메뉴 건너뛰기




Volumn , Issue , 2019, Pages 537-571

Interaction between milk proteins and micronutrients

Author keywords

Casein; Fatty acid; Food processing; Micronutrient; Milk protein; Mineral; Sugar; Surfactant; Vitamin; Lactoglobulin

Indexed keywords


EID: 85094126840     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-815251-5.00014-1     Document Type: Chapter
Times cited : (12)

References (252)
  • 1
    • 0035012945 scopus 로고    scopus 로고
    • Influence of sugars on high-pressure induced gelation of skim milk dispersions
    • Abbasi S., Dickinson E. Influence of sugars on high-pressure induced gelation of skim milk dispersions. Food Hydrocoll. 2001, 15:315-319.
    • (2001) Food Hydrocoll. , vol.15 , pp. 315-319
    • Abbasi, S.1    Dickinson, E.2
  • 2
    • 0346741245 scopus 로고    scopus 로고
    • Influence of high-pressure treatment on gelation of skim milk powder+low methoxyl pectin dispersions
    • Abbasi S., Dickinson E. Influence of high-pressure treatment on gelation of skim milk powder+low methoxyl pectin dispersions. High Pressure Res. 2002, 22:643-647.
    • (2002) High Pressure Res. , vol.22 , pp. 643-647
    • Abbasi, S.1    Dickinson, E.2
  • 3
    • 84855496627 scopus 로고    scopus 로고
    • Formation and potential uses of milk proteins as nano delivery vehicles for nutraceuticals: a review
    • Abd El-Salam M.H., El-Shibiny S. Formation and potential uses of milk proteins as nano delivery vehicles for nutraceuticals: a review. Int. J. Dairy Technol. 2012, 65:13-21.
    • (2012) Int. J. Dairy Technol. , vol.65 , pp. 13-21
    • Abd El-Salam, M.H.1    El-Shibiny, S.2
  • 4
    • 85094124335 scopus 로고
    • Effect of milk-proteins on retinol efficiency
    • Adrian J., Frangne R., Rabache M. Effect of milk-proteins on retinol efficiency. Sci. Aliment. 1984, 4:305-308.
    • (1984) Sci. Aliment. , vol.4 , pp. 305-308
    • Adrian, J.1    Frangne, R.2    Rabache, M.3
  • 7
    • 85055326232 scopus 로고    scopus 로고
    • Binding of beta-carotene to whey proteins: multi-spectroscopic techniques and docking studies
    • Allahdad Z., Varidi M., Zadmard R., Saboury A.A., Haertle T. Binding of beta-carotene to whey proteins: multi-spectroscopic techniques and docking studies. Food Chem. 2019, 277:96-106.
    • (2019) Food Chem. , vol.277 , pp. 96-106
    • Allahdad, Z.1    Varidi, M.2    Zadmard, R.3    Saboury, A.A.4    Haertle, T.5
  • 8
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8Å resolution
    • Anderson B.F., Baker H.M., Norris G.E., Rice D.W., Baker E.N. Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8Å resolution. J. Mol. Biol. 1989, 209:711-734.
    • (1989) J. Mol. Biol. , vol.209 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 9
    • 0015138397 scopus 로고
    • The use of trinitrobenzenesulfonic acid in studies on the binding of fatty acid anions to bovine serum albumin
    • Andersson L.O., Brandt J., Johansson S. The use of trinitrobenzenesulfonic acid in studies on the binding of fatty acid anions to bovine serum albumin. Arch. Biochem. Biophys. 1971, 146:428-440.
    • (1971) Arch. Biochem. Biophys. , vol.146 , pp. 428-440
    • Andersson, L.O.1    Brandt, J.2    Johansson, S.3
  • 10
    • 0024342795 scopus 로고
    • Interaction of rat α-fetoprotein and albumin with polyunsaturated and other fatty acids: determination of apparent association constants
    • Anel A., Calvo M., Naval J., Iturralde M., Alava M.A., Pineiro A. Interaction of rat α-fetoprotein and albumin with polyunsaturated and other fatty acids: determination of apparent association constants. FEBS Lett. 1989, 250:22-24.
    • (1989) FEBS Lett. , vol.250 , pp. 22-24
    • Anel, A.1    Calvo, M.2    Naval, J.3    Iturralde, M.4    Alava, M.A.5    Pineiro, A.6
  • 11
    • 78249288128 scopus 로고    scopus 로고
    • Instability of pressure-treated reconstituted skim milk to acidification
    • Anema S.G. Instability of pressure-treated reconstituted skim milk to acidification. Food Biophys. 2010, 5:321-329.
    • (2010) Food Biophys. , vol.5 , pp. 321-329
    • Anema, S.G.1
  • 12
    • 84863431263 scopus 로고    scopus 로고
    • Pressure-induced denaturation of β-lactoglobulin in skim milk: effect of milk concentration
    • Anema S.G. Pressure-induced denaturation of β-lactoglobulin in skim milk: effect of milk concentration. J. Agric. Food Chem. 2012, 60:6565-6570.
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 6565-6570
    • Anema, S.G.1
  • 13
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa T., Timasheff S.N. Stabilization of protein structure by sugars. Biochemistry 1982, 21:6536-6544.
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 14
    • 84977274027 scopus 로고    scopus 로고
    • Characterization of flavonoid-protein interactions using fluorescence spectroscopy: binding of pelargonidin to dairy proteins
    • Arroyo-Maya I.J., Campos-Terán J., Hernández-Arana A., McClements D.J. Characterization of flavonoid-protein interactions using fluorescence spectroscopy: binding of pelargonidin to dairy proteins. Food Chem. 2016, 213:431-439.
    • (2016) Food Chem. , vol.213 , pp. 431-439
    • Arroyo-Maya, I.J.1    Campos-Terán, J.2    Hernández-Arana, A.3    McClements, D.J.4
  • 15
    • 0030272655 scopus 로고    scopus 로고
    • The effect of temperature and ionic strength on the dimerization of β-lactoglobulin
    • Aymard P., Durand D., Nicolai T. The effect of temperature and ionic strength on the dimerization of β-lactoglobulin. Int. J. Biol. Macromol. 1996, 19:213-221.
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 213-221
    • Aymard, P.1    Durand, D.2    Nicolai, T.3
  • 16
    • 0034849394 scopus 로고    scopus 로고
    • Impact of preferential interactions on thermal stability and gelation of bovine serum albumin in aqueous sucrose solutions
    • Baier S., McClements D.J. Impact of preferential interactions on thermal stability and gelation of bovine serum albumin in aqueous sucrose solutions. J. Agric. Food Chem. 2001, 49:2600-2608.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 2600-2608
    • Baier, S.1    McClements, D.J.2
  • 17
    • 0348226844 scopus 로고    scopus 로고
    • Combined influence of NaCl and sucrose on heat-induced gelation of bovine serum albumin
    • Baier S.K., McClements D.J. Combined influence of NaCl and sucrose on heat-induced gelation of bovine serum albumin. J. Agric. Food Chem. 2003, 51:8107-8112.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 8107-8112
    • Baier, S.K.1    McClements, D.J.2
  • 18
    • 0344444642 scopus 로고    scopus 로고
    • Impact of glycerol on thermostability and heat-induced gelation of bovine serum albumin
    • Baier S.K., Decker E.A., McClements D.J. Impact of glycerol on thermostability and heat-induced gelation of bovine serum albumin. Food Hydrocoll. 2004, 18:91-100.
    • (2004) Food Hydrocoll. , vol.18 , pp. 91-100
    • Baier, S.K.1    Decker, E.A.2    McClements, D.J.3
  • 20
    • 27444437672 scopus 로고    scopus 로고
    • Interaction of bovine α-lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy
    • Barbana C., Pérez M.D., Sánchez L., Dalgalarrondo M., Chobert J.M., Haertlé T., Calvo M. Interaction of bovine α-lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy. Int. Dairy J. 2006, 16:18-25.
    • (2006) Int. Dairy J. , vol.16 , pp. 18-25
    • Barbana, C.1    Pérez, M.D.2    Sánchez, L.3    Dalgalarrondo, M.4    Chobert, J.M.5    Haertlé, T.6    Calvo, M.7
  • 21
    • 79957931676 scopus 로고    scopus 로고
    • Bound fatty acids modulate the sensitivity of bovine β-lactoglobulin to chemical and physical denaturation
    • Barbiroli A., Bonomi F., Ferranti P., Fessas D., Nasi A., Rasmussen P., Iametti S. Bound fatty acids modulate the sensitivity of bovine β-lactoglobulin to chemical and physical denaturation. J. Agric. Food Chem. 2011, 59:5729-5737.
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 5729-5737
    • Barbiroli, A.1    Bonomi, F.2    Ferranti, P.3    Fessas, D.4    Nasi, A.5    Rasmussen, P.6    Iametti, S.7
  • 22
    • 85018333525 scopus 로고    scopus 로고
    • Stabilization of beta-lactoglobulin by polyols and sugars against temperature-induced denaturation involves diverse and specific structural regions of the protein
    • Barbiroli A., Marengo M., Fessas D., Ragg E., Renzetti S., Bonomi F., Iametti S. Stabilization of beta-lactoglobulin by polyols and sugars against temperature-induced denaturation involves diverse and specific structural regions of the protein. Food Chem. 2017, 234:155-162.
    • (2017) Food Chem. , vol.234 , pp. 155-162
    • Barbiroli, A.1    Marengo, M.2    Fessas, D.3    Ragg, E.4    Renzetti, S.5    Bonomi, F.6    Iametti, S.7
  • 23
    • 78650915626 scopus 로고    scopus 로고
    • Energetics of ligand recognition and self-association of bovine β-lactoglobulin: differences between variants A and B
    • Bello M., Portillo-Téllez M.D.C., García-Hernández E. Energetics of ligand recognition and self-association of bovine β-lactoglobulin: differences between variants A and B. Biochemistry 2011, 50:151-161.
    • (2011) Biochemistry , vol.50 , pp. 151-161
    • Bello, M.1    Portillo-Téllez, M.D.C.2    García-Hernández, E.3
  • 24
    • 84875160537 scopus 로고    scopus 로고
    • Interaction of curcumin with phosphocasein micelles processed or not by dynamic high-pressure
    • Benzaria A., Maresca M., Taieb N., Dumay E. Interaction of curcumin with phosphocasein micelles processed or not by dynamic high-pressure. Food Chem. 2013, 138:2327-2337.
    • (2013) Food Chem. , vol.138 , pp. 2327-2337
    • Benzaria, A.1    Maresca, M.2    Taieb, N.3    Dumay, E.4
  • 25
    • 0022501369 scopus 로고
    • Isolation and characterization of lactoferrin separated from human whey by adsorption chromatography using Cibacron Blue F3G-A linked affinity adsorbent
    • Bezwoda W.R., Mansoor N. Isolation and characterization of lactoferrin separated from human whey by adsorption chromatography using Cibacron Blue F3G-A linked affinity adsorbent. Clin. Chim. Acta 1986, 157:89-93.
    • (1986) Clin. Chim. Acta , vol.157 , pp. 89-93
    • Bezwoda, W.R.1    Mansoor, N.2
  • 26
    • 0035346266 scopus 로고    scopus 로고
    • Interactions of chlorpromazine with milk proteins
    • Bhattacharyya J., Das K.P. Interactions of chlorpromazine with milk proteins. Mol. Cell. Biochem. 2001, 221:11-15.
    • (2001) Mol. Cell. Biochem. , vol.221 , pp. 11-15
    • Bhattacharyya, J.1    Das, K.P.2
  • 28
    • 84855837542 scopus 로고    scopus 로고
    • Locating the binding sites of folic acid with milk α- and β-caseins
    • Bourassa P., Tajmir-Riahi H.A. Locating the binding sites of folic acid with milk α- and β-caseins. J. Phys. Chem. B 2012, 116:513-519.
    • (2012) J. Phys. Chem. B , vol.116 , pp. 513-519
    • Bourassa, P.1    Tajmir-Riahi, H.A.2
  • 29
    • 0033858518 scopus 로고    scopus 로고
    • Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: a differential scanning calorimetric study
    • Boye J.I., Alli I. Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: a differential scanning calorimetric study. Food Res. Int. 2000, 33:673-682.
    • (2000) Food Res. Int. , vol.33 , pp. 673-682
    • Boye, J.I.1    Alli, I.2
  • 30
    • 0000027238 scopus 로고    scopus 로고
    • Interactions involved in the gelation of bovine serum albumin
    • Boye J.I., Alli I., Ismail A.A. Interactions involved in the gelation of bovine serum albumin. J. Agric. Food Chem. 1996, 44:996-1004.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 996-1004
    • Boye, J.I.1    Alli, I.2    Ismail, A.A.3
  • 31
    • 0030088058 scopus 로고    scopus 로고
    • Effects of physicochemical factors on the secondary structure of β-lactoglobulin
    • Boye J.I., Ismail A.A., Alli I. Effects of physicochemical factors on the secondary structure of β-lactoglobulin. J. Dairy Res. 1996, 63:97-109.
