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Volumn 116, Issue 4, 2009, Pages 884-891

Copper modulates the heat-induced sulfhydryl/disulfide interchange reactions of β-Lactoglobulin

Author keywords

Lactoglobulin; Copper; Covalent dimer; Free sulfhydryl group; Heat induced denaturation aggregation

Indexed keywords

BETA LACTOGLOBULIN; COPPER; CUPRIC ION; DIMER; DISULFIDE; THIOL DERIVATIVE;

EID: 67349185830     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2009.03.043     Document Type: Article
Times cited : (26)

References (35)
  • 2
    • 2642562735 scopus 로고    scopus 로고
    • Influence of the ionic strength on the heat-induced aggregation of the globular protein β-lactoglobulin at pH 7
    • Baussay K., Le Bon C., Nicolai T., Durand D., and Busnel J.P. Influence of the ionic strength on the heat-induced aggregation of the globular protein β-lactoglobulin at pH 7. Journal of Biological Macromolecules 34 (2004) 21-28
    • (2004) Journal of Biological Macromolecules , vol.34 , pp. 21-28
    • Baussay, K.1    Le Bon, C.2    Nicolai, T.3    Durand, D.4    Busnel, J.P.5
  • 4
    • 11144233790 scopus 로고    scopus 로고
    • Copper-catalyzed formation of disulfide-linked dimer of bovine β-lactoglobulin
    • Bouhallab S., Henry G., Caussin F., Croguennec T., Fauquant J., and Mollé D. Copper-catalyzed formation of disulfide-linked dimer of bovine β-lactoglobulin. Le Lait 84 (2004) 517-525
    • (2004) Le Lait , vol.84 , pp. 517-525
    • Bouhallab, S.1    Henry, G.2    Caussin, F.3    Croguennec, T.4    Fauquant, J.5    Mollé, D.6
  • 5
    • 0032053268 scopus 로고    scopus 로고
    • Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey
    • Bryant M.C., and McClements D.J. Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey. Trends in Food Science and Technology 9 (1998) 143-151
    • (1998) Trends in Food Science and Technology , vol.9 , pp. 143-151
    • Bryant, M.C.1    McClements, D.J.2
  • 7
    • 0142117403 scopus 로고    scopus 로고
    • Mineral modulation of thermal aggregation and gelation of whey proteins: From beta-lactoglobulin model system to whey protein isolate
    • Caussin F., Famelart M.H., Maubois J.L., and Bouhallab S. Mineral modulation of thermal aggregation and gelation of whey proteins: From beta-lactoglobulin model system to whey protein isolate. Le Lait 83 (2003) 1-12
    • (2003) Le Lait , vol.83 , pp. 1-12
    • Caussin, F.1    Famelart, M.H.2    Maubois, J.L.3    Bouhallab, S.4
  • 8
    • 33846596245 scopus 로고    scopus 로고
    • Influence of binding conjugated linoleic acid and myristic acid on the heat- and high-pressure-induced unfolding and aggregation of beta-lactoglobulin B
    • Considine T., Patel H.A., Singh H., and Creamer L.K. Influence of binding conjugated linoleic acid and myristic acid on the heat- and high-pressure-induced unfolding and aggregation of beta-lactoglobulin B. Food Chemistry 102 (2007) 1270-1280
    • (2007) Food Chemistry , vol.102 , pp. 1270-1280
    • Considine, T.1    Patel, H.A.2    Singh, H.3    Creamer, L.K.4
  • 9
    • 1542575976 scopus 로고    scopus 로고
    • Heat-induced denaturation/aggregation of β-lactoglobulin A and B: Kinetics of the first intermediates formed
    • Croguennec T., O'Kennedy B.T., and Mehra R. Heat-induced denaturation/aggregation of β-lactoglobulin A and B: Kinetics of the first intermediates formed. International Dairy Journal 14 (2004) 399-409
    • (2004) International Dairy Journal , vol.14 , pp. 399-409
    • Croguennec, T.1    O'Kennedy, B.T.2    Mehra, R.3
  • 10
    • 0037039276 scopus 로고    scopus 로고
    • Does β-lactoglobulin denaturation occurs via an intermediate state?
    • D'Alfonso L., Collini M., and Baldini G. Does β-lactoglobulin denaturation occurs via an intermediate state?. Biochemistry 41 (2002) 326-333
    • (2002) Biochemistry , vol.41 , pp. 326-333
    • D'Alfonso, L.1    Collini, M.2    Baldini, G.3
  • 11
    • 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., and Hemar Y. Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins. Trends in Food Science and Technology 13 (2002) 262-274
    • (2002) Trends in Food Science and Technology , vol.13 , pp. 262-274
    • De la Fuente, M.A.1    Singh, H.2    Hemar, Y.3
  • 12
    • 58149196312 scopus 로고    scopus 로고
    • Thermal behaviour of bovine β-lactoglobulin at temperature up to 150 °C
    • 10.1016/j.tifs.2008.09.012
    • De Wit J.N. Thermal behaviour of bovine β-lactoglobulin at temperature up to 150 °C. A review, Trends in Food Science and Technology (2008) 10.1016/j.tifs.2008.09.012
    • (2008) A review, Trends in Food Science and Technology
    • De Wit, J.N.1
  • 15
    • 40849094204 scopus 로고    scopus 로고
    • Dynamic rearrangement of disulfide bridges influences solubility of whey protein coatings
