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Volumn 213, Issue , 2016, Pages 431-439

Characterization of flavonoid-protein interactions using fluorescence spectroscopy: Binding of pelargonidin to dairy proteins

Author keywords

Anthocyanins; Flavonoids; Fluorescence; Milk proteins; Pelargonidin; Sodium caseinate; Whey protein isolate; Lactoglobulin

Indexed keywords

ANTHOCYANINS; BINDING SITES; DAIRIES; DICHROISM; FLAVONOIDS; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; QUENCHING; THERMODYNAMICS;

EID: 84977274027     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2016.06.105     Document Type: Article
Times cited : (196)

References (40)
  • 1
    • 84878314960 scopus 로고    scopus 로고
    • Binding of resveratrol with sodium caseinate in aqueous solutions
    • Acharya, D.P., Sanguansri, L., Augustin, M.A., Binding of resveratrol with sodium caseinate in aqueous solutions. Food Chemistry 141:2 (2013), 1050–1054.
    • (2013) Food Chemistry , vol.141 , Issue.2 , pp. 1050-1054
    • Acharya, D.P.1    Sanguansri, L.2    Augustin, M.A.3
  • 3
    • 0031035104 scopus 로고    scopus 로고
    • Anthocyanins as natural food colours—selected aspects
    • Bridle, P., Timberlake, C.F., Anthocyanins as natural food colours—selected aspects. Food Chemistry 58:1–2 (1997), 103–109.
    • (1997) Food Chemistry , vol.58 , Issue.1-2 , pp. 103-109
    • Bridle, P.1    Timberlake, C.F.2
  • 4
    • 78249284364 scopus 로고    scopus 로고
    • Anticancer activities of an anthocyanin-rich extract from black rice against breast cancer cells in vitro and in vivo
    • Chang, H., Yu, B., Yu, X., Yi, L., Chen, C., Mi, M., et al. Anticancer activities of an anthocyanin-rich extract from black rice against breast cancer cells in vitro and in vivo. Nutrition & Cancer 62:8 (2010), 1128–1136.
    • (2010) Nutrition & Cancer , vol.62 , Issue.8 , pp. 1128-1136
    • Chang, H.1    Yu, B.2    Yu, X.3    Yi, L.4    Chen, C.5    Mi, M.6
  • 7
    • 33744998881 scopus 로고    scopus 로고
    • Casein micelle structure: What can be learned from milk synthesis and structural biology?
    • Farrell, H.M. Jr., Malin, E.L., Brown, E.M., Qi, P.X., Casein micelle structure: What can be learned from milk synthesis and structural biology?. Current Opinion in Colloid & Interface Science 11:2–3 (2006), 135–147.
    • (2006) Current Opinion in Colloid & Interface Science , vol.11 , Issue.2-3 , pp. 135-147
    • Farrell, H.M.1    Malin, E.L.2    Brown, E.M.3    Qi, P.X.4
  • 9
    • 80052807887 scopus 로고    scopus 로고
    • Investigation into the interaction between resveratrol and whey proteins using fluorescence spectroscopy
    • Hemar, Y., Gerbeaud, M., Oliver, C.M., Augustin, M.A., Investigation into the interaction between resveratrol and whey proteins using fluorescence spectroscopy. International Journal of Food Science & Technology 46:10 (2011), 2137–2144.
    • (2011) International Journal of Food Science & Technology , vol.46 , Issue.10 , pp. 2137-2144
    • Hemar, Y.1    Gerbeaud, M.2    Oliver, C.M.3    Augustin, M.A.4
  • 10
    • 33745753267 scopus 로고    scopus 로고
    • Noncovalent cross-linking of casein by epigallocatechin gallate characterized by single molecule force microscopy
    • Jöbstl, E., Howse, J.R., Fairclough, J.P.A., Williamson, M.P., Noncovalent cross-linking of casein by epigallocatechin gallate characterized by single molecule force microscopy. Journal of Agricultural and Food Chemistry 54:12 (2006), 4077–4081.
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , Issue.12 , pp. 4077-4081
    • Jöbstl, E.1    Howse, J.R.2    Fairclough, J.P.A.3    Williamson, M.P.4
  • 15
    • 4243120936 scopus 로고    scopus 로고
    • Invited review: β-Lactoglobulin: Binding properties, structure, and function
    • Kontopidis, G., Holt, C., Sawyer, L., Invited review: β-Lactoglobulin: Binding properties, structure, and function. Journal of Dairy Science 87:4 (2004), 785–796.
    • (2004) Journal of Dairy Science , vol.87 , Issue.4 , pp. 785-796
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 16
    • 0027586726 scopus 로고
    • Three-dimensional molecular modeling of bovine caseins – A refined, energy-minimized beta-casein structure