    • (1996) J. Dairy Res. , vol.63 , pp. 97-109
    • Boye, J.I.1    Ismail, A.A.2    Alli, I.3
  • 32
    • 0001744217 scopus 로고    scopus 로고
    • Use of differential scanning calorimetry and infrared spectroscopy in the study of thermal and structural stability of α-lactalbumin
    • Boye J.I., Alli I., Ismail A.A. Use of differential scanning calorimetry and infrared spectroscopy in the study of thermal and structural stability of α-lactalbumin. J. Agric. Food Chem. 1997, 45:1116-1125.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1116-1125
    • Boye, J.I.1    Alli, I.2    Ismail, A.A.3
  • 33
    • 79955098484 scopus 로고    scopus 로고
    • Preparation and comparison of cytotoxic complexes formed between oleic acid and either bovine or human α-lactalbumin
    • Brinkmann C.R., Thiel S., Larsen M.K., Petersen T.E., Jensenius J.C., Heegaard C.W. Preparation and comparison of cytotoxic complexes formed between oleic acid and either bovine or human α-lactalbumin. J. Dairy Sci. 2011, 94:2159-2170.
    • (2011) J. Dairy Sci. , vol.94 , pp. 2159-2170
    • Brinkmann, C.R.1    Thiel, S.2    Larsen, M.K.3    Petersen, T.E.4    Jensenius, J.C.5    Heegaard, C.W.6
  • 34
    • 8644272468 scopus 로고    scopus 로고
    • Binding of alkylsulfonate ligands to bovine β-lactoglobulin: effects on protein denaturation by urea
    • Busti P., Scarpeci S., Gatti C.A., Delorenzi N.J. Binding of alkylsulfonate ligands to bovine β-lactoglobulin: effects on protein denaturation by urea. Food Hydrocoll. 2005, 19:249-255.
    • (2005) Food Hydrocoll. , vol.19 , pp. 249-255
    • Busti, P.1    Scarpeci, S.2    Gatti, C.A.3    Delorenzi, N.J.4
  • 35
    • 32544442673 scopus 로고    scopus 로고
    • Binding of alkylsulfonate ligands to bovine β-lactoglobulin: effects on protein thermal unfolding
    • Busti P., Gatti C.A., Delorenzi N.J. Binding of alkylsulfonate ligands to bovine β-lactoglobulin: effects on protein thermal unfolding. Food Res. Int. 2006, 39:503-509.
    • (2006) Food Res. Int. , vol.39 , pp. 503-509
    • Busti, P.1    Gatti, C.A.2    Delorenzi, N.J.3
  • 36
    • 84925203406 scopus 로고    scopus 로고
    • Iron-binding peptides from whey protein hydrolysates: evaluation, isolation and sequencing by LC-MS/MS
    • Caetano-Silva M.E., Bertoldo-Pacheco M.T., Paes-Leme A.F., Netto F.M. Iron-binding peptides from whey protein hydrolysates: evaluation, isolation and sequencing by LC-MS/MS. Food Res. Int. 2015, 71:132-139.
    • (2015) Food Res. Int. , vol.71 , pp. 132-139
    • Caetano-Silva, M.E.1    Bertoldo-Pacheco, M.T.2    Paes-Leme, A.F.3    Netto, F.M.4
  • 37
    • 85063336881 scopus 로고    scopus 로고
    • Elucidating the interaction mechanism of eriocitrin with β-casein by multi-spectroscopic and molecular simulation methods
    • Cao X., He Y., Kong Y., Mei X., Huo Y., He Y., Liu J. Elucidating the interaction mechanism of eriocitrin with β-casein by multi-spectroscopic and molecular simulation methods. Food Hydrocoll. 2019, 94:63-70.
    • (2019) Food Hydrocoll. , vol.94 , pp. 63-70
    • Cao, X.1    He, Y.2    Kong, Y.3    Mei, X.4    Huo, Y.5    He, Y.6    Liu, J.7
  • 39
    • 20644467984 scopus 로고    scopus 로고
    • Ligand-induced thermostability in proteins: thermodynamic analysis of ANS-albumin interaction
    • Celej M.S., Dassie S.A., Freire E., Bianconi M.L., Fidelio G.D. Ligand-induced thermostability in proteins: thermodynamic analysis of ANS-albumin interaction. Biochim. Biophys. Acta 2005, 1750:122-133.
    • (2005) Biochim. Biophys. Acta , vol.1750 , pp. 122-133
    • Celej, M.S.1    Dassie, S.A.2    Freire, E.3    Bianconi, M.L.4    Fidelio, G.D.5
  • 40
    • 34548611067 scopus 로고    scopus 로고
    • Inhibition of droplet flocculation in globular-protein stabilized oil-in-water emulsions by polyols
    • Chanasattru W., Decker E.A., McClements D.J. Inhibition of droplet flocculation in globular-protein stabilized oil-in-water emulsions by polyols. Food Res. Int. 2007, 40:1161-1169.
    • (2007) Food Res. Int. , vol.40 , pp. 1161-1169
    • Chanasattru, W.1    Decker, E.A.2    McClements, D.J.3
  • 41
    • 33846981881 scopus 로고    scopus 로고
    • Modulation of thermal stability and heat-induced gelation of beta-lactoglobulin by high glycerol and sorbitol levels
    • Chanasattru W., Decker E.A., McClements D.J. Modulation of thermal stability and heat-induced gelation of beta-lactoglobulin by high glycerol and sorbitol levels. Food Chem. 2007, 103:512-520.
    • (2007) Food Chem. , vol.103 , pp. 512-520
    • Chanasattru, W.1    Decker, E.A.2    McClements, D.J.3
  • 42
    • 34547681496 scopus 로고    scopus 로고
    • Physicochemical basis for cosolvent modulation of beta-lactoglobulin functionality: interfacial tension study
    • Chanasattru W., Decker E.A., McClements D.J. Physicochemical basis for cosolvent modulation of beta-lactoglobulin functionality: interfacial tension study. Food Res. Int. 2007, 40:1098-1105.
    • (2007) Food Res. Int. , vol.40 , pp. 1098-1105
    • Chanasattru, W.1    Decker, E.A.2    McClements, D.J.3
  • 43
    • 44649112351 scopus 로고    scopus 로고
    • Impact of cosolvents (polyols) on globular protein functionality: ultrasonic velocity, density, surface tension and solubility study
    • Chanasattru W., Decker E.A., McClements D.J. Impact of cosolvents (polyols) on globular protein functionality: ultrasonic velocity, density, surface tension and solubility study. Food Hydrocoll. 2008, 22:1475-1484.
    • (2008) Food Hydrocoll. , vol.22 , pp. 1475-1484
    • Chanasattru, W.1    Decker, E.A.2    McClements, D.J.3
  • 45
    • 0002142681 scopus 로고    scopus 로고
    • Interaction of β-lactoglobulin with flavour compounds
    • Royal Society of Chemistry, Cambridge, UK, A.J. Taylor, D.S. Mottram (Eds.)
    • Charles M., Bernal B., Guichard E. Interaction of β-lactoglobulin with flavour compounds. Flavour Science: Recent Developments 1996, 433-436. Royal Society of Chemistry, Cambridge, UK. A.J. Taylor, D.S. Mottram (Eds.).
    • (1996) Flavour Science: Recent Developments , pp. 433-436
    • Charles, M.1    Bernal, B.2    Guichard, E.3
  • 46
    • 85014565840 scopus 로고    scopus 로고
    • Structural stability of β-lactoglobulin in the presence of cetylpyridinum bromide: spectroscopic and molecular docking studies
    • Chavoshpour-Natanzi Z., Sahihi M., Gharaghani S. Structural stability of β-lactoglobulin in the presence of cetylpyridinum bromide: spectroscopic and molecular docking studies. J. Biomol. Struct. Dyn. 2018, 36:753-760.
    • (2018) J. Biomol. Struct. Dyn. , vol.36 , pp. 753-760
    • Chavoshpour-Natanzi, Z.1    Sahihi, M.2    Gharaghani, S.3
  • 47
    • 85026359748 scopus 로고    scopus 로고
    • Spectrofluorimetric and molecular docking studies on the interaction of cyanidin-3-O-glucoside with whey protein, β-lactoglobulin
    • Cheng J., Liu J.-H., Prasanna G., Jing P. Spectrofluorimetric and molecular docking studies on the interaction of cyanidin-3-O-glucoside with whey protein, β-lactoglobulin. Int. J. Biol. Macromol. 2017, 105:965-972.
    • (2017) Int. J. Biol. Macromol. , vol.105 , pp. 965-972
    • Cheng, J.1    Liu, J.-H.2    Prasanna, G.3    Jing, P.4
  • 48
    • 85046019144 scopus 로고    scopus 로고
    • Complexation of trans- and cis-resveratrol with bovine serum albumin, β-lactoglobulin or α-lactalbumin
    • Cheng H., Fang Z., Wusigale, Bakry A.M., Chen Y., Liang L. Complexation of trans- and cis-resveratrol with bovine serum albumin, β-lactoglobulin or α-lactalbumin. Food Hydrocoll. 2018, 81:242-252.
    • (2018) Food Hydrocoll. , vol.81 , pp. 242-252
    • Cheng, H.1    Fang, Z.2    Wusigale, B.A.M.3    Chen, Y.4    Liang, L.5
  • 49
    • 0028246854 scopus 로고
    • Probing the retinol-binding site of bovine β-lactoglobulin
    • Cho Y.J., Batt C.A., Sawyer L. Probing the retinol-binding site of bovine β-lactoglobulin. J. Biol. Chem. 1994, 269:11102-11107.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11102-11107
    • Cho, Y.J.1    Batt, C.A.2    Sawyer, L.3
  • 50
    • 85025568813 scopus 로고
    • The interaction of sucrose esters with β-lactoglobulin and β-casein from bovine-milk
    • Clark D.C., Wilde P.J., Wilson D.R., Wustneck R. The interaction of sucrose esters with β-lactoglobulin and β-casein from bovine-milk. Food Hydrocoll. 1992, 6:173-186.
    • (1992) Food Hydrocoll. , vol.6 , pp. 173-186
    • Clark, D.C.1    Wilde, P.J.2    Wilson, D.R.3    Wustneck, R.4
  • 51
    • 17144407576 scopus 로고    scopus 로고
    • Influence of binding of sodium dodecyl sulfate, all-trans-retinol, palmitate, and 8-anilino-1-naphthalenesulfonate on the heat-induced unfolding and aggregation of β-lactoglobulin B
    • Considine T., Patel H.A., Singh H., Creamer L.K. Influence of binding of sodium dodecyl sulfate, all-trans-retinol, palmitate, and 8-anilino-1-naphthalenesulfonate on the heat-induced unfolding and aggregation of β-lactoglobulin B. J. Agric. Food Chem. 2005, 53:3197-3205.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 3197-3205
    • Considine, T.1    Patel, H.A.2    Singh, H.3    Creamer, L.K.4
  • 52
    • 27144526439 scopus 로고    scopus 로고
    • Influence of binding of sodium dodecyl sulfate, all-trans-retinol, and 8-anilino-1-naphthalenesulfonate on the high-pressure-induced unfolding and aggregation of β-lactoglobulin B
    • Considine T., Singh H., Patel H.A., Creamer L.K. Influence of binding of sodium dodecyl sulfate, all-trans-retinol, and 8-anilino-1-naphthalenesulfonate on the high-pressure-induced unfolding and aggregation of β-lactoglobulin B. J. Agric. Food Chem. 2005, 53:8010-8018.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 8010-8018
    • Considine, T.1    Singh, H.2    Patel, H.A.3    Creamer, L.K.4
  • 54
    • 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 β-lactoglobulin B
    • Considine T., Patel H.A., Singh H., Creamer L.K. Influence of binding conjugated linoleic acid and myristic acid on the heat- and high-pressure-induced unfolding and aggregation of β-lactoglobulin B. Food Chem. 2007, 102:1270-1280.
    • (2007) Food Chem. , vol.102 , pp. 1270-1280
    • Considine, T.1    Patel, H.A.2    Singh, H.3    Creamer, L.K.4
  • 55
    • 0018813814 scopus 로고
    • A study of the effect of sodium dodecyl sulfate on bovine β-casein self-association
    • Creamer L. A study of the effect of sodium dodecyl sulfate on bovine β-casein self-association. Arch. Biochem. Biophys. 1980, 199:172-178.
    • (1980) Arch. Biochem. Biophys. , vol.199 , pp. 172-178
    • Creamer, L.1
  • 56
    • 0028989022 scopus 로고
    • Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin
    • Creamer L.K. Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin. Biochemistry 1995, 34:7170-7176.
    • (1995) Biochemistry , vol.34 , pp. 7170-7176
    • Creamer, L.K.1
  • 58
    • 85007573995 scopus 로고    scopus 로고
    • A review of methods used for investigation of protein-phenolic compound interactions
    • Czubinski J., Dwiecki K. A review of methods used for investigation of protein-phenolic compound interactions. Int. J. Food Sci. Technol. 2017, 52:573-585.
    • (2017) Int. J. Food Sci. Technol. , vol.52 , pp. 573-585
    • Czubinski, J.1    Dwiecki, K.2
  • 59
    • 84882531865 scopus 로고
    • Stabilization of vitamin C by β-lactoglobulin during heat treatment
    • Dai-Dong J.X., Novak G., Hardy J. Stabilization of vitamin C by β-lactoglobulin during heat treatment. Sci. Aliment. 1990, 10:393-401.
