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Volumn 52, Issue 17, 2004, Pages 5527-5532

Specificity of disulfide bond formation during thermal aggregation in solutions of β-lactoglobulin B and κ-casein A

Author keywords

lactoglobulin; casein; Cysteine; Cystine; Disulfide bonds; Heat induced aggregation; Mass spectrometry; Milk proteins; Thiol

Indexed keywords

BETA LACTOGLOBULIN; CASEIN; CYSTEINE; KAPPA CASEIN A; PEPTIDE; UNCLASSIFIED DRUG;

EID: 4143094993     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf049955h     Document Type: Article
Times cited : (42)

References (30)
  • 2
    • 0032838780 scopus 로고    scopus 로고
    • Effects of heat treatment and whey protein addition on the rheological properties and structure of acid skim milk gels
    • Lucey, J. A.; Munro, P. A. Singh, H. Effects of heat treatment and whey protein addition on the rheological properties and structure of acid skim milk gels. Int. Dairy J, 1999, 9, 275-279.
    • (1999) Int. Dairy J. , vol.9 , pp. 275-279
    • Lucey, J.A.1    Munro, P.A.2    Singh, H.3
  • 3
    • 0348110233 scopus 로고    scopus 로고
    • Role of the soluble and micelle-bound heat-induced protein aggregates on network formation in acid skim milk gels
    • Guyomarc'h, F.; Queguiner, C.; Law, A. J. R.; Horne, D. S.; Dalgleish, D. G. Role of the soluble and micelle-bound heat-induced protein aggregates on network formation in acid skim milk gels, J. Agric. Food Chem. 2003, 51, 7743-7750.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 7743-7750
    • Guyomarc'h, F.1    Queguiner, C.2    Law, A.J.R.3    Horne, D.S.4    Dalgleish, D.G.5
  • 7
    • 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
  • 8
    • 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, 6572.
    • (1998) Int. Dairy J. , vol.8 , pp. 6572
    • Sawyer, L.1    Brownlow, S.2    Polikarpov, I.3    Wu, S.Y.4
  • 9
    • 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
  • 10
    • 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. I. 1996, 9602, 341-349.
    • (1996) Int. Dairy Fed. S. I. , vol.9602 , pp. 341-349
    • Iametti, S.1    Bonomi, F.2
  • 11
    • 0000008540 scopus 로고    scopus 로고
    • Thermal unfolding of β-lactoglobulin: Characterization of initial unfolding events responsible for heat-induced sggregation
    • Prabakaran, S.; Damodaran, S. Thermal unfolding of β-lactoglobulin: characterization of initial unfolding events responsible for heat-induced sggregation. J. Agric. Food Chem. 1997, 45, 4303-4308.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 4303-4308
    • Prabakaran, S.1    Damodaran, S.2
  • 12
    • 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
  • 13
    • 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. 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.J.J.M.2
  • 14
    • 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
  • 15
    • 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
  • 16
    • 4143054391 scopus 로고    scopus 로고
    • Chemistry of the caseins
    • Fox, P. F., McSweeney, P. L. H., Eds.; Kluwer Academic/Plenum Publishers: New York, 3
    • Swaisgood, H. E. Chemistry of the caseins. In Advanced Dairy Chemistry-1: Proteins; Fox, P. F., McSweeney, P. L. H., Eds.; Kluwer Academic/Plenum Publishers: New York, 2003; Part A, 3, pp 139-202.
    • (2003) Advanced Dairy Chemistry-1: Proteins , Issue.PART A , pp. 139-202
    • Swaisgood, H.E.1
  • 17
    • 0348114294 scopus 로고    scopus 로고
    • Casein micelle structure, functions and interactions
    • Fox, P. F., McSweeney, P. L. H., Eds.; Kluwer Academic/Plenum Publishers: New York, 3
    • DeKruif, C. G.; Holt, C. Casein micelle structure, functions and interactions. In Advanced Dairy Chemistry-1: Proteins; Fox, P. F., McSweeney, P. L. H., Eds.; Kluwer Academic/Plenum Publishers: New York, 2003; Part A, 3, pp 233-276.
    • (2003) Advanced Dairy Chemistry-1: Proteins , Issue.PART A , pp. 233-276
    • DeKruif, C.G.1    Holt, C.2
  • 18
    • 0000599870 scopus 로고
    • The enzymatic coagulation of milk
    • Fox, P. F., Ed.; Elsevier Applied Science: London, U.K.
    • Dalgleish, D. G. The enzymatic coagulation of milk. In Advanced Dairy Chemistry-1: Proteins; Fox, P. F., Ed.; Elsevier Applied Science: London, U.K., 1992; pp 579-620.
    • (1992) Advanced Dairy Chemistry-1: Proteins , pp. 579-620
    • Dalgleish, D.G.1
  • 19
    • 0026552375 scopus 로고
    • Reexamination of the polymeric distributions of κ-casein isolated from bovine milk
    • Groves, M. L.; Dower, H. J.; Farrell, H. M., Jr. Reexamination of the polymeric distributions of κ-casein isolated from bovine milk. J. Protein Chem, 1992, 11, 21-28.
