메뉴 건너뛰기




Volumn 32, Issue 2, 2013, Pages 312-321

Effect of phospholipid molecular structure on its interaction with whey proteins in aqueous solution

Author keywords

Anionic zwitterionic phospholipids; Circular dichroism; Nuclear magnetic resonance; Whey protein phospholipid interactions

Indexed keywords

ACCIDENT PREVENTION; CHEMICAL SHIFT; CIRCULAR DICHROISM SPECTROSCOPY; CRYSTALLINE MATERIALS; HYDROPHOBICITY; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHOLIPIDS; PROTEINS; SURFACE ACTIVE AGENTS; ULTRAVIOLET SPECTROSCOPY;

EID: 84874402254     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2013.01.007     Document Type: Article
Times cited : (43)

References (42)
  • 1
    • 0000327631 scopus 로고
    • Standard errors and confidence intervals in nonlinear regression: comparison of Monte Carlo and parametric statistics
    • Alper J.S., Gelb R.I. Standard errors and confidence intervals in nonlinear regression: comparison of Monte Carlo and parametric statistics. The Journal of Physical Chemistry 1990, 94:4747-4751.
    • (1990) The Journal of Physical Chemistry , vol.94 , pp. 4747-4751
    • Alper, J.S.1    Gelb, R.I.2
  • 2
    • 20844448930 scopus 로고    scopus 로고
    • Structural changes of β-lactoglobulin during thermal unfolding and refolding - an FT-IR and circular dichroism study
    • Bhattacharjee C., Saha S., Biswas A., Kundu M., Ghosh L., Das K.P. Structural changes of β-lactoglobulin during thermal unfolding and refolding - an FT-IR and circular dichroism study. The Protein Journal 2005, 24:27-35.
    • (2005) The Protein Journal , vol.24 , pp. 27-35
    • Bhattacharjee, C.1    Saha, S.2    Biswas, A.3    Kundu, M.4    Ghosh, L.5    Das, K.P.6
  • 3
    • 51249181265 scopus 로고
    • Complex formation in sonicated mixtures of β-lactoglobulin and phosphatidylcholine
    • Brown E.M., Carroll R.J., Pfeffer P.E., Sampugna J. Complex formation in sonicated mixtures of β-lactoglobulin and phosphatidylcholine. Lipids 1983, 18:111-118.
    • (1983) Lipids , vol.18 , pp. 111-118
    • Brown, E.M.1    Carroll, R.J.2    Pfeffer, P.E.3    Sampugna, J.4
  • 4
    • 20844436321 scopus 로고    scopus 로고
    • Beta-lactoglobulin is a thermal marker in processed milk as studied by electrophoresis and circular dichroic spectra
    • Chen W.L., Hwang M.T., Liau C.Y., Ho J.C., Hong K.C., Mao S.J.T. Beta-lactoglobulin is a thermal marker in processed milk as studied by electrophoresis and circular dichroic spectra. Journal of Dairy Science 2005, 88:1618-1630.
    • (2005) Journal of Dairy Science , vol.88 , pp. 1618-1630
    • Chen, W.L.1    Hwang, M.T.2    Liau, C.Y.3    Ho, J.C.4    Hong, K.C.5    Mao, S.J.T.6
  • 5
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen Y.-H., Yang J.T., Martinez H.M. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 1972, 11:4120-4131.
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.-H.1    Yang, J.T.2    Martinez, H.M.3
  • 6
    • 63349108006 scopus 로고    scopus 로고
    • Improving the accuracy of pulsed field gradient NMR diffusion experiments: correction for gradient non-uniformity
    • Connell M.A., Bowyer P.J., Adam Bone P., Davis A.L., Swanson A.G., Nilsson M., et al. Improving the accuracy of pulsed field gradient NMR diffusion experiments: correction for gradient non-uniformity. Journal of Magnetic Resonance 2009, 198:121-131.