    • (1990) Sci. Aliment. , vol.10 , pp. 393-401
    • Dai-Dong, J.X.1    Novak, G.2    Hardy, J.3
  • 60
    • 0019016883 scopus 로고
    • Flavor protein interactions. Binding of carbonyls to bovine serum albumin: thermodynamic and conformational effects
    • Damodaran S., Kinsella J.E. Flavor protein interactions. Binding of carbonyls to bovine serum albumin: thermodynamic and conformational effects. J. Agric. Food Chem. 1980, 28:567-571.
    • (1980) J. Agric. Food Chem. , vol.28 , pp. 567-571
    • Damodaran, S.1    Kinsella, J.E.2
  • 61
    • 0019519117 scopus 로고
    • The effect of neutral salts on the stability of macromolecules-a new approach using a protein-ligand binding system
    • Damodaran S., Kinsella J.E. The effect of neutral salts on the stability of macromolecules-a new approach using a protein-ligand binding system. J. Biol. Chem. 1981, 256:3394-3398.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3394-3398
    • Damodaran, S.1    Kinsella, J.E.2
  • 62
    • 85094110520 scopus 로고    scopus 로고
    • Micronutrient fortification process and its uses.
    • PCT Application No. PCT/NZ2013/000109.
    • Das, S., Ellis, A., Mittal, V.A., Singh, H., Ye, A., 2013. Micronutrient fortification process and its uses. PCT Application No. PCT/NZ2013/000109.
    • (2013)
    • Das, S.1    Ellis, A.2    Mittal, V.A.3    Singh, H.4    Ye, A.5
  • 65
    • 84866726330 scopus 로고    scopus 로고
    • Structuring dairy systems through high pressure processing
    • Devi A.F., Buckow R., Hemar Y., Kasapis S. Structuring dairy systems through high pressure processing. J. Food Eng. 2013, 114:106-122.
    • (2013) J. Food Eng. , vol.114 , pp. 106-122
    • Devi, A.F.1    Buckow, R.2    Hemar, Y.3    Kasapis, S.4
  • 66
    • 84877652827 scopus 로고    scopus 로고
    • Effects of gastrointestinal pH conditions on the stability of the β-lactoglobulin/vitamin D3 complex and on the solubility of vitamin D3
    • Diarrassouba F., Remondetto G., Liang L., Garrait G., Beyssac E., Subirade M. Effects of gastrointestinal pH conditions on the stability of the β-lactoglobulin/vitamin D3 complex and on the solubility of vitamin D3. Food Res. Int. 2013, 52:515-521.
    • (2013) Food Res. Int. , vol.52 , pp. 515-521
    • Diarrassouba, F.1    Remondetto, G.2    Liang, L.3    Garrait, G.4    Beyssac, E.5    Subirade, M.6
  • 67
    • 77956012747 scopus 로고    scopus 로고
    • Flocculation of protein-stabilized oil-in-water emulsions
    • Dickinson E. Flocculation of protein-stabilized oil-in-water emulsions. Colloids Surf. B 2010, 81:130-140.
    • (2010) Colloids Surf. B , vol.81 , pp. 130-140
    • Dickinson, E.1
  • 68
    • 0036325580 scopus 로고    scopus 로고
    • Effects of sucrose and sorbitol on the gel formation of a whey protein isolate
    • Dierckx S., Huyghebaert A. Effects of sucrose and sorbitol on the gel formation of a whey protein isolate. Food Hydrocoll. 2002, 16:489-497.
    • (2002) Food Hydrocoll. , vol.16 , pp. 489-497
    • Dierckx, S.1    Huyghebaert, A.2
  • 69
    • 84941356034 scopus 로고    scopus 로고
    • Comparative structural and conformational studies on two forms of β-lactoglobulin (A and B) upon interaction with lead ion
    • Divsalar A., Saboury A.A. Comparative structural and conformational studies on two forms of β-lactoglobulin (A and B) upon interaction with lead ion. FEBS J. 2005, 272:340.
    • (2005) FEBS J. , vol.272 , pp. 340
    • Divsalar, A.1    Saboury, A.A.2
  • 70
    • 33751375150 scopus 로고    scopus 로고
    • Comparative and structural analysis of the interaction between β-lactoglobulin type A and B with a new anticancer component (2,2'-bipyridin n-hexyl dithiocarbamato Pd(II) nitrate)
    • Divsalar A., Saboury A.A., Mansoori-Torshizi H., Hemmatinejad B. Comparative and structural analysis of the interaction between β-lactoglobulin type A and B with a new anticancer component (2,2'-bipyridin n-hexyl dithiocarbamato Pd(II) nitrate). Bull. Korean Chem. Soc. 2006, 27:1801-1808.
    • (2006) Bull. Korean Chem. Soc. , vol.27 , pp. 1801-1808
    • Divsalar, A.1    Saboury, A.A.2    Mansoori-Torshizi, H.3    Hemmatinejad, B.4
  • 71
    • 84882508563 scopus 로고    scopus 로고
    • A study on the interaction between β-lactoglobulin a and a new antitumor reagent (2,2-bipyridinglycinato Pd(II) chloride)
    • Divsalar A., Saboury A.A., Moosavi-Movahedi A.A. A study on the interaction between β-lactoglobulin a and a new antitumor reagent (2,2-bipyridinglycinato Pd(II) chloride). FEBS J. 2006, 273:333.
    • (2006) FEBS J. , vol.273 , pp. 333
    • Divsalar, A.1    Saboury, A.A.2    Moosavi-Movahedi, A.A.3
  • 73
    • 0025603181 scopus 로고
    • Alcohol induced changes of β-lactoglobulin-retinol-binding stoichiometry
    • Dufour E., Haertle T. Alcohol induced changes of β-lactoglobulin-retinol-binding stoichiometry. Protein Eng. 1990, 4:185-190.
    • (1990) Protein Eng. , vol.4 , pp. 185-190
    • Dufour, E.1    Haertle, T.2
  • 74
    • 0025784171 scopus 로고
    • Binding of retinoids and β-carotene to β-lactoglobulin. Influence of protein modifications
    • Dufour E., Marden M.C., Haertle T. Binding of retinoids and β-carotene to β-lactoglobulin. Influence of protein modifications. Biochim. Biophys. Acta 1991, 1079:316-320.
    • (1991) Biochim. Biophys. Acta , vol.1079 , pp. 316-320
    • Dufour, E.1    Marden, M.C.2    Haertle, T.3
  • 75
    • 0028180075 scopus 로고
    • High-pressure effects on β-lactoglobulin interactions with ligands studied by fluorescence
    • Dufour E., Hui Bon Hoa G., Haertle T. High-pressure effects on β-lactoglobulin interactions with ligands studied by fluorescence. Biochim. Biophys. Acta 1994, 1206:166-172.
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 166-172
    • Dufour, E.1    Hui Bon Hoa, G.2    Haertle, T.3
  • 76
    • 0000521535 scopus 로고
    • High-pressure unfolding and aggregation of β-lactoglobulin and the baroprotective effects of sucrose
    • Dumay E.M., Kalichevsky M.T., Cheftel J.C. High-pressure unfolding and aggregation of β-lactoglobulin and the baroprotective effects of sucrose. J. Agric. Food Chem. 1994, 42:1861-1868.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1861-1868
    • Dumay, E.M.1    Kalichevsky, M.T.2    Cheftel, J.C.3
  • 77
    • 16444386143 scopus 로고    scopus 로고
    • Characteristics of pressure-induced gels of β-lactoglobulin at various times after pressure release
    • Dumay E.M., Kalichevsky M.T., Cheftel J.C. Characteristics of pressure-induced gels of β-lactoglobulin at various times after pressure release. LWT-Food Sci. Technol. 1998, 31:10-19.
    • (1998) LWT-Food Sci. Technol. , vol.31 , pp. 10-19
    • Dumay, E.M.1    Kalichevsky, M.T.2    Cheftel, J.C.3
  • 78
  • 79
    • 79960894785 scopus 로고    scopus 로고
    • Casein-based formulations as promising controlled release drug delivery systems
    • Elzoghby A.O., Abo El-Fotoh W.S., Elgindy N.A. Casein-based formulations as promising controlled release drug delivery systems. J. Control. Release 2011, 153:206-216.
    • (2011) J. Control. Release , vol.153 , pp. 206-216
    • Elzoghby, A.O.1    Abo El-Fotoh, W.S.2    Elgindy, N.A.3
  • 80
    • 84873459472 scopus 로고    scopus 로고
    • Novel spray-dried genipin-crosslinked casein nanoparticles for prolonged release of alfuzosin hydrochloride
    • Elzoghby A.O., Samy W.M., Elgindy N.A. Novel spray-dried genipin-crosslinked casein nanoparticles for prolonged release of alfuzosin hydrochloride. Pharm. Res. 2013, 30:512-522.
    • (2013) Pharm. Res. , vol.30 , pp. 512-522
    • Elzoghby, A.O.1    Samy, W.M.2    Elgindy, N.A.3
  • 81
    • 0032076415 scopus 로고    scopus 로고
    • Potential uses of caseinophosphopeptides
    • FitzGerald R.J. Potential uses of caseinophosphopeptides. Int. Dairy J. 1998, 8:451-457.
    • (1998) Int. Dairy J. , vol.8 , pp. 451-457
    • FitzGerald, R.J.1
  • 83
    • 21344467091 scopus 로고
    • Interaction of sucrose ester with casein micelles as characterized by size-exclusion chromatography
    • Fontecha J., Swaisgood H.E. Interaction of sucrose ester with casein micelles as characterized by size-exclusion chromatography. J. Dairy Sci. 1995, 78:2660-2665.
    • (1995) J. Dairy Sci. , vol.78 , pp. 2660-2665
    • Fontecha, J.1    Swaisgood, H.E.2
  • 84
    • 0015988783 scopus 로고
    • Some observations on possible nutritional significance of vitamin-B12-binding and folate-binding proteins in milk
    • Ford J.E. Some observations on possible nutritional significance of vitamin-B12-binding and folate-binding proteins in milk. Br. J. Nutr. 1974, 31:243-257.
    • (1974) Br. J. Nutr. , vol.31 , pp. 243-257
    • Ford, J.E.1
  • 85
    • 27144471876 scopus 로고    scopus 로고
    • Interactions of vitamin D3 with bovine β-lactoglobulin A and β-casein
    • Forrest S.A., Yada R.Y., Rousseau D. Interactions of vitamin D3 with bovine β-lactoglobulin A and β-casein. J. Agric. Food Chem. 2005, 53:8003-8009.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 8003-8009
    • Forrest, S.A.1    Yada, R.Y.2    Rousseau, D.3
  • 86
    • 0000020280 scopus 로고
    • Parameters affecting binding of volatile flavor compounds in model food systems 1. Proteins
    • Franzen K.L., Kinsella J.E. Parameters affecting binding of volatile flavor compounds in model food systems 1. Proteins. J. Agric. Food Chem. 1974, 22:675-678.
    • (1974) J. Agric. Food Chem. , vol.22 , pp. 675-678
    • Franzen, K.L.1    Kinsella, J.E.2
  • 87
    • 0027522088 scopus 로고
    • Probing the fatty acid binding site of β-lactoglobulins
    • Frapin D., Dufour E., Haertle T. Probing the fatty acid binding site of β-lactoglobulins. J. Protein Chem. 1993, 12:443-449.
    • (1993) J. Protein Chem. , vol.12 , pp. 443-449
    • Frapin, D.1    Dufour, E.2    Haertle, T.3
  • 88
    • 0015523573 scopus 로고
    • The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, β-lactoglobulin, and the retinol-binding protein of human plasma
    • Futterman S., Heller J. The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, β-lactoglobulin, and the retinol-binding protein of human plasma. J. Biol. Chem. 1972, 247:5168-5172.
    • (1972) J. Biol. Chem. , vol.247 , pp. 5168-5172
    • Futterman, S.1    Heller, J.2
  • 90
    • 0034670197 scopus 로고    scopus 로고
    • Interactions between b-lactoglobulin and flavour compounds
    • Guichard E., Langourieux S. Interactions between b-lactoglobulin and flavour compounds. Food Chem. 2000, 71:301-308.
    • (2000) Food Chem. , vol.71 , pp. 301-308
    • Guichard, E.1    Langourieux, S.2
  • 91
    • 85019619431 scopus 로고    scopus 로고
    • Preparation of milk protein-vitamin A complexes and their evaluation for vitamin A binding ability
    • Gupta C., Arora S., Syama M.A., Sharma A. Preparation of milk protein-vitamin A complexes and their evaluation for vitamin A binding ability. Food Chem. 2017, 237:141-149.
    • (2017) Food Chem. , vol.237 , pp. 141-149
    • Gupta, C.1    Arora, S.2    Syama, M.A.3    Sharma, A.4
  • 92
    • 33746351961 scopus 로고    scopus 로고
    • Binding studies and computer-aided modelling of macromolecule/odorant interactions
    • Guth H., Fritzler R. Binding studies and computer-aided modelling of macromolecule/odorant interactions. Chem. Biodivers. 2004, 1:2001-2023.
    • (2004) Chem. Biodivers. , vol.1 , pp. 2001-2023
    • Guth, H.1    Fritzler, R.2
  • 93
    • 84875670462 scopus 로고    scopus 로고
    • Formation and characterization of quercetin-loaded chitosan oligosaccharide/β-lactoglobulin nanoparticle
    • Ha H.K., Kim J.W., Lee M.R., Lee W.J. Formation and characterization of quercetin-loaded chitosan oligosaccharide/β-lactoglobulin nanoparticle. Food Res. Int. 2013, 52:82-90.