    • Kumosinski, T., Brown, E., Farrell, H. Jr., Three-dimensional molecular modeling of bovine caseins – A refined, energy-minimized beta-casein structure. Journal of Dairy Science 73 (1993), 931–945.
    • (1993) Journal of Dairy Science , vol.73 , pp. 931-945
    • Kumosinski, T.1    Brown, E.2    Farrell, H.3
  • 17
    • 0004040064 scopus 로고    scopus 로고
    • Principles of fluorescence spectroscopy
    • 2nd ed. Kluwer Academic/Plenum Publishers New York, NY
    • Lakowicz, J., Principles of fluorescence spectroscopy. 2nd ed., 1999, Kluwer Academic/Plenum Publishers, New York, NY.
    • (1999)
    • Lakowicz, J.1
  • 18
    • 77953865084 scopus 로고    scopus 로고
    • Principles of fluorescence spectroscopy
    • 3rd ed. Springer New York, NY (Chapter 16)
    • Lakowicz, J., Principles of fluorescence spectroscopy. 3rd ed., 2006, Springer, New York, NY (Chapter 16).
    • (2006)
    • Lakowicz, J.1
  • 19
    • 0015895751 scopus 로고
    • Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale
    • Lakowicz, J., Weber, G., Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry 12:21 (1973), 4171–4179.
    • (1973) Biochemistry , vol.12 , Issue.21 , pp. 4171-4179
    • Lakowicz, J.1    Weber, G.2
  • 20
    • 38849129380 scopus 로고    scopus 로고
    • Interaction of β-lactoglobulin with resveratrol and its biological implications
    • Liang, L., Tajmir-Riahi, H.A., Subirade, M., Interaction of β-lactoglobulin with resveratrol and its biological implications. Biomacromolecules 9:1 (2008), 50–56.
    • (2008) Biomacromolecules , vol.9 , Issue.1 , pp. 50-56
    • Liang, L.1    Tajmir-Riahi, H.A.2    Subirade, M.3
  • 22
    • 0036836538 scopus 로고    scopus 로고
    • Structural parameterization of the binding enthalpy of small ligands
    • Luque, I., Freire, E., Structural parameterization of the binding enthalpy of small ligands. PROTEINS: Structure Function, and Genetics 49 (2002), 181–190.
    • (2002) PROTEINS: Structure Function, and Genetics , vol.49 , pp. 181-190
    • Luque, I.1    Freire, E.2
  • 24
    • 0348078399 scopus 로고    scopus 로고
    • A thermodynamic study of azide binding to myoglobin
    • Marcoline, A.T., Elgren, T.E., A thermodynamic study of azide binding to myoglobin. Journal of Chemical Education, 75(12), 1998, 1622.
    • (1998) Journal of Chemical Education , vol.75 , Issue.12 , pp. 1622
    • Marcoline, A.T.1    Elgren, T.E.2
  • 25
    • 0027347215 scopus 로고
    • Whey-protein concentrates and isolates – Processing and functional-properties
    • Morr, C.V., Ha, E.Y.W., Whey-protein concentrates and isolates – Processing and functional-properties. Critical Reviews in Food Science and Nutrition 33:6 (1993), 431–476.
    • (1993) Critical Reviews in Food Science and Nutrition , vol.33 , Issue.6 , pp. 431-476
    • Morr, C.V.1    Ha, E.Y.W.2
  • 26
    • 84855409117 scopus 로고    scopus 로고
    • Influence of formulation and processing on absorption and metabolism of flavan-3-ols from tea and cocoa
    • Neilson, A.P., Ferruzzi, M.G., Influence of formulation and processing on absorption and metabolism of flavan-3-ols from tea and cocoa. Annual Review of Food Science and Technology 2 (2011), 125–151.
    • (2011) Annual Review of Food Science and Technology , vol.2 , pp. 125-151
    • Neilson, A.P.1    Ferruzzi, M.G.2
  • 27
    • 11244303574 scopus 로고    scopus 로고
    • Interaction of flavonoids with bovine serum albumin: A fluorescence quenching study
    • Papadopoulou, A., Green, R.J., Frazier, R.A., Interaction of flavonoids with bovine serum albumin: A fluorescence quenching study. Journal of Agricultural and Food Chemistry 53:1 (2005), 158–163.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.1 , pp. 158-163
    • Papadopoulou, A.1    Green, R.J.2    Frazier, R.A.3
  • 30
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: forces contributing to stability
    • Ross, P.D., Subramanian, S., Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20:11 (1981), 3096–3102.
    • (1981) Biochemistry , vol.20 , Issue.11 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 31
    • 84857648468 scopus 로고    scopus 로고