    • (2009) Journal of Magnetic Resonance , vol.198 , pp. 121-131
    • Connell, M.A.1    Bowyer, P.J.2    Adam Bone, P.3    Davis, A.L.4    Swanson, A.G.5    Nilsson, M.6
  • 7
    • 0021107160 scopus 로고
    • Intervesicular phospholipid transfer. A free-flow electrophoresis study
    • De Cuyper M., Joniau M., Dangreau H. Intervesicular phospholipid transfer. A free-flow electrophoresis study. Biochemistry 1983, 22:415-420.
    • (1983) Biochemistry , vol.22 , pp. 415-420
    • De Cuyper, M.1    Joniau, M.2    Dangreau, H.3
  • 8
    • 0035290424 scopus 로고    scopus 로고
    • Mild isolation procedure discloses new protein structural properties of beta-lactoglobulin
    • De Jongh H.H., Gröneveld T., De Groot J. Mild isolation procedure discloses new protein structural properties of beta-lactoglobulin. Journal of Dairy Science 2001, 84:562-571.
    • (2001) Journal of Dairy Science , vol.84 , pp. 562-571
    • De Jongh, H.H.1    Gröneveld, T.2    De Groot, J.3
  • 9
    • 58149196312 scopus 로고    scopus 로고
    • Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150 °C. A review
    • De Wit J.N. Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150 °C. A review. Trends in Food Science & Technology 2009, 20:27-34.
    • (2009) Trends in Food Science & Technology , vol.20 , pp. 27-34
    • De Wit, J.N.1
  • 10
    • 0031549131 scopus 로고    scopus 로고
    • Influence of an anionic surfactant on the rheology of heat-set [beta]-lactoglobulin-stabilized emulsion gels
    • Dickinson E., Hong S.T. Influence of an anionic surfactant on the rheology of heat-set [beta]-lactoglobulin-stabilized emulsion gels. Colloids and Surfaces A: Physicochemical and Engineering Aspects 1997, 127:1-10.
    • (1997) Colloids and Surfaces A: Physicochemical and Engineering Aspects , vol.127 , pp. 1-10
    • Dickinson, E.1    Hong, S.T.2
  • 11
    • 0034287494 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants
    • Gelamo E.L., Tabak M. Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2000, 56:2255-2271.
    • (2000) Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy , vol.56 , pp. 2255-2271
    • Gelamo, E.L.1    Tabak, M.2
  • 12
    • 2142837130 scopus 로고    scopus 로고
    • Heat treatment of whey proteins in the presence of anionic surfactants
    • Giroux H.J., Britten M. Heat treatment of whey proteins in the presence of anionic surfactants. Food Hydrocolloids 2004, 18:685-692.
    • (2004) Food Hydrocolloids , vol.18 , pp. 685-692
    • Giroux, H.J.1    Britten, M.2
  • 15
    • 0001424822 scopus 로고    scopus 로고
    • Suppression of convection artifacts in stimulated-echo diffusion experiments. Double-stimulated-echo experiments
    • Jerschow A., Müller N. Suppression of convection artifacts in stimulated-echo diffusion experiments. Double-stimulated-echo experiments. Journal of Magnetic Resonance 1997, 125:372-375.
    • (1997) Journal of Magnetic Resonance , vol.125 , pp. 372-375
    • Jerschow, A.1    Müller, N.2
  • 16
    • 84976155146 scopus 로고
    • Changes in milk on heating - viscosity measurements
    • Jeurnink T.J.M., Dekruif K.G. Changes in milk on heating - viscosity measurements. Journal of Dairy Research 1993, 60:139-150.
    • (1993) Journal of Dairy Research , vol.60 , pp. 139-150
    • Jeurnink, T.J.M.1    Dekruif, K.G.2
  • 17
    • 0001684352 scopus 로고
    • Surfactant interactions with biomembranes and proteins
    • Jones M.N. Surfactant interactions with biomembranes and proteins. Chemical Society Reviews 1992, 21:127-137.
    • (1992) Chemical Society Reviews , vol.21 , pp. 127-137
    • Jones, M.N.1
  • 18
    • 0031004544 scopus 로고    scopus 로고
    • The application of circular dichroism to studies of protein folding and unfolding
    • Kelly S.M., Price N.C. The application of circular dichroism to studies of protein folding and unfolding. Biochimica et biophysica acta 1997, 1338:161-185.