    • (2013) Food Res. Int. , vol.52 , pp. 82-90
    • Ha, H.K.1    Kim, J.W.2    Lee, M.R.3    Lee, W.J.4
  • 95
    • 0006179834 scopus 로고    scopus 로고
    • Hydration changes upon protein unfolding: cosolvent effect analysis
    • Hammou H.O., Plaza del Pino I.M., Sanchez-Ruiz J.M. Hydration changes upon protein unfolding: cosolvent effect analysis. New J. Chem. 1998, 22:1453-1461.
    • (1998) New J. Chem. , vol.22 , pp. 1453-1461
    • Hammou, H.O.1    Plaza del Pino, I.M.2    Sanchez-Ruiz, J.M.3
  • 97
    • 0034768130 scopus 로고    scopus 로고
    • Characterization of heat-induced aggregates of β-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment
    • Havea P., Singh H., Creamer L.K. Characterization of heat-induced aggregates of β-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment. J. Dairy Res. 2001, 68:483-497.
    • (2001) J. Dairy Res. , vol.68 , pp. 483-497
    • Havea, P.1    Singh, H.2    Creamer, L.K.3
  • 98
    • 84876105321 scopus 로고    scopus 로고
    • A surface enhanced Raman spectroscopic study of interactions between casein and polymethoxyflavones
    • He L., Zheng J., Labuza T.P., Xiao H. A surface enhanced Raman spectroscopic study of interactions between casein and polymethoxyflavones. J. Raman Spectrosc. 2013, 44:531-535.
    • (2013) J. Raman Spectrosc. , vol.44 , pp. 531-535
    • He, L.1    Zheng, J.2    Labuza, T.P.3    Xiao, H.4
  • 101
    • 0001575393 scopus 로고
    • Flavor binding by whey proteins
    • Jasinski E., Kilara A. Flavor binding by whey proteins. Milchwissenschaft 1985, 40:596-599.
    • (1985) Milchwissenschaft , vol.40 , pp. 596-599
    • Jasinski, E.1    Kilara, A.2
  • 102
    • 85011664712 scopus 로고    scopus 로고
    • Comparison of binding interaction between β-lactoglobulin and three common polyphenols using multi-spectroscopy and modeling methods
    • Jia J., Gao X., Hao M., Tang L. Comparison of binding interaction between β-lactoglobulin and three common polyphenols using multi-spectroscopy and modeling methods. Food Chem. 2017, 228:143-151.
    • (2017) Food Chem. , vol.228 , pp. 143-151
    • Jia, J.1    Gao, X.2    Hao, M.3    Tang, L.4
  • 103
    • 0017230911 scopus 로고
    • The interaction between β-lactoglobulin and sodium n-dodecylsulphate
    • Jones M.N., Wilkinson A. The interaction between β-lactoglobulin and sodium n-dodecylsulphate. Biochem. J. 1976, 153:713-718.
    • (1976) Biochem. J. , vol.153 , pp. 713-718
    • Jones, M.N.1    Wilkinson, A.2
  • 104
    • 0030511662 scopus 로고    scopus 로고
    • Effect of di-saccharides on the thermal properties of whey proteins determined by differential scanning calorimetry (DSC)
    • Jou K.D., Harper W.J. Effect of di-saccharides on the thermal properties of whey proteins determined by differential scanning calorimetry (DSC). Milchwissenschaft 1996, 51:509-511.
    • (1996) Milchwissenschaft , vol.51 , pp. 509-511
    • Jou, K.D.1    Harper, W.J.2
  • 105
    • 0033671303 scopus 로고    scopus 로고
    • Determination of apparent binding constants for aroma compounds with β-lactoglobulin by dynamic coupled column liquid chromatography
    • Jouenne E., Crouzet J. Determination of apparent binding constants for aroma compounds with β-lactoglobulin by dynamic coupled column liquid chromatography. J. Agric. Food Chem. 2000, 48:5396-5400.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 5396-5400
    • Jouenne, E.1    Crouzet, J.2
  • 106
    • 0037467420 scopus 로고    scopus 로고
    • Investigation of binding behaviour of α- and β-ionones to β-lactoglobulin at different pH values using a diffusion-based NOE pumping technique
    • Jung D.M., Ebeler S.E. Investigation of binding behaviour of α- and β-ionones to β-lactoglobulin at different pH values using a diffusion-based NOE pumping technique. J. Agric. Food Chem. 2003, 51:1988-1993.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 1988-1993
    • Jung, D.M.1    Ebeler, S.E.2
  • 107
    • 0037125101 scopus 로고    scopus 로고
    • Application of pulse field gradient NMR techniques for investigating binding of flavor compounds to macromolecules
    • Jung D.M., de Ropp J.S., Ebeler S.E. Application of pulse field gradient NMR techniques for investigating binding of flavor compounds to macromolecules. J. Agric. Food Chem. 2002, 50:4262-4269.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 4262-4269
    • Jung, D.M.1    de Ropp, J.S.2    Ebeler, S.E.3
  • 110
    • 0025736765 scopus 로고
    • Binding form of vitamin-B2 in bovine-milk-its concentration, distribution and binding linkage
    • Kanno C., Kanehara N., Shirafuji K., Tanji R., Imai T. Binding form of vitamin-B2 in bovine-milk-its concentration, distribution and binding linkage. J. Nutr. Sci. Vitaminol. 1991, 37:15-27.
    • (1991) J. Nutr. Sci. Vitaminol. , vol.37 , pp. 15-27
    • Kanno, C.1    Kanehara, N.2    Shirafuji, K.3    Tanji, R.4    Imai, T.5
  • 111
    • 1542295067 scopus 로고    scopus 로고
    • Thermal stability of proteins in aqueous polyol solutions: role of the surface tension of water in the stabilizing effect of polyols
    • Kaushik J.K., Bhat R. Thermal stability of proteins in aqueous polyol solutions: role of the surface tension of water in the stabilizing effect of polyols. J. Phys. Chem. B 1998, 102:7058-7066.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 7058-7066
    • Kaushik, J.K.1    Bhat, R.2
  • 113
    • 78651060876 scopus 로고    scopus 로고
    • Interaction between beta-casein and whey proteins as a function of pH and salt concentration
    • Kehoe J.J., Foegeding E.A. Interaction between beta-casein and whey proteins as a function of pH and salt concentration. J. Agric. Food Chem. 2011, 59:349-355.
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 349-355
    • Kehoe, J.J.1    Foegeding, E.A.2
  • 116
    • 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. J. Dairy Sci. 2004, 87:785-796.
    • (2004) J. Dairy Sci. , vol.87 , pp. 785-796
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 117
    • 33947316219 scopus 로고    scopus 로고
    • Promiscuous binding of ligands by β-lactoglobulin involves hydrophobic interactions and plasticity
    • Konuma T., Sakurai M., Goto Y. Promiscuous binding of ligands by β-lactoglobulin involves hydrophobic interactions and plasticity. J. Mol. Biol. 2007, 368:209-218.
    • (2007) J. Mol. Biol. , vol.368 , pp. 209-218
    • Konuma, T.1    Sakurai, M.2    Goto, Y.3
  • 118
    • 33746362954 scopus 로고    scopus 로고
    • Interactions of milk proteins and volatile compounds: implications in the development of protein foods
    • Kühn J., Considine T., Singh H. Interactions of milk proteins and volatile compounds: implications in the development of protein foods. J. Food Sci. 2006, 71:R72-R82.
    • (2006) J. Food Sci. , vol.71 , pp. R72-R82
    • Kühn, J.1    Considine, T.2    Singh, H.3
  • 119
    • 0034072201 scopus 로고    scopus 로고
    • Influence of sucrose on the thermal denaturation, gelation, and emulsion stabilization of whey proteins
    • Kulmyrzaev A., Bryant C., McClements D.J. Influence of sucrose on the thermal denaturation, gelation, and emulsion stabilization of whey proteins. J. Agric. Food Chem. 2000, 48:1593-1597.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 1593-1597
    • Kulmyrzaev, A.1    Bryant, C.2    McClements, D.J.3
  • 120
    • 0039666742 scopus 로고
    • Insect sex pheromone binding by bovine β-lactoglobulin
    • Lamiot E., Dufour E., Haertle T. Insect sex pheromone binding by bovine β-lactoglobulin. J. Agric. Food Chem. 1994, 42:695-699.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 695-699
    • Lamiot, E.1    Dufour, E.2    Haertle, T.3
  • 121
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee J.C., Timasheff S.N. The stabilization of proteins by sucrose. J. Biol. Chem. 1981, 256:7193-7201.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 122
    • 20544474519 scopus 로고    scopus 로고
    • How homogeneous are the trehalose, maltose and sucrose water solutions? An insight from molecular dynamics simulations
    • Lerbret E., Bordat P., Affouard F., Deschamps M., Migliardo F. How homogeneous are the trehalose, maltose and sucrose water solutions? An insight from molecular dynamics simulations. J. Phys. Chem. B 2005, 109:11046-11057.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 11046-11057
    • Lerbret, E.1    Bordat, P.2    Affouard, F.3    Deschamps, M.4    Migliardo, F.5
  • 123
    • 85046686844 scopus 로고    scopus 로고
    • Comparing the binding interaction between β-lactoglobulin and flavonoids with different structure by multi-spectroscopy analysis and molecular docking
    • Li T., Hu P., Dai T., Li P., Ye X., Chen J., Liu C. Comparing the binding interaction between β-lactoglobulin and flavonoids with different structure by multi-spectroscopy analysis and molecular docking. Spectrochim. Acta A: Mol. Biomol. Spectrosc. 2018, 201:197-206.
    • (2018) Spectrochim. Acta A: Mol. Biomol. Spectrosc. , vol.201 , pp. 197-206
    • Li, T.1    Hu, P.2    Dai, T.3    Li, P.4    Ye, X.5    Chen, J.6    Liu, C.7
  • 124
    • 84857059676 scopus 로고    scopus 로고
    • Study of the acid and thermal stability of β-lactoglobulin-ligand complexes using fluorescence quenching
    • Liang L., Subirade M. Study of the acid and thermal stability of β-lactoglobulin-ligand complexes using fluorescence quenching. Food Chem. 2012, 132(4):2023-2029.
    • (2012) Food Chem. , vol.132 , Issue.4 , pp. 2023-2029
    • Liang, L.1    Subirade, M.2
  • 125
    • 75149137932 scopus 로고
    • Studies on the interaction between casein and vitamin A
    • Lietaer E., Poiffait A., Adrian J. Studies on the interaction between casein and vitamin A. LWT-Food Sci. Technol. 1991, 24:39-45.
    • (1991) LWT-Food Sci. Technol. , vol.24 , pp. 39-45
    • Lietaer, E.1    Poiffait, A.2    Adrian, J.3
  • 126
    • 0030040794 scopus 로고    scopus 로고
    • On the role of surface tension in the stabilization of globular proteins
    • Lin T.Y., Timasheff S.N. On the role of surface tension in the stabilization of globular proteins. Protein Sci. 1996, 5:372-381.
    • (1996) Protein Sci. , vol.5 , pp. 372-381
    • Lin, T.Y.1    Timasheff, S.N.2
  • 127
    • 0030783517 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine-lactalbumin
    • Lindner R.A., Kapur A., Carver J.A. The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine-lactalbumin. J. Biol. Chem. 1997, 272:27722-27729.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27722-27729
    • Lindner, R.A.1    Kapur, A.2    Carver, J.A.3
  • 130
  • 131
    • 84856230634 scopus 로고    scopus 로고
    • Casein micelles for nanoencapsulation of hydrophobic compounds.
    • Patent Application
    • Livney, Y.D., Dalgleish, D.G., 2007. Casein micelles for nanoencapsulation of hydrophobic compounds. Patent Application WO2007122613 A1.
    • (2007)
    • Livney, Y.D.1    Dalgleish, D.G.2
  • 133
    • 85026497614 scopus 로고    scopus 로고
    • Optimization of vitamins A and D3 loading in re-assembled casein micelles and effect of loading on stability of vitamin D3 during storage
    • Loewen A., Chan B., Li-Chan E.C.Y. Optimization of vitamins A and D3 loading in re-assembled casein micelles and effect of loading on stability of vitamin D3 during storage. Food Chem. 2018, 240:472-481.
    • (2018) Food Chem. , vol.240 , pp. 472-481
    • Loewen, A.1    Chan, B.2    Li-Chan, E.C.Y.3
  • 134
    • 56449094569 scopus 로고    scopus 로고
    • Recent advances in technologies for vitamin A protection in foods
    • Loveday S.M., Singh H. Recent advances in technologies for vitamin A protection in foods. Trends Food Sci. Technol. 2008, 19:657-668.
    • (2008) Trends Food Sci. Technol. , vol.19 , pp. 657-668
    • Loveday, S.M.1    Singh, H.2
  • 135
    • 84887253281 scopus 로고    scopus 로고
    • Food protein nanoparticles: formation, properties and applications
    • Blackwell Publishing, Oxford, UK, B. Bhandari, Y.H. Roos (Eds.)
    • Loveday S.M., Rao M.A., Singh H. Food protein nanoparticles: formation, properties and applications. Food Materials Science and Engineering 2012, 263-294. Blackwell Publishing, Oxford, UK. B. Bhandari, Y.H. Roos (Eds.).