    • Evaluation of the effects of anthocyanins in type 2 diabetes
    • Sancho, R.A.S., Pastore, G.M., Evaluation of the effects of anthocyanins in type 2 diabetes. Food Research International 46:1 (2012), 378–386.
    • (2012) Food Research International , vol.46 , Issue.1 , pp. 378-386
    • Sancho, R.A.S.1    Pastore, G.M.2
  • 32
    • 84915813866 scopus 로고    scopus 로고
    • Biophysical studies of interaction between hydrolysable tannins isolated from Oenothera gigas and Geranium sanguineum with human serum albumin
    • Sekowski, S., Ionov, M., Kaszuba, M., Mavlyanov, S., Bryszewska, M., Zamaraeva, M., Biophysical studies of interaction between hydrolysable tannins isolated from Oenothera gigas and Geranium sanguineum with human serum albumin. Colloids and Surfaces B: Biointerfaces 123 (2014), 623–628.
    • (2014) Colloids and Surfaces B: Biointerfaces , vol.123 , pp. 623-628
    • Sekowski, S.1    Ionov, M.2    Kaszuba, M.3    Mavlyanov, S.4    Bryszewska, M.5    Zamaraeva, M.6
  • 33
    • 84946922971 scopus 로고    scopus 로고
    • A note on the use of steady-state fluorescence quenching to quantify nanoparticle-protein interactions
    • Sousa, A.A., A note on the use of steady-state fluorescence quenching to quantify nanoparticle-protein interactions. Journal of Fluorescence 25:6 (2015), 1567–1575.
    • (2015) Journal of Fluorescence , vol.25 , Issue.6 , pp. 1567-1575
    • Sousa, A.A.1
  • 34
    • 79959690715 scopus 로고    scopus 로고
    • Fluorescence quenching and ligand binding: A critical discussion of a popular methodology
    • van de Weert, M., Stella, L., Fluorescence quenching and ligand binding: A critical discussion of a popular methodology. Journal of Molecular Structure 998:1–3 (2011), 144–150.
    • (2011) Journal of Molecular Structure , vol.998 , Issue.1-3 , pp. 144-150
    • van de Weert, M.1    Stella, L.2
  • 35
    • 0003913658 scopus 로고
    • Dairy chemistry and physics
    • John Wiley & Sons New York, NY
    • Walstra, P., Jenness, R., Dairy chemistry and physics. 1984, John Wiley & Sons, New York, NY.
    • (1984)
    • Walstra, P.1    Jenness, R.2
  • 37
    • 46149098431 scopus 로고    scopus 로고
    • Probing the interaction of trans-resveratrol with bovine serum albumin: A fluorescence quenching study with tachiya model
    • Xiao, J.B., Chen, X.Q., Jiang, X.Y., Hilczer, M., Tachiya, M., Probing the interaction of trans-resveratrol with bovine serum albumin: A fluorescence quenching study with tachiya model. Journal of Fluorescence 18:3–4 (2008), 671–678.
    • (2008) Journal of Fluorescence , vol.18 , Issue.3-4 , pp. 671-678
    • Xiao, J.B.1    Chen, X.Q.2    Jiang, X.Y.3    Hilczer, M.4    Tachiya, M.5
  • 38
    • 60849118125 scopus 로고    scopus 로고
    • Effects of casein, ovalbumin, and dextran on the astringency of tea polyphenols determined by quartz crystal microbalance with dissipation
    • Yan, Y., Hu, J., Yao, P., Effects of casein, ovalbumin, and dextran on the astringency of tea polyphenols determined by quartz crystal microbalance with dissipation. Langmuir 25 (2009), 397–402.
    • (2009) Langmuir , vol.25 , pp. 397-402
    • Yan, Y.1    Hu, J.2    Yao, P.3
  • 39
    • 78751616461 scopus 로고    scopus 로고
    • Food matrix affecting anthocyanin bioavailability: Review
    • Yang, M., Koo, S.I., Song, W.O., Chun, O.K., Food matrix affecting anthocyanin bioavailability: Review. Current Medicinal Chemistry 18:2 (2011), 291–300.
    • (2011) Current Medicinal Chemistry , vol.18 , Issue.2 , pp. 291-300
    • Yang, M.1    Koo, S.I.2    Song, W.O.3    Chun, O.K.4
  • 40
    • 80054991125 scopus 로고    scopus 로고
    • Interaction of epigallocatechin-3-gallate with β-lactoglobulin: molecular characterization and biological implication
    • Zorilla, R., Liang, L., Remondetto, G., Subirade, M., Interaction of epigallocatechin-3-gallate with β-lactoglobulin: molecular characterization and biological implication. Dairy Science & Technology 91:5 (2011), 629–644.
    • (2011) Dairy Science & Technology , vol.91 , Issue.5 , pp. 629-644
    • Zorilla, R.1    Liang, L.2    Remondetto, G.3    Subirade, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.