    • (1992) J. Protein Chem. , vol.11 , pp. 21-28
    • Groves, M.L.1    Dower, H.J.2    Farrell Jr., H.M.3
  • 20
    • 54749100755 scopus 로고    scopus 로고
    • Environmental effects on disulfide bonding patterns of bovine K-casein
    • Groves, M. L.; Wickham, E. D.; Farrell, H. M., Jr. Environmental effects on disulfide bonding patterns of bovine K-casein. J, Protein Chem. 1998, 17, 73-84.
    • (1998) J. Protein Chem. , vol.17 , pp. 73-84
    • Groves, M.L.1    Wickham, E.D.2    Farrell Jr., H.M.3
  • 21
    • 0026683462 scopus 로고
    • The multimeric structure and disulfide-bonding pattern of bovine κ-casein
    • Rasmussen, L. K.; Hojrup, P.; Petersen, T. E. The multimeric structure and disulfide-bonding pattern of bovine κ-casein. Eur. J. Biochem. 1992, 207, 215-222.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 215-222
    • Rasmussen, L.K.1    Hojrup, P.2    Petersen, T.E.3
  • 22
    • 0037327004 scopus 로고    scopus 로고
    • Heat-induced interactions of β-lactoglobulin A and κ-casein B in a model system
    • Cho, Y.; Singh, H.; Creamer, L. K. Heat-induced interactions of β-lactoglobulin A and κ-casein B in a model system. J. Dairy Res. 2003, 70, 61-71.
    • (2003) J. Dairy Res. , vol.70 , pp. 61-71
    • Cho, Y.1    Singh, H.2    Creamer, L.K.3
  • 23
    • 0036006646 scopus 로고    scopus 로고
    • Heat-induced covalent complex between casein micelles and beta-lactoglobulin from goat's milk: Identification of an involved disulfide bond
    • Henry, G.; Mollé, D.; Morgan, F.; Fauquant, J.; Bouhallab, S, Heat-induced covalent complex between casein micelles and beta-lactoglobulin from goat's milk: identification of an involved disulfide bond. J. Agric. Food Chem. 2002, 50, 185-191.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 185-191
    • Henry, G.1    Mollé, D.2    Morgan, F.3    Fauquant, J.4    Bouhallab, S.5
  • 24
    • 0011298264 scopus 로고
    • The sizes and conformations of the proteins in adsorbed layers of individual caseins on lattices and in oil-in-water emulsions
    • Dalgleish, D. G. The sizes and conformations of the proteins in adsorbed layers of individual caseins on lattices and in oil-in-water emulsions. Colloid Surf. B: Biointetfaces 1993, 1, 1-8.
    • (1993) Colloid Surf. B: Biointetfaces , vol.1 , pp. 1-8
    • Dalgleish, D.G.1
  • 25
    • 0000930823 scopus 로고
    • Separation of major casein fractions using cation-exchange fast protein liquid chromatography
    • Hollar, C. M.; Law, A. J. R.; Dalgleish, D. G.; Brown, R. J. Separation of major casein fractions using cation-exchange fast protein liquid chromatography. J. Dairy Sci. 1991, 74, 2403-2409.
    • (1991) J. Dairy Sci. , vol.74 , pp. 2403-2409
    • Hollar, C.M.1    Law, A.J.R.2    Dalgleish, D.G.3    Brown, R.J.4
  • 26
    • 0346336103 scopus 로고    scopus 로고
    • Steric effects governing disulfide bond interchange during thermal aggregation in solutions of β-lactoglobulin B and α-lactalbumin
    • Livney, Y. D.; Verespej, E.; Dalgleish, D. G. Steric effects governing disulfide bond interchange during thermal aggregation in solutions of β-lactoglobulin B and α-lactalbumin. J. Agric. Food Chem. 2003, 51, 8098-8106.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 8098-8106
    • Livney, Y.D.1    Verespej, E.2    Dalgleish, D.G.3
  • 27
    • 4143128515 scopus 로고    scopus 로고
    • ExPASy Molecular Biology Server. Swiss Institute of Bioinformatics (SIB)
    • Swiss-Prot Protein knowledgebase. ExPASy Molecular Biology Server; Swiss Institute of Bioinformatics (SIB), 2003; http:// www.expasy.org/sprot/.
    • (2003) Swiss-Prot Protein Knowledgebase
  • 28
    • 0348008332 scopus 로고    scopus 로고
    • copyright 1995-2003; The Regents of the University of California
    • Baker, P.; Clauser, K. MS-Digest©. ProteinProspector 4.04, copyright 1995-2003; The Regents of the University of California, 2002; http://prospector.ucsf.edu/ucsfhtml4.0/msdigest.htm.
    • (2002) MS-Digest©. ProteinProspector 4.04
    • Baker, P.1    Clauser, K.2
  • 29
    • 0036704306 scopus 로고    scopus 로고
    • Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins
    • de la Fuente, M. A.; Singh, H.; Hemar, Y. Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins. Trends Food Sci. Technol. 2002, 13, 262-274.
    • (2002) Trends Food Sci. Technol. , vol.13 , pp. 262-274
    • De La Fuente, M.A.1    Singh, H.2    Hemar, Y.3
  • 30
    • 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. Commun. 2003, 301, 465-471.
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 465-471
    • Croguennec, T.1    Bouhallab, S.2    Mollé, D.3    O'Kennedy, B.T.4    Mehra, R.5


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