    • (2012) Food Materials Science and Engineering , pp. 263-294
    • Loveday, S.M.1    Rao, M.A.2    Singh, H.3
  • 136
    • 84883556744 scopus 로고    scopus 로고
    • Innovative yoghurts: novel processing technologies for improving acid milk gel texture
    • Loveday S.M., Sarkar A., Singh H. Innovative yoghurts: novel processing technologies for improving acid milk gel texture. Trends Food Sci. Technol. 2013, 33:5-20.
    • (2013) Trends Food Sci. Technol. , vol.33 , pp. 5-20
    • Loveday, S.M.1    Sarkar, A.2    Singh, H.3
  • 137
    • 27744538417 scopus 로고    scopus 로고
    • Effect of cationic surfactants on the interaction between sodium perfluorooctanoate and β-lactoglobulin
    • Lu R.-C., Cao A.-N., Lai L.-H., Xiao J.-X. Effect of cationic surfactants on the interaction between sodium perfluorooctanoate and β-lactoglobulin. J. Colloid Interface Sci. 2006, 293:61-68.
    • (2006) J. Colloid Interface Sci. , vol.293 , pp. 61-68
    • Lu, R.-C.1    Cao, A.-N.2    Lai, L.-H.3    Xiao, J.-X.4
  • 138
    • 0031240572 scopus 로고    scopus 로고
    • Interaction of mercury with human and bovine milk proteins
    • Mata L., Sanchez L., Calvo M. Interaction of mercury with human and bovine milk proteins. Biosci. Biotechnol. Biochem. 1997, 61:1641-1645.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1641-1645
    • Mata, L.1    Sanchez, L.2    Calvo, M.3
  • 139
    • 0029942515 scopus 로고    scopus 로고
    • Biopolymer-surfactant interaction: 4. Kinetics of binding of cetyltrimethyl ammonium bromide with gelatin, hemoglobin, β-lactoglobulin and lysozyme
    • Maulik S., Moulik S.P., Chattoraj D.K. Biopolymer-surfactant interaction: 4. Kinetics of binding of cetyltrimethyl ammonium bromide with gelatin, hemoglobin, β-lactoglobulin and lysozyme. J. Biomol. Struct. Dyn. 1996, 13:771-780.
    • (1996) J. Biomol. Struct. Dyn. , vol.13 , pp. 771-780
    • Maulik, S.1    Moulik, S.P.2    Chattoraj, D.K.3
  • 140
    • 0036731234 scopus 로고    scopus 로고
    • Modulation of globular protein functionality by weakly interacting cosolvents
    • McClements D.J. Modulation of globular protein functionality by weakly interacting cosolvents. Crit. Rev. Food Sci. Nutr. 2002, 42:417-471.
    • (2002) Crit. Rev. Food Sci. Nutr. , vol.42 , pp. 417-471
    • McClements, D.J.1
  • 141
    • 0000773537 scopus 로고
    • Vanillin interaction with milk protein isolates in sweetened drinks
    • McNeill V.L., Schmidt K.A. Vanillin interaction with milk protein isolates in sweetened drinks. J. Food Sci. 1993, 58(1142-1144):1147.
    • (1993) J. Food Sci. , vol.58 , Issue.1142-1144 , pp. 1147
    • McNeill, V.L.1    Schmidt, K.A.2
  • 142
    • 84877080943 scopus 로고    scopus 로고
    • Interactions of β-lactoglobulin variants A and B with vitamin A. Competitive binding of retinoids and carotenoids
    • Mensi A., Choiset Y., Rabesona H., Haertlé T., Borel P., Chobert J.-M. Interactions of β-lactoglobulin variants A and B with vitamin A. Competitive binding of retinoids and carotenoids. J. Agric. Food Chem. 2013, 61:4114-4119.
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 4114-4119
    • Mensi, A.1    Choiset, Y.2    Rabesona, H.3    Haertlé, T.4    Borel, P.5    Chobert, J.-M.6
  • 143
    • 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., Jameson G.B. Bovine β-lactoglobulin is dimeric under imitative physiological conditions: dissociation equilibrium and rate constants over the pH range of 2.5-7.5. Biophys. J. 2012, 103:303-312.
    • (2012) Biophys. J. , 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    Jameson, G.B.7
  • 144
    • 84925332821 scopus 로고    scopus 로고
    • Influence of calcium depletion on iron-binding properties of milk
    • Mittal V.A., Ellis A., Ye A., Das S., Singh H. Influence of calcium depletion on iron-binding properties of milk. J. Dairy Sci. 2015, 98:2103-2113.
    • (2015) J. Dairy Sci. , vol.98 , pp. 2103-2113
    • Mittal, V.A.1    Ellis, A.2    Ye, A.3    Das, S.4    Singh, H.5
  • 146
    • 85021079551 scopus 로고    scopus 로고
    • The adsorption of orthophosphate onto casein-iron precipitates
    • Mittal V.A., Ellis A., Ye A., Edwards P.J.B., Singh H. The adsorption of orthophosphate onto casein-iron precipitates. Food Chem. 2018, 239:17-22.
    • (2018) Food Chem. , vol.239 , pp. 17-22
    • Mittal, V.A.1    Ellis, A.2    Ye, A.3    Edwards, P.J.B.4    Singh, H.5
  • 147
    • 84930210665 scopus 로고    scopus 로고
    • Exploring the interaction of naringenin with bovine beta-casein nanoparticles using spectroscopy
    • Moeiniafshari A.-A., Zarrabi A., Bordbar A.-K. Exploring the interaction of naringenin with bovine beta-casein nanoparticles using spectroscopy. Food Hydrocoll. 2015, 51:1-6.
    • (2015) Food Hydrocoll. , vol.51 , pp. 1-6
    • Moeiniafshari, A.-A.1    Zarrabi, A.2    Bordbar, A.-K.3
  • 148
    • 84923647904 scopus 로고    scopus 로고
    • Study on the interactions of trans-resveratrol and curcumin with bovine α-lactalbumin by spectroscopic analysis and molecular docking
    • Mohammadi F., Moeeni M. Study on the interactions of trans-resveratrol and curcumin with bovine α-lactalbumin by spectroscopic analysis and molecular docking. Mater. Sci. Eng. C 2015, 50:358-366.
    • (2015) Mater. Sci. Eng. C , vol.50 , pp. 358-366
    • Mohammadi, F.1    Moeeni, M.2
  • 149
    • 0014672035 scopus 로고
    • Hydrophobic binding of hydrocarbons by proteins II. Relationship of protein structure
    • Mohammadzadeh K.A., Smith G.M., Feeney R.E. Hydrophobic binding of hydrocarbons by proteins II. Relationship of protein structure. Biochim. Biophys. Acta 1969, 194:256-264.
    • (1969) Biochim. Biophys. Acta , vol.194 , pp. 256-264
    • Mohammadzadeh, K.A.1    Smith, G.M.2    Feeney, R.E.3
  • 150
    • 84872683329 scopus 로고    scopus 로고
    • Binding of vitamin A by casein micelles in commercial skim milk
    • Mohan M.S., Jurat-Fuentes J.L., Harte F. Binding of vitamin A by casein micelles in commercial skim milk. J. Dairy Sci. 2013, 96:790-798.
    • (2013) J. Dairy Sci. , vol.96 , pp. 790-798
    • Mohan, M.S.1    Jurat-Fuentes, J.L.2    Harte, F.3
  • 151
    • 0023661017 scopus 로고
    • Crystal structure of the trigonal form of bovine β-lactoglobulin and of its complex with retinol at 2.5 Å resolution
    • Monaco H.L., Zanotti G., Spadon P., Bolognesi M., Sawyer L., Eliopoulos E.E. Crystal structure of the trigonal form of bovine β-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 1987, 197:695-706.
    • (1987) J. Mol. Biol. , 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
  • 152
    • 0033857440 scopus 로고    scopus 로고
    • Sugar-casein interaction in deuterated solutions of bovine and caprine casein as determined by oxygen-17 and carbon-13 nuclear magnetic resonance: a case of preferential interactions
    • Mora-Gutierrez A., Farrell H.M. Sugar-casein interaction in deuterated solutions of bovine and caprine casein as determined by oxygen-17 and carbon-13 nuclear magnetic resonance: a case of preferential interactions. J. Agric. Food Chem. 2000, 48:3245-3255.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 3245-3255
    • Mora-Gutierrez, A.1    Farrell, H.M.2
  • 153
    • 0034849396 scopus 로고    scopus 로고
    • Interaction of β-lactoglobulin with small hydrophobic ligands as monitored by fluorometry and equilibrium dialysis: nonlinear quenching effects related to protein-protein association
    • Muresan S., van der Bent A., de Wolf F.A. Interaction of β-lactoglobulin with small hydrophobic ligands as monitored by fluorometry and equilibrium dialysis: nonlinear quenching effects related to protein-protein association. J. Agric. Food Chem. 2001, 49:2609-2618.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 2609-2618
    • Muresan, S.1    van der Bent, A.2    de Wolf, F.A.3
  • 154
    • 0033397255 scopus 로고    scopus 로고
    • Enhancement of the foaming properties of protein dried in the presence of trehalose
    • Murray B.S., Liang H.J. Enhancement of the foaming properties of protein dried in the presence of trehalose. J. Agric. Food Chem. 1999, 47:4984-4991.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 4984-4991
    • Murray, B.S.1    Liang, H.J.2
  • 155
    • 0027630799 scopus 로고
    • Iron-binding properties of bovine lactoferrin in iron-rich solution
    • Nagasako Y., Saito H., Tamura Y., Shimamura S., Tomita M. Iron-binding properties of bovine lactoferrin in iron-rich solution. J. Dairy Sci. 1993, 76:1876-1881.
    • (1993) J. Dairy Sci. , vol.76 , pp. 1876-1881
    • Nagasako, Y.1    Saito, H.2    Tamura, Y.3    Shimamura, S.4    Tomita, M.5
  • 156
    • 84856230214 scopus 로고    scopus 로고
    • Non-covalent binding of proteins to polyphenols correlates with their amino acid sequence
    • Nagy K., Courtet-Compondu M.C., Williamson G., Rezzi S., Kussmann M., Rytz A. Non-covalent binding of proteins to polyphenols correlates with their amino acid sequence. Food Chem. 2012, 132:1333-1339.
    • (2012) Food Chem. , vol.132 , pp. 1333-1339
    • Nagy, K.1    Courtet-Compondu, M.C.2    Williamson, G.3    Rezzi, S.4    Kussmann, M.5    Rytz, A.6
  • 157
    • 0031035893 scopus 로고    scopus 로고
    • Fatty acids and retinoids bind independently and simultaneously to β-lactoglobulin
    • Narayan M., Berliner L.J. Fatty acids and retinoids bind independently and simultaneously to β-lactoglobulin. Biochemistry 1997, 36:1906-1911.
    • (1997) Biochemistry , vol.36 , pp. 1906-1911
    • Narayan, M.1    Berliner, L.J.2
  • 158
    • 0031892161 scopus 로고    scopus 로고
    • Mapping fatty acid binding to β-lactoglobulin: ligand binding is restricted by modification of Cys 121
    • Narayan M., Berliner L.J. Mapping fatty acid binding to β-lactoglobulin: ligand binding is restricted by modification of Cys 121. Protein Sci. 1998, 7:150-157.
    • (1998) Protein Sci. , vol.7 , pp. 150-157
    • Narayan, M.1    Berliner, L.J.2
  • 159
    • 4344626567 scopus 로고    scopus 로고
    • Quantitative description of the interaction between folate and the folate-binding protein from cow's milk
    • Nixon P.F., Jones M., Winzor D.J. Quantitative description of the interaction between folate and the folate-binding protein from cow's milk. Biochem. J. 2004, 382:215-221.
    • (2004) Biochem. J. , vol.382 , pp. 215-221
    • Nixon, P.F.1    Jones, M.2    Winzor, D.J.3
  • 160
    • 0742331980 scopus 로고    scopus 로고
    • Heat-induced coagulation of milk
    • Kluwer Academic/Plenum Publishers, New York, NY, P.F. Fox, P.L.H. McSweeney (Eds.)
    • O'Connell J.E., Fox P.F. Heat-induced coagulation of milk. Advanced Dairy Chemistry-Proteins 2003, 879-945. Kluwer Academic/Plenum Publishers, New York, NY. third ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Advanced Dairy Chemistry-Proteins , pp. 879-945
    • O'Connell, J.E.1    Fox, P.F.2
  • 162
    • 84924956062 scopus 로고    scopus 로고
    • Molecular characterization of whey protein hydrolysate fractions with ferrous chelating and enhanced iron solubility capabilities
    • O'Loughlin I.B., Kelly P.M., Murray B.A., Fitzgerald R.J., Brodkorb A. Molecular characterization of whey protein hydrolysate fractions with ferrous chelating and enhanced iron solubility capabilities. J. Agric. Food Chem. 2015, 63(10):270-2714.
    • (2015) J. Agric. Food Chem. , vol.63 , Issue.10 , pp. 270-2714
    • O'Loughlin, I.B.1    Kelly, P.M.2    Murray, B.A.3    Fitzgerald, R.J.4    Brodkorb, A.5
  • 163
    • 33845282222 scopus 로고
    • Binding of alkanone flavors to β-lactoglobulin-effects of conformational and chemical modification
    • O'Neill T.E., Kinsella J.E. Binding of alkanone flavors to β-lactoglobulin-effects of conformational and chemical modification. J. Agric. Food Chem. 1987, 35:770-774.