    • (1997) Biochimica et biophysica acta , vol.1338 , pp. 161-185
    • Kelly, S.M.1    Price, N.C.2
  • 19
    • 25144518570 scopus 로고    scopus 로고
    • Effect of thermal treatment on interfacial properties of beta-lactoglobulin
    • Kim D.a., Cornec M., Narsimhan G. Effect of thermal treatment on interfacial properties of beta-lactoglobulin. Journal of Colloid and Interface Science 2005, 285:100-109.
    • (2005) Journal of Colloid and Interface Science , vol.285 , pp. 100-109
    • Kim, D.A.1    Cornec, M.2    Narsimhan, G.3
  • 20
    • 0034633725 scopus 로고    scopus 로고
    • Interaction of beta-lactoglobulin with phospholipid bilayers: a molecular level elucidation as revealed by infrared spectroscopy
    • Lefèvre T., Subirade M. Interaction of beta-lactoglobulin with phospholipid bilayers: a molecular level elucidation as revealed by infrared spectroscopy. International Journal of Biological Macromolecules 2000, 28:59-67.
    • (2000) International Journal of Biological Macromolecules , vol.28 , pp. 59-67
    • Lefèvre, T.1    Subirade, M.2
  • 21
    • 0035839994 scopus 로고    scopus 로고
    • Conformational rearrangement of beta-lactoglobulin upon interaction with an anionic membrane
    • Lefèvre T., Subirade M. Conformational rearrangement of beta-lactoglobulin upon interaction with an anionic membrane. Biochimica et Biophysica acta 2001, 1549:37-50.
    • (2001) Biochimica et Biophysica acta , vol.1549 , pp. 37-50
    • Lefèvre, T.1    Subirade, M.2
  • 22
    • 33646889069 scopus 로고    scopus 로고
    • Conformational changes of beta-lactoglobulin induced by anionic phospholipid
    • Liu X., Shang L., Jiang X., Dong S., Wang E. Conformational changes of beta-lactoglobulin induced by anionic phospholipid. Biophysical Chemistry 2006, 121:218-223.
    • (2006) Biophysical Chemistry , vol.121 , pp. 218-223
    • Liu, X.1    Shang, L.2    Jiang, X.3    Dong, S.4    Wang, E.5
  • 23
    • 33646912243 scopus 로고    scopus 로고
    • Interactions of β-lactoglobulin with sodium decylsulfonate, decyltriethylammonium bromide, and their mixtures
    • Lu R.-C., Cao A.-N., Lai L.-H., Xiao J.-X. Interactions of β-lactoglobulin with sodium decylsulfonate, decyltriethylammonium bromide, and their mixtures. Journal of Colloid and Interface Science 2006, 299:617-625.
    • (2006) Journal of Colloid and Interface Science , vol.299 , pp. 617-625
    • Lu, R.-C.1    Cao, A.-N.2    Lai, L.-H.3    Xiao, J.-X.4
  • 24
    • 14544271897 scopus 로고    scopus 로고
    • Interaction between bovine serum albumin and equimolarly mixed cationic-anionic surfactants decyltriethylammonium bromide-sodium decyl sulfonate
    • Lu R.-C., Cao A.-N., Lai L.-H., Zhu B.-Y., Zhao G.-X., Xiao J.-X. Interaction between bovine serum albumin and equimolarly mixed cationic-anionic surfactants decyltriethylammonium bromide-sodium decyl sulfonate. Colloids and Surfaces. B, Biointerfaces 2005, 41:139-143.
    • (2005) Colloids and Surfaces. B, Biointerfaces , vol.41 , pp. 139-143
    • Lu, R.-C.1    Cao, A.-N.2    Lai, L.-H.3    Zhu, B.-Y.4    Zhao, G.-X.5    Xiao, J.-X.6
  • 25
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by Saturation Transfer Difference NMR spectroscopy
    • Mayer M., Meyer B. Characterization of ligand binding by Saturation Transfer Difference NMR spectroscopy. Angewandte Chemie International Edition 1999, 38:1784-1788.
