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Volumn 139, Issue 1-4, 2013, Pages 611-616

Probing the binding between norbixin and dairy proteins by spectroscopy methods

Author keywords

Casein; Circular dichroism spectroscopy; Fluorescence quenching; FTIR; Norbixin; Whey protein

Indexed keywords

BINDING AFFINITIES; BOVINE SERUM ALBUMINS; FLUORESCENCE QUENCHING; FTIR; INDIVIDUAL PROTEINS; NORBIXIN; WHEY PROTEIN ISOLATE; WHEY PROTEINS;

EID: 84875943100     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2013.01.073     Document Type: Article
Times cited : (70)

References (38)
  • 3
    • 77950502396 scopus 로고    scopus 로고
    • Effect of premeal consumption of whey protein and its hydrolysate on food intake and postmeal glycemia and insulin responses in young adults
    • T. Akhavan, B.L. Luhovyy, P.H. Brown, C.E. Cho, and G.H. Anderson Effect of premeal consumption of whey protein and its hydrolysate on food intake and postmeal glycemia and insulin responses in young adults American Journal of Clinical Nutrition 91 4 2010 966 975
    • (2010) American Journal of Clinical Nutrition , vol.91 , Issue.4 , pp. 966-975
    • Akhavan, T.1    Luhovyy, B.L.2    Brown, P.H.3    Cho, C.E.4    Anderson, G.H.5
  • 4
    • 0037933420 scopus 로고    scopus 로고
    • Biosynthesis of the food and cosmetic plant pigment bixin (annatto)
    • F. Bouvier, O. Dogbo, and B. Camara Biosynthesis of the food and cosmetic plant pigment bixin (annatto) Science 300 5628 2003 2089 2091
    • (2003) Science , vol.300 , Issue.5628 , pp. 2089-2091
    • Bouvier, F.1    Dogbo, O.2    Camara, B.3
  • 6
    • 78049290463 scopus 로고    scopus 로고
    • Zinc-induced precipitation of milk fat globule membranes: A simple method for the preparation of fat-free whey protein isolate
    • S. Damodaran Zinc-induced precipitation of milk fat globule membranes: A simple method for the preparation of fat-free whey protein isolate Journal of Agricultural and Food Chemistry 58 20 2010 11052 11057
    • (2010) Journal of Agricultural and Food Chemistry , vol.58 , Issue.20 , pp. 11052-11057
    • Damodaran, S.1
  • 8
    • 0032867556 scopus 로고    scopus 로고
    • The three recombinant domains of human serum albumin-Structural characterization and ligand binding properties
    • M. Dockal, D.C. Carter, and F. Ruker The three recombinant domains of human serum albumin-Structural characterization and ligand binding properties Journal of Biological Chemistry 274 41 1999 29303 29310
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.41 , pp. 29303-29310
    • Dockal, M.1    Carter, D.C.2    Ruker, F.3
  • 9
    • 0035177887 scopus 로고    scopus 로고
    • Secondary structural studies of bovine caseins: Temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization
    • H.M. Farrell Jr., E.D. Wickham, J.J. Unruh, P.X. Qi, and P.D. Hoagland Secondary structural studies of bovine caseins: Temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization Food Hydrocolloids 15 4-6 2001 341 354
    • (2001) Food Hydrocolloids , vol.15 , Issue.46 , pp. 341-354
    • Farrell, Jr.H.M.1    Wickham, E.D.2    Unruh, J.J.3    Qi, P.X.4    Hoagland, P.D.5
  • 12
    • 44849107381 scopus 로고    scopus 로고
    • Characterisation of sodium caseinate as a function of ionic strength, pH and temperature using static and dynamic light scattering
    • A. HadjSadok, A. Pitkowski, T. Nicolai, L. Benyahia, and N. Moulai-Mostefa Characterisation of sodium caseinate as a function of ionic strength, pH and temperature using static and dynamic light scattering Food Hydrocolloids 22 8 2008 1460 1466
    • (2008) Food Hydrocolloids , vol.22 , Issue.8 , pp. 1460-1466
    • Hadjsadok, A.1    Pitkowski, A.2    Nicolai, T.3    Benyahia, L.4    Moulai-Mostefa, N.5
  • 13
    • 42049108379 scopus 로고    scopus 로고
    • Characterization of protein capacity of nanocation exchanger particles as filling material for functional magnetic beads for bioseparation purposes
    • B. Hickstein, and U.A. Peuker Characterization of protein capacity of nanocation exchanger particles as filling material for functional magnetic beads for bioseparation purposes Biotechnology Progress 24 2 2008 409 416
    • (2008) Biotechnology Progress , vol.24 , Issue.2 , pp. 409-416
    • Hickstein, B.1    Peuker, U.A.2
  • 17
    • 0032483094 scopus 로고    scopus 로고
    • Retinol and retinoic acid bind to a surface cleft in bovine beta-lactoglobulin: A method of binding site determination using fluorescence resonance energy transfer