    • (1987) J. Agric. Food Chem. , vol.35 , pp. 770-774
    • O'Neill, T.E.1    Kinsella, J.E.2
  • 165
    • 84937525091 scopus 로고    scopus 로고
    • Effects of pH and protein conformation on in-solution complexation between bovine α-lactalbumin and oleic acid: binding trend analysis by using SPR and ITC
    • Park Y.J., Kim K.H., Lim D.W., Lee E.K. Effects of pH and protein conformation on in-solution complexation between bovine α-lactalbumin and oleic acid: binding trend analysis by using SPR and ITC. Process Biochem. 2015, 50:1379-1387.
    • (2015) Process Biochem. , vol.50 , pp. 1379-1387
    • Park, Y.J.1    Kim, K.H.2    Lim, D.W.3    Lee, E.K.4
  • 166
    • 0032463144 scopus 로고    scopus 로고
    • Improvement of zinc intestinal absorption and reduction of zinc/iron interaction using metal bound to the caseinophosphopeptide 1-25 of β-casein
    • Peres J.M., Bouhallab S., Petit C., Bureau F., Maubois J.L., Arhan P., Bougle D. Improvement of zinc intestinal absorption and reduction of zinc/iron interaction using metal bound to the caseinophosphopeptide 1-25 of β-casein. Reprod. Nutr. Dev. 1998, 38:465-472.
    • (1998) Reprod. Nutr. Dev. , vol.38 , pp. 465-472
    • Peres, J.M.1    Bouhallab, S.2    Petit, C.3    Bureau, F.4    Maubois, J.L.5    Arhan, P.6    Bougle, D.7
  • 167
    • 0029302371 scopus 로고
    • Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review
    • Pérez M.D., Calvo M. Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review. J. Dairy Sci. 1995, 78:978-988.
    • (1995) J. Dairy Sci. , vol.78 , pp. 978-988
    • Pérez, M.D.1    Calvo, M.2
  • 169
    • 0025356635 scopus 로고
    • Synthesis and evolution of concentration of β-lactoglobulin and α-lactalbumin from cow and sheep colostrums and milk throughout early lactation
    • Pérez M.D., Sanchez L., Aranda P., Ena J.M., Calvo M. Synthesis and evolution of concentration of β-lactoglobulin and α-lactalbumin from cow and sheep colostrums and milk throughout early lactation. Cell. Mol. Biol. 1990, 36:205-212.
    • (1990) Cell. Mol. Biol. , vol.36 , pp. 205-212
    • Pérez, M.D.1    Sanchez, L.2    Aranda, P.3    Ena, J.M.4    Calvo, M.5
  • 170
    • 0026595106 scopus 로고
    • Effect of β-lactoglobulin on the activity of pregastric lipase. A possible role for this protein in ruminant milk
    • Pérez M.D., Sanchez L., Aranda P., Ena J.M., Oria R., Calvo M. Effect of β-lactoglobulin on the activity of pregastric lipase. A possible role for this protein in ruminant milk. Biochim. Biophys. Acta 1992, 1123:151-155.
    • (1992) Biochim. Biophys. Acta , vol.1123 , pp. 151-155
    • Pérez, M.D.1    Sanchez, L.2    Aranda, P.3    Ena, J.M.4    Oria, R.5    Calvo, M.6
  • 171
    • 0027549546 scopus 로고
    • Comparison of the ability to bind lipids of β-lactoglobulin and serum-albumin of milk from ruminant and non-ruminant species
    • Pérez M.D., Puyol P., Ena J.M., Calvo M. Comparison of the ability to bind lipids of β-lactoglobulin and serum-albumin of milk from ruminant and non-ruminant species. J. Dairy Res. 1993, 60:55-63.
    • (1993) J. Dairy Res. , vol.60 , pp. 55-63
    • Pérez, M.D.1    Puyol, P.2    Ena, J.M.3    Calvo, M.4
  • 173
    • 0025739751 scopus 로고
    • Interaction between casein and vitamin A during food processing
    • Poiffait A., Adrian J. Interaction between casein and vitamin A during food processing. Adv. Exp. Med. Biol. 1991, 289:61-73.
    • (1991) Adv. Exp. Med. Biol. , vol.289 , pp. 61-73
    • Poiffait, A.1    Adrian, J.2
  • 174
    • 77956022419 scopus 로고    scopus 로고
    • Enthalpically driven peptide stabilization by protective osmolytes
    • Politi R., Harries D. Enthalpically driven peptide stabilization by protective osmolytes. Chem. Commun. 2010, 46:6449-6451.
    • (2010) Chem. Commun. , vol.46 , pp. 6449-6451
    • Politi, R.1    Harries, D.2
  • 175
    • 84887346615 scopus 로고
    • Interaction of bovine β-lactoglobulin and other bovine and human whey proteins with retinol and fatty acids
    • Puyol P., Perez M.D., Peiro J.M., Calvo M. Interaction of bovine β-lactoglobulin and other bovine and human whey proteins with retinol and fatty acids. Agric. Biol. Chem. 1991, 55:2515-2520.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 2515-2520
    • Puyol, P.1    Perez, M.D.2    Peiro, J.M.3    Calvo, M.4
  • 176
    • 0041791450 scopus 로고
    • Study on interaction between β-lactoglobulin and other bovine whey proteins with ascorbic acid
    • Puyol P., Perez M.D., Mata L., Calvo M. Study on interaction between β-lactoglobulin and other bovine whey proteins with ascorbic acid. Milchwissenschaft 1994, 49:25-27.
    • (1994) Milchwissenschaft , vol.49 , pp. 25-27
    • Puyol, P.1    Perez, M.D.2    Mata, L.3    Calvo, M.4
  • 177
    • 85007524174 scopus 로고    scopus 로고
    • Stabilization of whey protein isolate (WPI) through interactions with sugar beet pectin (SBP) induced by controlled dry-heating
    • Qi P.X., Xiao Y., Wickham E.D. Stabilization of whey protein isolate (WPI) through interactions with sugar beet pectin (SBP) induced by controlled dry-heating. Food Hydrocoll. 2017, 67:1-13.
    • (2017) Food Hydrocoll. , vol.67 , pp. 1-13
    • Qi, P.X.1    Xiao, Y.2    Wickham, E.D.3
  • 178
    • 0031738305 scopus 로고    scopus 로고
    • 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin
    • Qin B.Y., Creamer L.K., Baker E.N., Jameson G.B. 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin. FEBS Lett. 1998, 438:272-278.
    • (1998) FEBS Lett. , vol.438 , pp. 272-278
    • Qin, B.Y.1    Creamer, L.K.2    Baker, E.N.3    Jameson, G.B.4
  • 181
    • 84856220538 scopus 로고    scopus 로고
    • Heating of milk alters the binding of curcumin to casein micelles. A fluorescence spectroscopy study
    • Rahimi Yazdi S., Corredig M. Heating of milk alters the binding of curcumin to casein micelles. A fluorescence spectroscopy study. Food Chem. 2012, 132:1143-1149.
    • (2012) Food Chem. , vol.132 , pp. 1143-1149
    • Rahimi Yazdi, S.1    Corredig, M.2
  • 182
    • 49749159804 scopus 로고
    • The effects of several milk components and similar compounds on the utilization of carotene by the rat
    • Raica N., Vavich M.G., Kemmerer A.R. The effects of several milk components and similar compounds on the utilization of carotene by the rat. Arch. Biochem. Biophys. 1959, 83:376-380.
    • (1959) Arch. Biochem. Biophys. , vol.83 , pp. 376-380
    • Raica, N.1    Vavich, M.G.2    Kemmerer, A.R.3
  • 183
    • 85010250962 scopus 로고
    • Flavour retention during drying
    • Reineccius G.A., Coulter S.T. Flavour retention during drying. J. Dairy Sci. 1969, 52:1219-1223.
    • (1969) J. Dairy Sci. , vol.52 , pp. 1219-1223
    • Reineccius, G.A.1    Coulter, S.T.2
  • 184
    • 0037139161 scopus 로고    scopus 로고
    • Effect of the aqueous phase composition on the adsorption of bovine serum albumin to the air-water interface
    • Rodríguez Niño M.R., Rodríguez Patino J.M. Effect of the aqueous phase composition on the adsorption of bovine serum albumin to the air-water interface. Ind. Eng. Chem. Res. 2002, 41:1489-1495.
    • (2002) Ind. Eng. Chem. Res. , vol.41 , pp. 1489-1495
    • Rodríguez Niño, M.R.1    Rodríguez Patino, J.M.2
  • 185
    • 33847160392 scopus 로고    scopus 로고
    • Thermal stability of β-lactoglobulin in the presence of aqueous solution of alcohols and polyols
    • Romero C.M., Lozano J.M., Sancho J., Giraldo G.I. Thermal stability of β-lactoglobulin in the presence of aqueous solution of alcohols and polyols. Int. J. Biol. Macromol. 2007, 40:423-428.
    • (2007) Int. J. Biol. Macromol. , vol.40 , pp. 423-428
    • Romero, C.M.1    Lozano, J.M.2    Sancho, J.3    Giraldo, G.I.4
  • 186
    • 35748961997 scopus 로고    scopus 로고
    • Molecular basis of osmolyte effects on protein and metabolites
    • Rösgen J. Molecular basis of osmolyte effects on protein and metabolites. Methods Enzymol. 2007, 428:459-486.
    • (2007) Methods Enzymol. , vol.428 , pp. 459-486
    • Rösgen, J.1
  • 187
    • 33644596182 scopus 로고    scopus 로고
    • Thermodynamics of binding interactions between bovine β-lactoglobulin A and the antihypertensive peptide β-Lg f142-148
    • Roufik S., Gauthier S.F., Leng X., Turgeon S.L. Thermodynamics of binding interactions between bovine β-lactoglobulin A and the antihypertensive peptide β-Lg f142-148. Biomacromolecules 2006, 7:419-426.
    • (2006) Biomacromolecules , vol.7 , pp. 419-426
    • Roufik, S.1    Gauthier, S.F.2    Leng, X.3    Turgeon, S.L.4
  • 188
    • 84858693960 scopus 로고    scopus 로고
    • Fluorescence spectroscopic study on interaction of retinol with β-lactoglobulin in the presence of cetylpyridinium chloride
    • Sahihi M., Ghayeb Y., Bordbar A.-K. Fluorescence spectroscopic study on interaction of retinol with β-lactoglobulin in the presence of cetylpyridinium chloride. Spectroscopy 2012, 27:27-34.
    • (2012) Spectroscopy , vol.27 , pp. 27-34
    • Sahihi, M.1    Ghayeb, Y.2    Bordbar, A.-K.3
  • 189
    • 84873710829 scopus 로고    scopus 로고
    • Thermal protection of β-carotene in re-assembled casein micelles during different processing technologies applied in food industry
    • Sáiz-Abajo M.J., González-Ferrero C., Moreno-Ruiz A., Romo-Hualde A., González-Navarro C.J. Thermal protection of β-carotene in re-assembled casein micelles during different processing technologies applied in food industry. Food Chem. 2013, 138:1581-1587.
    • (2013) Food Chem. , vol.138 , pp. 1581-1587
    • Sáiz-Abajo, M.J.1    González-Ferrero, C.2    Moreno-Ruiz, A.3    Romo-Hualde, A.4    González-Navarro, C.J.5
  • 190
    • 0021056137 scopus 로고
    • Neonatal role of milk folate-binding protein-studies on the course of digestion of goat's milk folate binder in the 6-d-old kid
    • Salter D.N., Mowlem A. Neonatal role of milk folate-binding protein-studies on the course of digestion of goat's milk folate binder in the 6-d-old kid. Br. J. Nutr. 1983, 50:589-596.
    • (1983) Br. J. Nutr. , vol.50 , pp. 589-596
    • Salter, D.N.1    Mowlem, A.2
  • 191
    • 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. 1999, 9:791-800.
    • (1999) 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
  • 193
    • 85033460801 scopus 로고    scopus 로고
    • Biophysical and computational comparison on the binding affinity of three important nutrients to beta-lactoglobulin: folic acid, ascorbic acid and vitamin K3
    • Shahraki S., Heydari A., Saeidifar M., Gomroki M. Biophysical and computational comparison on the binding affinity of three important nutrients to beta-lactoglobulin: folic acid, ascorbic acid and vitamin K3. J. Biomol. Struct. Dyn. 2018, 36:3651-3665.
    • (2018) J. Biomol. Struct. Dyn. , vol.36 , pp. 3651-3665
    • Shahraki, S.1    Heydari, A.2    Saeidifar, M.3    Gomroki, M.4
  • 194
    • 77957346768 scopus 로고    scopus 로고
    • β-Casein nanoparticles as an oral delivery system for chemotherapeutic drugs: impact of drug structure and properties on co-assembly
    • Shapira A., Assaraf Y.G., Epstein D., Livney Y.D. β-Casein nanoparticles as an oral delivery system for chemotherapeutic drugs: impact of drug structure and properties on co-assembly. Pharm. Res. 2010, 27:2175-2186.