    • (1999) Angewandte Chemie International Edition , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 26
    • 84864744643 scopus 로고    scopus 로고
    • Bovine β-lactoglobulin is dimeric under imitative physiological conditions: dissociation equilibrium and rate constants over the pH range of 2.5-7.5
    • Mercadante D., Melton L.D., Norris G.E., Loo T.S., Williams M.A.K., Dobson R.C.J., et al. Bovine β-lactoglobulin is dimeric under imitative physiological conditions: dissociation equilibrium and rate constants over the pH range of 2.5-7.5. Biophysical Journal 2012, 103:303-312.
    • (2012) Biophysical Journal , vol.103 , pp. 303-312
    • Mercadante, D.1    Melton, L.D.2    Norris, G.E.3    Loo, T.S.4    Williams, M.A.K.5    Dobson, R.C.J.6
  • 27
    • 0023661017 scopus 로고
    • Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 A resolution
    • Monaco H.L., Zanotti G., Spadon P., Bolognesi M., Sawyer L., Eliopoulos E.E. Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 A resolution. Journal of Molecular Biology 1987, 197:695-706.
    • (1987) Journal of Molecular Biology , vol.197 , pp. 695-706
    • Monaco, H.L.1    Zanotti, G.2    Spadon, P.3    Bolognesi, M.4    Sawyer, L.5    Eliopoulos, E.E.6
  • 28
    • 0037452731 scopus 로고    scopus 로고
    • Role of the surfactant polar head structure in protein-surfactant complexation: Zein Protein solubilization by SDS and by SDS/C12En Surfactant Solutions
    • Moore P.N., Puvvada S., Blankschtein D. Role of the surfactant polar head structure in protein-surfactant complexation: Zein Protein solubilization by SDS and by SDS/C12En Surfactant Solutions. Langmuir 2003, 19:1009-1016.
    • (2003) Langmuir , vol.19 , pp. 1009-1016
    • Moore, P.N.1    Puvvada, S.2    Blankschtein, D.3
  • 29
    • 79952534829 scopus 로고    scopus 로고
    • Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties
    • Moro A., Báez G.D., Busti P.a., Ballerini G.a., Delorenzi N.J. Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties. Food Hydrocolloids 2011, 25:1009-1015.
    • (2011) Food Hydrocolloids , vol.25 , pp. 1009-1015
    • Moro, A.1    Báez, G.D.2    Busti, P.A.3    Ballerini, G.A.4    Delorenzi, N.J.5
  • 30
    • 0343417669 scopus 로고
    • Protein-surfactant interactions. Nuclear magnetic resonance and binding isotherm studies of interactions between bovine serum albumin and sodium dodecyl sulphate
    • Oakes J. Protein-surfactant interactions. Nuclear magnetic resonance and binding isotherm studies of interactions between bovine serum albumin and sodium dodecyl sulphate. Journal of the Chemical Society, Faraday Transactions 1974, 1(70):2200-2209.
    • (1974) Journal of the Chemical Society, Faraday Transactions , vol.1 , Issue.70 , pp. 2200-2209
    • Oakes, J.1
  • 31
    • 0025827317 scopus 로고
    • Spontaneous phospholipid transfer: development of a quantitative model
    • Pownall H.J., Bick D.L.M., Massey J.B. Spontaneous phospholipid transfer: development of a quantitative model. Biochemistry 1991, 30(23):5696-5700. 10.1021/bi00237a009.
    • (1991) Biochemistry , vol.30 , Issue.23 , pp. 5696-5700
    • Pownall, H.J.1    Bick, D.L.M.2    Massey, J.B.3
  • 32
    • 2442688971 scopus 로고    scopus 로고
    • Heat stability of milk
    • Singh H. Heat stability of milk. International Journal Of Dairy Technology 2004, 57(2-3):111-119. 10.1111/j.1471-0307.2004.00143.x.