    • D.C. Lange, R. Kothari, R.C. Patel, and S.C. Patel Retinol and retinoic acid bind to a surface cleft in bovine beta-lactoglobulin: A method of binding site determination using fluorescence resonance energy transfer Biophysical Chemistry 74 1 1998 45 51
    • (1998) Biophysical Chemistry , vol.74 , Issue.1 , pp. 45-51
    • Lange, D.C.1    Kothari, R.2    Patel, R.C.3    Patel, S.C.4
  • 18
    • 38049085214 scopus 로고    scopus 로고
    • Changes and roles of secondary structures of whey protein for the formation of protein membrane at soy oil/water interface under high-pressure homogenization
    • S.-H. Lee, T. Lefèvre, M. Subirade, and P. Paquin Changes and roles of secondary structures of whey protein for the formation of protein membrane at soy oil/water interface under high-pressure homogenization Journal of Agricultural and Food Chemistry 55 26 2007 10924 10931
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.26 , pp. 10924-10931
    • Lee, S.-H.1    Lefèvre, T.2    Subirade, M.3    Paquin, P.4
  • 20
    • 0001542122 scopus 로고
    • Disulfide bond formation affects stability of whey protein isolate emulsions
    • D.J. McClements, F.J. Monahan, and J.E. Kinsella Disulfide bond formation affects stability of whey protein isolate emulsions Journal of Food Science 58 5 1993 1036 1039
    • (1993) Journal of Food Science , vol.58 , Issue.5 , pp. 1036-1039
    • McClements, D.J.1    Monahan, F.J.2    Kinsella, J.E.3
  • 21
    • 0038737944 scopus 로고    scopus 로고
    • Thermodynamics of micellization of bovine beta-casein studied by high-sensitivity differential scanning calorimetry
    • L.M. Mikheeva, N.V. Grinberg, V.Y. Grinberg, A.R. Khokhlov, and C.G. de Kruif Thermodynamics of micellization of bovine beta-casein studied by high-sensitivity differential scanning calorimetry Langmuir 19 7 2003 2913 2921
    • (2003) Langmuir , vol.19 , Issue.7 , pp. 2913-2921
    • Mikheeva, L.M.1    Grinberg, N.V.2    Grinberg, V.Y.3    Khokhlov, A.R.4    De Kruif, C.G.5
  • 22
    • 0033930449 scopus 로고    scopus 로고
    • Purification of glycomacropeptide from dialyzed and non-dialyzed sweet whey by anion-exchange chromatography at different pH values
    • T. Nakano, and L. Ozimek Purification of glycomacropeptide from dialyzed and non-dialyzed sweet whey by anion-exchange chromatography at different pH values Biotechnology Letters 22 13 2000 1081 1086
    • (2000) Biotechnology Letters , vol.22 , Issue.13 , pp. 1081-1086
    • Nakano, T.1    Ozimek, L.2
  • 23
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • J.T. Pelton, and L.R. McLean Spectroscopic methods for analysis of protein secondary structure Analytical Biochemistry 277 2 2000 167 176
    • (2000) Analytical Biochemistry , vol.277 , Issue.2 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 24
    • 0015377367 scopus 로고
    • Fluorescence of N′-formylkynurenine and of proteins exposed to sunlight
    • A. Pirie Fluorescence of N′-formylkynurenine and of proteins exposed to sunlight Biochemical Journal 128 5 1972 1365
    • (1972) Biochemical Journal , vol.128 , Issue.5 , pp. 1365
    • Pirie, A.1
  • 25
    • 84916555996 scopus 로고
    • Effect of binding of retinol and palmitic acid to bovine β-lactoglobulin on its resistance to thermal denaturation
    • P. Puyol, M.D. Perez, J.M. Peiro, and M. Calvo Effect of binding of retinol and palmitic acid to bovine β-lactoglobulin on its resistance to thermal denaturation Journal of Dairy Science 77 6 1994 1494 1502
    • (1994) Journal of Dairy Science , vol.77 , Issue.6 , pp. 1494-1502
    • Puyol, P.1    Perez, M.D.2    Peiro, J.M.3    Calvo, M.4
  • 26
    • 36348949020 scopus 로고    scopus 로고
    • Interaction of rofecoxib with human serum albumin: Determination of binding constants and the binding site by spectroscopic methods
    • Z.D. Qi, B. Zhou, Q. Xiao, C. Shi, Y. Liu, and J. Dai Interaction of rofecoxib with human serum albumin: Determination of binding constants and the binding site by spectroscopic methods Journal of Photochemistry and Photobiology A: Chemistry 193 2-3 2008 81 88
    • (2008) Journal of Photochemistry and Photobiology A: Chemistry , vol.193 , Issue.23 , pp. 81-88
    • Qi, Z.D.1    Zhou, B.2    Xiao, Q.3    Shi, C.4    Liu, Y.5    Dai, J.6
  • 27
    • 0020595601 scopus 로고
    • Peptide-substrates for chymosin(rennin): Conformational studies of kappa-casein and some kappa-casein-related oligopeptides by circular-dichroism and secondary structure prediction