    • (2010) Pharm. Res. , vol.27 , pp. 2175-2186
    • Shapira, A.1    Assaraf, Y.G.2    Epstein, D.3    Livney, Y.D.4
  • 195
    • 84952628153 scopus 로고    scopus 로고
    • Preparation of succinylated sodium caseinate-iron complex by adopting ultrafiltration technology: a novel food fortificant
    • Shilpashree B.G., Arora S., Sharma V., Singh A.K. Preparation of succinylated sodium caseinate-iron complex by adopting ultrafiltration technology: a novel food fortificant. Innov. Food Sci. Emerg. Technol. 2015, 32:165-171.
    • (2015) Innov. Food Sci. Emerg. Technol. , vol.32 , pp. 165-171
    • Shilpashree, B.G.1    Arora, S.2    Sharma, V.3    Singh, A.K.4
  • 196
    • 84944189690 scopus 로고    scopus 로고
    • Preparation of iron bound succinylated milk protein concentrate and evaluation of its stability
    • Shilpashree B.G., Arora S., Sharma V., Bajaj R.K., Tomar S.K. Preparation of iron bound succinylated milk protein concentrate and evaluation of its stability. Food Chem. 2016, 196:800-807.
    • (2016) Food Chem. , vol.196 , pp. 800-807
    • Shilpashree, B.G.1    Arora, S.2    Sharma, V.3    Bajaj, R.K.4    Tomar, S.K.5
  • 197
    • 0030524887 scopus 로고    scopus 로고
    • Stabilities of bovine β-lactoglobulin/retinol or retinoic acid complexes against tryptic hydrolysis, heating and light-induced oxidation
    • Shimoyamada M., Yoshimura H., Tomida K., Watanabe K. Stabilities of bovine β-lactoglobulin/retinol or retinoic acid complexes against tryptic hydrolysis, heating and light-induced oxidation. Lebensm. Wiss. Technol. 1996, 29:763-766.
    • (1996) Lebensm. Wiss. Technol. , vol.29 , pp. 763-766
    • Shimoyamada, M.1    Yoshimura, H.2    Tomida, K.3    Watanabe, K.4
  • 199
    • 16344386295 scopus 로고    scopus 로고
    • Thermal denaturation, aggregation and gelation of whey proteins
    • Kluwer Academic/Plenum Publishers, New York, NY, P.F. Fox, P.L.H. McSweeney (Eds.)
    • Singh H., Havea P. Thermal denaturation, aggregation and gelation of whey proteins. Advanced Dairy Chemistry-Proteins 2003, 1261-1287. Kluwer Academic/Plenum Publishers, New York, NY. third ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Advanced Dairy Chemistry-Proteins , pp. 1261-1287
    • Singh, H.1    Havea, P.2
  • 200
    • 79251618192 scopus 로고    scopus 로고
    • Protein and DNA destabilization by osmolytes: the other side of the coin
    • Singh L.R., Poddar N.K., Dar T.A., Kumar R., Ahmad F. Protein and DNA destabilization by osmolytes: the other side of the coin. Life Sci. 2011, 88:117-125.
    • (2011) Life Sci. , vol.88 , pp. 117-125
    • Singh, L.R.1    Poddar, N.K.2    Dar, T.A.3    Kumar, R.4    Ahmad, F.5
  • 202
    • 78049267292 scopus 로고    scopus 로고
    • Interaction of curcumin with β-lactoglobulin; stability, spectroscopic analysis, and molecular modeling of the complex
    • Sneharani A.H., Karakkat J.V., Singh S.A., Rao A.G.A. Interaction of curcumin with β-lactoglobulin; stability, spectroscopic analysis, and molecular modeling of the complex. J. Agric. Food Chem. 2010, 58:11130-11139.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 11130-11139
    • Sneharani, A.H.1    Karakkat, J.V.2    Singh, S.A.3    Rao, A.G.A.4
  • 203
    • 0032143329 scopus 로고    scopus 로고
    • Immobilized β-lactoglobulin on a HPLC-column: a rapid way to determine protein-flavour interactions
    • Sostmann K., Guichard E. Immobilized β-lactoglobulin on a HPLC-column: a rapid way to determine protein-flavour interactions. Food Chem. 1998, 62:509-513.
    • (1998) Food Chem. , vol.62 , pp. 509-513
    • Sostmann, K.1    Guichard, E.2
  • 204
    • 0016691920 scopus 로고
    • Fatty acid binding to plasma albumin
    • Spector A.A. Fatty acid binding to plasma albumin. J. Lipid Res. 1975, 16:165-179.
    • (1975) J. Lipid Res. , vol.16 , pp. 165-179
    • Spector, A.A.1
  • 205
    • 0014440335 scopus 로고
    • Binding of long-chain fatty acids to bovine serum albumin
    • Spector A.A., John K., Fletcher J.E. Binding of long-chain fatty acids to bovine serum albumin. J. Lipid Res. 1969, 10:56-67.
    • (1969) J. Lipid Res. , vol.10 , pp. 56-67
    • Spector, A.A.1    John, K.2    Fletcher, J.E.3
  • 206
    • 0033410063 scopus 로고    scopus 로고
    • Whey protein aggregation under shear conditions-effects of lactose and heating temperature on aggregate size and structure
    • Spiegel T. Whey protein aggregation under shear conditions-effects of lactose and heating temperature on aggregate size and structure. Int. J. Food Sci. Technol. 1999, 34:523-531.
    • (1999) Int. J. Food Sci. Technol. , vol.34 , pp. 523-531
    • Spiegel, T.1
  • 207
    • 52549105587 scopus 로고    scopus 로고
    • Interaction of α-lactalbumin with mini-αA-crystallin
    • Sreelakshmi Y., Sharma K.K. Interaction of α-lactalbumin with mini-αA-crystallin. J. Protein Chem. 2001, 20:123-130.
    • (2001) J. Protein Chem. , vol.20 , pp. 123-130
    • Sreelakshmi, Y.1    Sharma, K.K.2
  • 208
    • 84867896149 scopus 로고    scopus 로고
    • Binding affinity between dietary polyphenols and β-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed
    • Stojadinovic M., Radosavljevic J., Ognjenovic J., Vesic J., Prodic I., Stanic-Vucinic D., Cirkovic Velickovic T. Binding affinity between dietary polyphenols and β-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed. Food Chem. 2013, 136:1263-1271.
    • (2013) Food Chem. , vol.136 , pp. 1263-1271
    • Stojadinovic, M.1    Radosavljevic, J.2    Ognjenovic, J.3    Vesic, J.4    Prodic, I.5    Stanic-Vucinic, D.6    Cirkovic Velickovic, T.7
  • 209
    • 59649116856 scopus 로고    scopus 로고
    • Characterisation of binding of iron to sodium caseinate and whey protein isolate
    • Sugiarto M., Ye A., Singh H. Characterisation of binding of iron to sodium caseinate and whey protein isolate. Food Chem. 2009, 114:1007-1013.
    • (2009) Food Chem. , vol.114 , pp. 1007-1013
    • Sugiarto, M.1    Ye, A.2    Singh, H.3
  • 210
    • 77950652975 scopus 로고    scopus 로고
    • Milk protein-iron complexes: inhibition of lipid oxidation in an emulsion
    • Sugiarto M., Ye A., Taylor M.W., Singh H. Milk protein-iron complexes: inhibition of lipid oxidation in an emulsion. Dairy Sci. Technol. 2010, 90:87-98.
    • (2010) Dairy Sci. Technol. , vol.90 , pp. 87-98
    • Sugiarto, M.1    Ye, A.2    Taylor, M.W.3    Singh, H.4
  • 211
    • 67650813264 scopus 로고    scopus 로고
    • Protein ingredient for carrying lipophilic nutrients.
    • United States Patent
    • Swaisgood, H.E., 2001. Protein ingredient for carrying lipophilic nutrients. United States Patent 6,290,274.
    • (2001)
    • Swaisgood, H.E.1
  • 212
    • 0002772383 scopus 로고    scopus 로고
    • Chemistry of the caseins
    • Kluwer Academic/Plenum Publishers, New York, NY, P.F. Fox, P.L.H. McSweeney (Eds.)
    • Swaisgood H.E. Chemistry of the caseins. Advanced Dairy Chemistry-Proteins 2003, 139-201. Kluwer Academic/Plenum Publishers, New York, NY. third ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Advanced Dairy Chemistry-Proteins , pp. 139-201
    • Swaisgood, H.E.1
  • 213
    • 0014959664 scopus 로고
    • Amino acid sequence adjoining the lone tryptophan of human serum albumin. A binding site of the protein
    • Swaney J.B., Klotz I.M. Amino acid sequence adjoining the lone tryptophan of human serum albumin. A binding site of the protein. Biochem. J. 1970, 9:2570-2574.
    • (1970) Biochem. J. , vol.9 , pp. 2570-2574
    • Swaney, J.B.1    Klotz, I.M.2
  • 214
    • 51649095462 scopus 로고    scopus 로고
    • β-Lactoglobulin structure and retinol binding changes in presence of anionic and neutral detergents
    • Taheri-Kafrani A., Bordbar A.-K., Mousavi S.H.-A., Haertle T. β-Lactoglobulin structure and retinol binding changes in presence of anionic and neutral detergents. J. Agric. Food Chem. 2008, 56:7528-7534.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 7528-7534
    • Taheri-Kafrani, A.1    Bordbar, A.-K.2    Mousavi, S.H.-A.3    Haertle, T.4
  • 215
    • 23744432029 scopus 로고    scopus 로고
    • Measurement of the kinetics of protein unfolding in viscous systems and implications for protein stability in freeze-drying
    • Tang X., Pikal M.J. Measurement of the kinetics of protein unfolding in viscous systems and implications for protein stability in freeze-drying. Pharm. Res. 2005, 22:1176-1185.
    • (2005) Pharm. Res. , vol.22 , pp. 1176-1185
    • Tang, X.1    Pikal, M.J.2
  • 216
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak-interactions with water-how do solvents affect these processes
    • Timasheff S.N. The control of protein stability and association by weak-interactions with water-how do solvents affect these processes. Annu. Rev. Biophys. Biomol. Struct. 1993, 22:67-97.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 217
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated
    • Timasheff S.N. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 1998, 51:355-432.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 218
    • 0037137253 scopus 로고    scopus 로고
    • Protein hydration, thermodynamic binding, and preferential hydration
    • Timasheff S.N. Protein hydration, thermodynamic binding, and preferential hydration. Biochemistry 2002, 41:13473-13482.
    • (2002) Biochemistry , vol.41 , pp. 13473-13482
    • Timasheff, S.N.1
  • 219
    • 33750185683 scopus 로고    scopus 로고
    • Stabilization of yeast hexokinase A by polyol osmolytes: correlation with the physicochemical properties of aqueous solutions
    • Tiwari A., Bhat R. Stabilization of yeast hexokinase A by polyol osmolytes: correlation with the physicochemical properties of aqueous solutions. Biophys. Chem. 2006, 124:90-99.
    • (2006) Biophys. Chem. , vol.124 , pp. 90-99
    • Tiwari, A.1    Bhat, R.2
  • 220
    • 0011783672 scopus 로고
    • Antioxidant effects of protein-bound riboflavin and free riboflavin
    • Toyosaki T., Mineshita T. Antioxidant effects of protein-bound riboflavin and free riboflavin. J. Food Sci. 1988, 53:1851-1853.
    • (1988) J. Food Sci. , vol.53 , pp. 1851-1853
    • Toyosaki, T.1    Mineshita, T.2
  • 221
    • 0016365852 scopus 로고
    • Drug interactions. 1. Binding of ascorbic-acid and fatty-acid ascorbyl esters to bovine serum-albumin
    • Tukamoto T., Ozeki S., Hattori F., Ishida T. Drug interactions. 1. Binding of ascorbic-acid and fatty-acid ascorbyl esters to bovine serum-albumin. Chem. Pharm. Bull. 1974, 22:385-389.
    • (1974) Chem. Pharm. Bull. , vol.22 , pp. 385-389
    • Tukamoto, T.1    Ozeki, S.2    Hattori, F.3    Ishida, T.4
  • 222
    • 84865452727 scopus 로고    scopus 로고
    • Thermal stability of the iron-lactoferrin complex in aqueous solution is improved by soluble soybean polysaccharide
    • Ueno H.M., Ueda N., Morita M., Kakehi Y., Kobayashi T. Thermal stability of the iron-lactoferrin complex in aqueous solution is improved by soluble soybean polysaccharide. Food Biophys. 2012, 7:183-189.
    • (2012) Food Biophys. , vol.7 , pp. 183-189
    • Ueno, H.M.1    Ueda, N.2    Morita, M.3    Kakehi, Y.4    Kobayashi, T.5
  • 223
    • 0036306701 scopus 로고    scopus 로고
    • Influence of composition and structure of oil-in-water emulsions on retention of aroma compounds
    • van Ruth S.M., de Vries G., Geary M., Giannouli P. Influence of composition and structure of oil-in-water emulsions on retention of aroma compounds. J. Sci. Food Agric. 2002, 82:1028-1035.
    • (2002) J. Sci. Food Agric. , vol.82 , pp. 1028-1035
    • van Ruth, S.M.1    de Vries, G.2    Geary, M.3    Giannouli, P.4
  • 224
    • 0034492053 scopus 로고    scopus 로고
    • Mineral-binding milk proteins and peptides; occurrence, biochemical and technological characteristics
    • Vegarud G.E., Langsrud T., Svenning C. Mineral-binding milk proteins and peptides; occurrence, biochemical and technological characteristics. Br. J. Nutr. 2000, 84(Suppl. 1):S91-S98.