    • (2004) International Journal Of Dairy Technology , vol.57 , Issue.2-3 , pp. 111-119
    • Singh, H.1
  • 33
    • 0021740101 scopus 로고
    • Vesicle membrane-water partition coefficients determined from Fourier transform pulsed-gradient spin-echo NMR based self-diffusion data. Application to anesthetic binding in tetracaine-phosphatidylcholine-water systems
    • Stilbs P., Arvidson G., Lindblom G. Vesicle membrane-water partition coefficients determined from Fourier transform pulsed-gradient spin-echo NMR based self-diffusion data. Application to anesthetic binding in tetracaine-phosphatidylcholine-water systems. Chemistry and Physics of Lipids 1984, 35:309-314. 10.1016/0009-3084(84)90073-2.
    • (1984) Chemistry and Physics of Lipids , vol.35 , pp. 309-314
    • Stilbs, P.1    Arvidson, G.2    Lindblom, G.3
  • 34
    • 0017743991 scopus 로고
    • Further studies on detergent-induced conformational transitions in proteins. Circular dichroism of ovalbumin, bacterial α-amylase, papain, and β-lactoglobulin at various pH values
    • Su Y., Jirgensons B. Further studies on detergent-induced conformational transitions in proteins. Circular dichroism of ovalbumin, bacterial α-amylase, papain, and β-lactoglobulin at various pH values. Archives of Biochemistry and Biophysics 1977, 181(1):137-146. 10.1016/0003-9861(77)90491-X.
    • (1977) Archives of Biochemistry and Biophysics , vol.181 , Issue.1 , pp. 137-146
    • Su, Y.1    Jirgensons, B.2
  • 35
    • 71749087957 scopus 로고    scopus 로고
    • Widening the view on dispersant-pigment interactions in colloidal dispersions with Saturation Transfer Difference NMR spectroscopy
    • Szczygiel A., Timmermans L., Fritzinger B., Martins J.C. Widening the view on dispersant-pigment interactions in colloidal dispersions with Saturation Transfer Difference NMR spectroscopy. Journal of the American Chemical Society 2009, 131:17756-17758. 10.1021/ja905637y.
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 17756-17758
    • Szczygiel, A.1    Timmermans, L.2    Fritzinger, B.3    Martins, J.C.4
  • 36
    • 0000509349 scopus 로고
    • Secondary structures of bovine serum albumin in anionic and cationic surfactant solutions
    • Takeda K., Shigeta K., Aoki K. Secondary structures of bovine serum albumin in anionic and cationic surfactant solutions. Journal of Colloid and Interface Science 1987, 117:120-126. 10.1016/0021-9797(87)90174-3.
    • (1987) Journal of Colloid and Interface Science , vol.117 , pp. 120-126
    • Takeda, K.1    Shigeta, K.2    Aoki, K.3
  • 40
    • 1342293174 scopus 로고    scopus 로고
    • Conformational transitions in beta-lactoglobulin induced by cationic amphiphiles: equilibrium studies
    • Viseu M.I., Carvalho T.I., Costa S.M.B. Conformational transitions in beta-lactoglobulin induced by cationic amphiphiles: equilibrium studies. Biophysical Journal 2004, 86:2392-2402.
    • (2004) Biophysical Journal , vol.86 , pp. 2392-2402
    • Viseu, M.I.1    Carvalho, T.I.2    Costa, S.M.B.3
  • 41
    • 33744534909 scopus 로고    scopus 로고
    • Effects of heating at neutral and acid pH on the structure of beta-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy
    • Wada R., Fujita Y., Kitabatake N. Effects of heating at neutral and acid pH on the structure of beta-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy. Biochimica et biophysica acta 2006, 1760:841-847.
    • (2006) Biochimica et biophysica acta , vol.1760 , pp. 841-847
    • Wada, R.1    Fujita, Y.2    Kitabatake, N.3
  • 42
    • 33745830875 scopus 로고    scopus 로고
    • Lipid-induced conformational transitions of b-lactoglobulin
    • Zhang X., Keiderling T. Lipid-induced conformational transitions of b-lactoglobulin. Biochemistry 2006, 45:8444-8452.
    • (2006) Biochemistry , vol.45 , pp. 8444-8452
    • Zhang, X.1    Keiderling, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.