    • J. Raap, K.E.T. Kerling, H.J. Vreeman, and S. Visser Peptide-substrates for chymosin(rennin): Conformational studies of kappa-casein and some kappa-casein-related oligopeptides by circular-dichroism and secondary structure prediction Archives of Biochemistry and Biophysics 221 1 1983 117 124
    • (1983) Archives of Biochemistry and Biophysics , vol.221 , Issue.1 , pp. 117-124
    • Raap, J.1    Kerling, K.E.T.2    Vreeman, H.J.3    Visser, S.4
  • 28
    • 84856220538 scopus 로고    scopus 로고
    • Heating of milk alters the binding of curcumin to casein micelles. A fluorescence spectroscopy study
    • S. Rahimi Yazdi, and M. Corredig Heating of milk alters the binding of curcumin to casein micelles. A fluorescence spectroscopy study Food Chemistry 132 3 2012 1143 1149
    • (2012) Food Chemistry , vol.132 , Issue.3 , pp. 1143-1149
    • Rahimi Yazdi, S.1    Corredig, M.2
  • 29
    • 0036768548 scopus 로고    scopus 로고
    • Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid
    • H.M. Rawel, S. Rohn, H.-P. Kruse, and J. Kroll Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid Food Chemistry 78 4 2002 443 455
    • (2002) Food Chemistry , vol.78 , Issue.4 , pp. 443-455
    • Rawel, H.M.1    Rohn, S.2    Kruse, H.-P.3    Kroll, J.4
  • 31
    • 0030199270 scopus 로고    scopus 로고
    • The biotechnological utilization of cheese whey: A review
    • M.I.G. Siso The biotechnological utilization of cheese whey: A review Bioresource Technology 57 1 1996 1 11
    • (1996) Bioresource Technology , vol.57 , Issue.1 , pp. 1-11
    • Siso, M.I.G.1
  • 32
    • 2442637545 scopus 로고    scopus 로고
    • A biological perspective on the structure and function of caseins and casein micelles
    • E. Smyth, R.A. Clegg, and C. Holt A biological perspective on the structure and function of caseins and casein micelles International Journal of Dairy Technology 57 2-3 2004 121 126
    • (2004) International Journal of Dairy Technology , vol.57 , Issue.23 , pp. 121-126
    • Smyth, E.1    Clegg, R.A.2    Holt, C.3
  • 33
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • N. Sreerama, and R.W. Woody Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set Analytical Biochemistry 287 2 2000 252 260
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 34
    • 54049105710 scopus 로고    scopus 로고
    • Effect of minor milk proteins in chymosin separated whey and casein fractions on cheese yield as determined by proteomics and multivariate data analysis
    • A. Wedholm, H.S. Møller, A. Stensballe, H. Lindmark-Månsson, A.H. Karlsson, and R. Andersson Effect of minor milk proteins in chymosin separated whey and casein fractions on cheese yield as determined by proteomics and multivariate data analysis Journal of Dairy Science 91 10 2008 3787 3797
    • (2008) Journal of Dairy Science , vol.91 , Issue.10 , pp. 3787-3797
    • Wedholm, A.1    Møller, H.S.2    Stensballe, A.3    Lindmark-Månsson, H.4    Karlsson, A.H.5    Andersson, R.6
  • 36
    • 0033833408 scopus 로고    scopus 로고
    • Apple pectin complexes with whey protein isolate
    • H. Zaleska, S.G. Ring, and P. Tomasik Apple pectin complexes with whey protein isolate Food Hydrocolloids 14 4 2000 377 382
    • (2000) Food Hydrocolloids , vol.14 , Issue.4 , pp. 377-382
    • Zaleska, H.1    Ring, S.G.2    Tomasik, P.3
  • 37
    • 84863131920 scopus 로고    scopus 로고
    • Binding between Bixin and whey protein at pH 7.4 studied by spectroscopy and isothermal titration calorimetry
    • Y. Zhang, and Q.X. Zhong Binding between Bixin and whey protein at pH 7.4 studied by spectroscopy and isothermal titration calorimetry Journal of Agricultural and Food Chemistry 60 7 2012 1880 1886
    • (2012) Journal of Agricultural and Food Chemistry , vol.60 , Issue.7 , pp. 1880-1886
    • Zhang, Y.1    Zhong, Q.X.2
  • 38
    • 30544433324 scopus 로고    scopus 로고
    • Binding of the pepper alkaloid piperine to bovine β-lactoglobulin: Circular dichroism spectroscopy and molecular modeling study
    • F. Zsila, E. Hazai, and L. Sawyer Binding of the pepper alkaloid piperine to bovine β-lactoglobulin: Circular dichroism spectroscopy and molecular modeling study Journal of Agricultural and Food Chemistry 53 26 2005 10179 10185
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.26 , pp. 10179-10185
    • Zsila, F.1    Hazai, E.2    Sawyer, L.3


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