    • Floris R., Bondar I., Weinbreck F., and Alting A.C. Dynamic rearrangement of disulfide bridges influences solubility of whey protein coatings. International Dairy Journal 18 (2008) 566-573
    • (2008) International Dairy Journal , vol.18 , pp. 566-573
    • Floris, R.1    Bondar, I.2    Weinbreck, F.3    Alting, A.C.4
  • 17
    • 0000008542 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin: Role of free thiol group and disulfide bonds
    • Hoffmann M.A.M., and van Mil P.J.J.M. Heat-induced aggregation of β-lactoglobulin: Role of 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
  • 18
    • 0029924648 scopus 로고    scopus 로고
    • Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin
    • Iametti S., Degregori B., Vecchio G., and Bonomi F. Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. European Journal of Biochemistry 237 (1996) 106-112
    • (1996) European Journal of Biochemistry , vol.237 , pp. 106-112
    • Iametti, S.1    Degregori, B.2    Vecchio, G.3    Bonomi, F.4
  • 20
    • 0034856440 scopus 로고    scopus 로고
    • Reversible conformational change in β-lactoglobulin A modified with N-ethylmaleimide and resistance to molecular aggregation on heating
    • Kitabatake N., Wada R., and Fujita Y. Reversible conformational change in β-lactoglobulin A modified with N-ethylmaleimide and resistance to molecular aggregation on heating. Journal of Agricultural and Food Chemistry 49 (2001) 4011-4018
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 4011-4018
    • Kitabatake, N.1    Wada, R.2    Fujita, Y.3
  • 21
    • 4243120936 scopus 로고    scopus 로고
    • Invited review: Beta-lactoglobulin: Binding properties, structure, and function
    • Kontopidis G., Holt C., and Sawyer L. Invited review: Beta-lactoglobulin: Binding properties, structure, and function. Journal of Dairy Science 87 (2004) 785-796
    • (2004) Journal of Dairy Science , vol.87 , pp. 785-796
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 9144274502 scopus 로고    scopus 로고
    • (S)-Cysteine chemisorption on Cu (1 1 0) from the gas or liquid phase An FT-RAIRS and XPS study
    • Mateo Marti E., Methivier C., and Pradier C.M. (S)-Cysteine chemisorption on Cu (1 1 0) from the gas or liquid phase An FT-RAIRS and XPS study. Science 20 (2004) 10223-10230
    • (2004) Science , vol.20 , pp. 10223-10230
    • Mateo Marti, E.1    Methivier, C.2    Pradier, C.M.3
  • 24
    • 0005518437 scopus 로고    scopus 로고
    • Milk microfiltrate, a convenient starting material for fractionation of whey proteins and derivatives
    • Munich, Germany, September 12-14
    • Maubois, J.-L., Fauquant, J., Famelart, M. H., & Caussin, F. (2001) Milk microfiltrate, a convenient starting material for fractionation of whey proteins and derivatives. In Proceedings of the third International whey conference (pp. 59-72), Munich, Germany, September 12-14.
    • (2001) Proceedings of the third International whey conference , pp. 59-72
    • Maubois, J.-L.1    Fauquant, J.2    Famelart, M.H.3    Caussin, F.4
  • 25
    • 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., and 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
  • 26
    • 35748948052 scopus 로고    scopus 로고
    • Thermal aggregation of β-lactoglobulin in presence of metal ions
    • Navarra G., Leone M., and Militello V. Thermal aggregation of β-lactoglobulin in presence of metal ions. Biophysical Chemistry 131 (2007) 52-61
    • (2007) Biophysical Chemistry , vol.131 , pp. 52-61
    • Navarra, G.1    Leone, M.2    Militello, V.3
  • 29
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6, 7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis
    • Qi X.L., Holt C., Mc Nulty D., Clarke D.T., Brownlow S., and Jones G.R. Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6, 7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis. Biochemical Journal 324 (1997) 341-346
    • (1997) Biochemical Journal , vol.324 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    Mc Nulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 30
    • 0028567981 scopus 로고
    • A model of the denaturation and aggregation of β-lactoglobulin
    • Roefs S.P.F.M., and de Kruif K.G. A model of 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
  • 31
    • 0033501546 scopus 로고    scopus 로고
    • Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin at neutral pH
    • Schokker E.P., Singh H., Pinder D.N., Norris G.E., and Creamer L.K. Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin at neutral pH. International Dairy Journal 9 (1999) 791-800
    • (1999) International Dairy Journal , vol.9 , pp. 791-800
    • Schokker, E.P.1    Singh, H.2    Pinder, D.N.3    Norris, G.E.4    Creamer, L.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.