    • (2000) Br. J. Nutr. , vol.84 , pp. S91-S98
    • Vegarud, G.E.1    Langsrud, T.2    Svenning, C.3
  • 225
    • 36549015809 scopus 로고    scopus 로고
    • Unfolding kinetics of β-lactoglobulin induced by surfactant and denaturant: a stopped-flow/fluorescence study
    • Viseu M.I., Melo E.P., Carvalho T.I., Correia R.F., Costa S.M.B. Unfolding kinetics of β-lactoglobulin induced by surfactant and denaturant: a stopped-flow/fluorescence study. Biophys. J. 2007, 93:3601-3612.
    • (2007) Biophys. J. , vol.93 , pp. 3601-3612
    • Viseu, M.I.1    Melo, E.P.2    Carvalho, T.I.3    Correia, R.F.4    Costa, S.M.B.5
  • 226
  • 227
    • 0031160713 scopus 로고    scopus 로고
    • Binding of retinoids to β-lactoglobulin isolated by bioselective adsorption
    • Wang Q.W., Allen J.C., Swaisgood H.E. Binding of retinoids to β-lactoglobulin isolated by bioselective adsorption. J. Dairy Sci. 1997, 80:1047-1053.
    • (1997) J. Dairy Sci. , vol.80 , pp. 1047-1053
    • Wang, Q.W.1    Allen, J.C.2    Swaisgood, H.E.3
  • 228
    • 85094105377 scopus 로고    scopus 로고
    • Binding of vitamin D and cholesterol to β-lactoglobulin
    • Wang Q.W., Allen J.C., Swaisgood H.E. Binding of vitamin D and cholesterol to β-lactoglobulin. J. Dairy Sci. 1997, 82:257-264.
    • (1997) J. Dairy Sci. , vol.82 , pp. 257-264
    • Wang, Q.W.1    Allen, J.C.2    Swaisgood, H.E.3
  • 229
    • 0033071880 scopus 로고    scopus 로고
    • Binding of lipophilic nutrients to β-lactoglobulin prepared by bioselective adsorption
    • Wang Q., Allen J.C., Swaisgood H.E. Binding of lipophilic nutrients to β-lactoglobulin prepared by bioselective adsorption. J. Dairy Sci. 1999, 82:257-264.
    • (1999) J. Dairy Sci. , vol.82 , pp. 257-264
    • Wang, Q.1    Allen, J.C.2    Swaisgood, H.E.3
  • 230
    • 79959976470 scopus 로고    scopus 로고
    • Preparation and characteristics of yak casein hydrolysate-iron complex
    • Wang X., Li M., Li M., Mao X., Zhou J., Ren F. Preparation and characteristics of yak casein hydrolysate-iron complex. Int. J. Food Sci. Technol. 2011, 46:1705-1710.
    • (2011) Int. J. Food Sci. Technol. , vol.46 , pp. 1705-1710
    • Wang, X.1    Li, M.2    Li, M.3    Mao, X.4    Zhou, J.5    Ren, F.6
  • 231
    • 0031999031 scopus 로고    scopus 로고
    • Binding of sodium dodecyl sulphate and dodecyl trimethyl ammonium chloride to β-lactoglobulin: a calorimetric study
    • Waninge R., Paulsson M., Nylander T., Ninham B., Sellers P. Binding of sodium dodecyl sulphate and dodecyl trimethyl ammonium chloride to β-lactoglobulin: a calorimetric study. Int. Dairy J. 1998, 8:141-148.
    • (1998) Int. Dairy J. , vol.8 , pp. 141-148
    • Waninge, R.1    Paulsson, M.2    Nylander, T.3    Ninham, B.4    Sellers, P.5
  • 232
    • 0027032801 scopus 로고
    • Bioactivity of cis and dicis isomers of vitamin A esters
    • Weiser H., Somorjai G. Bioactivity of cis and dicis isomers of vitamin A esters. Int. J. Vitam. Nutr. Res. 1992, 62:201-208.
    • (1992) Int. J. Vitam. Nutr. Res. , vol.62 , pp. 201-208
    • Weiser, H.1    Somorjai, G.2
  • 233
    • 4644335636 scopus 로고    scopus 로고
    • Reduced protein adsorption at solid interfaces by sugar excipients
    • Wendorf J.R., Radke C.J., Blanch H.W. Reduced protein adsorption at solid interfaces by sugar excipients. Biotechnol. Bioeng. 2004, 87:565-573.
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 565-573
    • Wendorf, J.R.1    Radke, C.J.2    Blanch, H.W.3
  • 234
    • 0345313659 scopus 로고    scopus 로고
    • β-Lactoglobulin binds palmitate within its central cavity
    • Wu S.Y., Perez M.D., Puyol P., Sawyer L. β-Lactoglobulin binds palmitate within its central cavity. J. Biol. Chem. 1999, 274:170-174.
    • (1999) J. Biol. Chem. , vol.274 , pp. 170-174
    • Wu, S.Y.1    Perez, M.D.2    Puyol, P.3    Sawyer, L.4
  • 235
    • 80052793160 scopus 로고    scopus 로고
    • Analysis of binding interaction between (-)-epigallocatechin (EGC) and β-lactoglobulin by multi-spectroscopic method
    • Wu X., Wu H., Liu M., Liu Z., Xu H., Lai F. Analysis of binding interaction between (-)-epigallocatechin (EGC) and β-lactoglobulin by multi-spectroscopic method. Spectrochim. Acta A 2011, 82:164-168.
    • (2011) Spectrochim. Acta A , vol.82 , pp. 164-168
    • Wu, X.1    Wu, H.2    Liu, M.3    Liu, Z.4    Xu, H.5    Lai, F.6
  • 236
    • 84872275671 scopus 로고    scopus 로고
    • Studies on the interaction of -epigallocatechin-3-gallate from green tea with bovine β-lactoglobulin by spectroscopic methods and docking
    • Wu X., Dey R., Wu H., Liu Z., He Q., Zeng X. Studies on the interaction of -epigallocatechin-3-gallate from green tea with bovine β-lactoglobulin by spectroscopic methods and docking. Int. J. Dairy Technol. 2013, 66:7-13.
    • (2013) Int. J. Dairy Technol. , vol.66 , pp. 7-13
    • Wu, X.1    Dey, R.2    Wu, H.3    Liu, Z.4    He, Q.5    Zeng, X.6
  • 237
    • 0030973690 scopus 로고    scopus 로고
    • The thermodynamic mechanism of protein stabilization by trehalose
    • Xie G., Timasheff S.N. The thermodynamic mechanism of protein stabilization by trehalose. Biophys. Chem. 1997, 64:25-43.
    • (1997) Biophys. Chem. , vol.64 , pp. 25-43
    • Xie, G.1    Timasheff, S.N.2
  • 238
    • 0031013887 scopus 로고    scopus 로고
    • Mechanism of the stabilization of ribonuclease A by sorbitol: preferential hydration is greater for the denatured than for the native protein
    • Xie G.F., Timasheff S.N. Mechanism of the stabilization of ribonuclease A by sorbitol: preferential hydration is greater for the denatured than for the native protein. Protein Sci. 1997, 6:211-221.
    • (1997) Protein Sci. , vol.6 , pp. 211-221
    • Xie, G.F.1    Timasheff, S.N.2
  • 239
    • 84882843632 scopus 로고    scopus 로고
    • Milk enhances intestinal absorption of green tea catechins in in vitro digestion/Caco-2 cells model
    • Xie Y., Kosińska A., Xu H., Andlauer W. Milk enhances intestinal absorption of green tea catechins in in vitro digestion/Caco-2 cells model. Food Res. Int. 2013, 53:793-800.
    • (2013) Food Res. Int. , vol.53 , pp. 793-800
    • Xie, Y.1    Kosińska, A.2    Xu, H.3    Andlauer, W.4
  • 241
    • 84940531108 scopus 로고    scopus 로고
    • Factors affecting the interactions between beta-lactoglobulin and fatty acids as revealed in molecular dynamics simulations
    • Yi C., Wambo T.O. Factors affecting the interactions between beta-lactoglobulin and fatty acids as revealed in molecular dynamics simulations. Phys. Chem. Chem. Phys. 2015, 17:23074-23080.
    • (2015) Phys. Chem. Chem. Phys. , vol.17 , pp. 23074-23080
    • Yi, C.1    Wambo, T.O.2
  • 242
    • 85052823935 scopus 로고    scopus 로고
    • Interactions between milk proteins and polyphenols: binding mechanisms, related changes, and the future trends in the dairy industry
    • Yildirim-Elikoglu S., Erdem Y.K. Interactions between milk proteins and polyphenols: binding mechanisms, related changes, and the future trends in the dairy industry. Food Rev. Intl. 2018, 34:665-697.
    • (2018) Food Rev. Intl. , vol.34 , pp. 665-697
    • Yildirim-Elikoglu, S.1    Erdem, Y.K.2
  • 243
    • 85029692896 scopus 로고    scopus 로고
    • Characteristics of the interaction mechanism between tannic acid and sodium caseinate using multispectroscopic and thermodynamics methods
    • Zhan F., Yang J., Li J., Wang Y., Li B. Characteristics of the interaction mechanism between tannic acid and sodium caseinate using multispectroscopic and thermodynamics methods. Food Hydrocoll. 2018, 75:81-87.
    • (2018) Food Hydrocoll. , vol.75 , pp. 81-87
    • Zhan, F.1    Yang, J.2    Li, J.3    Wang, Y.4    Li, B.5
  • 244
    • 84875333731 scopus 로고    scopus 로고
    • Encapsulation of bixin in sodium caseinate to deliver the colorant in transparent dispersions
    • Zhang Y., Zhong Q. Encapsulation of bixin in sodium caseinate to deliver the colorant in transparent dispersions. Food Hydrocoll. 2013, 33:1-9.
    • (2013) Food Hydrocoll. , vol.33 , pp. 1-9
    • Zhang, Y.1    Zhong, Q.2
  • 245
    • 84875943100 scopus 로고    scopus 로고
    • Probing the binding between norbixin and dairy proteins by spectroscopy methods
    • Zhang Y., Zhong Q. Probing the binding between norbixin and dairy proteins by spectroscopy methods. Food Chem. 2013, 139:611-616.
    • (2013) Food Chem. , vol.139 , pp. 611-616
    • Zhang, Y.1    Zhong, Q.2
  • 248
    • 84864060915 scopus 로고    scopus 로고
    • Preparation and characterization of β-lactoglobulin hydrolysate-iron complexes
    • Zhou J., Wang X., Ai T., Cheng X., Guo H.Y., Teng G.X., Mao X.Y. Preparation and characterization of β-lactoglobulin hydrolysate-iron complexes. J. Dairy Sci. 2012, 95:4230-4236.
    • (2012) J. Dairy Sci. , vol.95 , pp. 4230-4236
    • Zhou, J.1    Wang, X.2    Ai, T.3    Cheng, X.4    Guo, H.Y.5    Teng, G.X.6    Mao, X.Y.7
  • 249
    • 33746338463 scopus 로고    scopus 로고
    • Institute of Food, Nutrition and Human Health, Massey University, Palmerston North, New Zealand
    • Zhu X.Q. Interactions Between Flavour Compounds and Milk Proteins 2003, Institute of Food, Nutrition and Human Health, Massey University, Palmerston North, New Zealand.
    • (2003) Interactions Between Flavour Compounds and Milk Proteins
    • Zhu, X.Q.1
  • 250
    • 79952539269 scopus 로고    scopus 로고
    • Re-assembled casein micelles and casein nanoparticles as nano-vehicles for ω-3 polyunsaturated fatty acids
    • Zimet P., Rosenberg D., Livney Y.D. Re-assembled casein micelles and casein nanoparticles as nano-vehicles for ω-3 polyunsaturated fatty acids. Food Hydrocoll. 2011, 25:1270-1276.
    • (2011) Food Hydrocoll. , vol.25 , pp. 1270-1276
    • Zimet, P.1    Rosenberg, D.2    Livney, Y.D.3
  • 251
    • 0037024342 scopus 로고    scopus 로고
    • Induced chirality upon binding of cis-parinaric acid to bovine β-lactoglobulin: spectroscopic characterization of the complex
    • Zsila F., Imre T., Szabó P.T., Bikádi Z., Simonyi M. Induced chirality upon binding of cis-parinaric acid to bovine β-lactoglobulin: spectroscopic characterization of the complex. FEBS Lett. 2002, 520:81-87.
    • (2002) FEBS Lett. , vol.520 , pp. 81-87
    • Zsila, F.1    Imre, T.2    Szabó, P.T.3    Bikádi, Z.4    Simonyi, M.5
  • 252
    • 30544433324 scopus 로고    scopus 로고
    • Binding of the pepper alkaloid piperine to bovine β-lactoglobulin: circular dichroism spectroscopy and molecular modeling study
    • Zsila F., Hazai E., Sawyer L. Binding of the pepper alkaloid piperine to bovine β-lactoglobulin: circular dichroism spectroscopy and molecular modeling study. J. Agric. Food Chem. 2005, 53:10179-10185.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 10179-10185
    • Zsila, F.1    Hazai, E.2    Sawyer, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.