye, J. I.; Alli, I. Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: a differential scanning calorimetric study. Food Res. Int. 2000, 33, 673-682.
    • (2000) Food Res. Int. , vol.33 , pp. 673-682
    • Boye, J.I.1    Alli, I.2
  • 31
    • 0347377945 scopus 로고
    • Thermodynamic parameters of thermal denaturation of β-lactoglobulin and of α-lactalbumin
    • Relkin, P.; Eynard, L.; Launay, B. Thermodynamic parameters of thermal denaturation of β-lactoglobulin and of α-lactalbumin. Calorim. Anal. Therm. 1992, 22, 177-184.
    • (1992) Calorim. Anal. Therm. , vol.22 , pp. 177-184
    • Relkin, P.1    Eynard, L.2    Launay, B.3
  • 32
    • 0348008332 scopus 로고    scopus 로고
    • Copyright (1995-2003), The Regents of the University of California
    • Baker, P.; Clauser, K. MS-Digest. ProteinProspector 4.04; http:// prospector.ucsf.edu/ucsfhtml4.0/msdigest.htm; Copyright (1995-2003), The Regents of the University of California, 2002.
    • (2002) MS-Digest. ProteinProspector 4.04
    • Baker, P.1    Clauser, K.2
  • 33
    • 0001592750 scopus 로고    scopus 로고
    • Heat-induced interactions and gelation of mixtures of β-lactoglobulin and α-lactalbumin
    • Gezimati, J.; Creamer, L. K.; Singh, H. Heat-induced interactions and gelation of mixtures of β-lactoglobulin and α-lactalbumin. J. Agric. Food Chem. 1997, 45, 1130-1136.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1130-1136
    • Gezimati, J.1    Creamer, L.K.2    Singh, H.3
  • 34
    • 0030582682 scopus 로고    scopus 로고
    • Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL
    • Katsumata, K.; Okazaki, A.; Tsurupa, P.; Kuwajima, K. Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL. J. Mol. Biol. 1996, 264, 643-649.
    • (1996) J. Mol. Biol. , vol.264 , pp. 643-649
    • Katsumata, K.1    Okazaki, A.2    Tsurupa, P.3    Kuwajima, K.4
  • 35
    • 1842421133 scopus 로고    scopus 로고
    • The role of α-lactalbumin in heat-induced gelation of whey proteins
    • ACS Symposium Series 650; Parris, N., Kato, A., Creamer, L. K., Pearce, J., Eds.; American Chemical Society: Washington, DC
    • Matsudomi, N.; Oshita, T. The role of α-lactalbumin in heat-induced gelation of whey proteins. In Macromolecular Interactions in Food Technology; ACS Symposium Series 650; Parris, N., Kato, A., Creamer, L. K., Pearce, J., Eds.; American Chemical Society: Washington, DC, 1996; pp 93-103.
    • (1996) Macromolecular Interactions in Food Technology , pp. 93-103
    • Matsudomi, N.1    Oshita, T.2
  • 36
    • 0025182227 scopus 로고
    • Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond
    • Kuwajima, K.; Ikeguchi, M.; Sugawara, T.; Hiraoka, Y.; Sugai, S. Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond. Biochemistry 1990, 29, 8240-8249.
    • (1990) Biochemistry , vol.29 , pp. 8240-8249
    • Kuwajima, K.1    Ikeguchi, M.2    Sugawara, T.3    Hiraoka, Y.4    Sugai, S.5


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