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Volumn 232, Issue , 2017, Pages 697-703

Formation of lactoferrin/sodium caseinate complexes and their adsorption behaviour at the air/water interface

Author keywords

Heat stability; Interfacial tension; Lactoferrin; Sodium caseinate; Turbidity; Zeta potential

Indexed keywords

FOOD TECHNOLOGY; PHYSICAL CHEMISTRY; SURFACE TENSION; TURBIDITY; ZETA POTENTIAL;

EID: 85017622322     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2017.04.072     Document Type: Article
Times cited : (35)

References (34)
  • 1
    • 77958468107 scopus 로고    scopus 로고
    • Characterization of lactoferrin oil-in-water emulsions and their stability in recombined milk
    • Acero-Lopez, A., Schell, P., Corredig, M., Alexander, M., Characterization of lactoferrin oil-in-water emulsions and their stability in recombined milk. Journal of Dairy Research 77 (2010), 445–451.
    • (2010) Journal of Dairy Research , vol.77 , pp. 445-451
    • Acero-Lopez, A.1    Schell, P.2    Corredig, M.3    Alexander, M.4
  • 2
    • 84863832439 scopus 로고    scopus 로고
    • Lactoferrin binding to transglutaminase cross-linked casein micelles
    • Anema, S.G., De Kruif, C.G., Lactoferrin binding to transglutaminase cross-linked casein micelles. International Dairy Journal 26 (2012), 83–87.
    • (2012) International Dairy Journal , vol.26 , pp. 83-87
    • Anema, S.G.1    De Kruif, C.G.2
  • 3
    • 84859298220 scopus 로고    scopus 로고
    • Co-acervates of lactoferrin and caseins
    • Anema, S.G., De Kruif, C.G., Co-acervates of lactoferrin and caseins. Soft Matter, 8, 2012, 4471.
    • (2012) Soft Matter , vol.8 , pp. 4471
    • Anema, S.G.1    De Kruif, C.G.2
  • 4
    • 84880851921 scopus 로고    scopus 로고
    • Protein composition of different sized casein micelles in milk after the binding of lactoferrin or lysozyme
    • Anema, S.G., De Kruif, C.G., Protein composition of different sized casein micelles in milk after the binding of lactoferrin or lysozyme. Journal of Agriculture and Food Chemistry 61 (2013), 7142–7149.
    • (2013) Journal of Agriculture and Food Chemistry , vol.61 , pp. 7142-7149
    • Anema, S.G.1    De Kruif, C.G.2
  • 5
    • 0036880244 scopus 로고    scopus 로고
    • Dilatational elasticity moduli of water-crude oil interfaces using the oscillating pendant drop
    • Aske, N., Orr, R., Sjoblom, J., Dilatational elasticity moduli of water-crude oil interfaces using the oscillating pendant drop. Journal of Dispersion Science and Technology 23 (2002), 809–825.
    • (2002) Journal of Dispersion Science and Technology , vol.23 , pp. 809-825
    • Aske, N.1    Orr, R.2    Sjoblom, J.3
  • 6
    • 79952538805 scopus 로고    scopus 로고
    • Formation and characterization of lactoferrin/pectin electrostatic complexes: Impact of composition, pH and thermal treatment
    • Bengoechea, C., Jones, O.G., Guerrero, A., McClements, D.J., Formation and characterization of lactoferrin/pectin electrostatic complexes: Impact of composition, pH and thermal treatment. Food Hydrocolloids 25 (2011), 1227–1232.
    • (2011) Food Hydrocolloids , vol.25 , pp. 1227-1232
    • Bengoechea, C.1    Jones, O.G.2    Guerrero, A.3    McClements, D.J.4
  • 7
    • 84879486580 scopus 로고    scopus 로고
    • Physico-chemical properties of different forms of bovine lactoferrin
    • Bokkhim, H., Bansal, N., Grondahl, L., Bhandari, B., Physico-chemical properties of different forms of bovine lactoferrin. Food Chemistry 141 (2013), 3007–3013.
    • (2013) Food Chemistry , vol.141 , pp. 3007-3013
    • Bokkhim, H.1    Bansal, N.2    Grondahl, L.3    Bhandari, B.4
  • 8
    • 33847030648 scopus 로고    scopus 로고
    • Heat-induced aggregation of bovine lactoferrin at neutral pH: Effect of iron saturation
    • Brisson, G., Britten, M., Pouliot, Y., Heat-induced aggregation of bovine lactoferrin at neutral pH: Effect of iron saturation. International Dairy Journal 17 (2007), 617–624.
    • (2007) International Dairy Journal , vol.17 , pp. 617-624
    • Brisson, G.1    Britten, M.2    Pouliot, Y.3
  • 10
    • 84862647834 scopus 로고    scopus 로고
    • The structure of the casein micelle of milk and its changes during processing
    • Dalgleish, D.G., Corredig, M., The structure of the casein micelle of milk and its changes during processing. Annual Review of Food Science and Technology 3 (2012), 449–467.
    • (2012) Annual Review of Food Science and Technology , vol.3 , pp. 449-467
    • Dalgleish, D.G.1    Corredig, M.2
  • 14
    • 0031568202 scopus 로고    scopus 로고
    • Creaming and flocculation of oil-in-water emulsions containing sodium caseinate
    • Dickson, E., Golding, M., Povey, M.J.W., Creaming and flocculation of oil-in-water emulsions containing sodium caseinate. Journal of Colloid and Interface Science 185 (1997), 515–529.
    • (1997) Journal of Colloid and Interface Science , vol.185 , pp. 515-529
    • Dickson, E.1    Golding, M.2    Povey, M.J.W.3
  • 15
    • 0029899693 scopus 로고    scopus 로고
    • Real time pendant drop tensiometer using image processing with interfacial area and interfacial tension control capabilities
    • Faour, G., Grimaldi, M., Richou, J., Bois, A., Real time pendant drop tensiometer using image processing with interfacial area and interfacial tension control capabilities. Journal of Colloid and Interface Science 181 (1996), 385–392.
    • (1996) Journal of Colloid and Interface Science , vol.181 , pp. 385-392
    • Faour, G.1    Grimaldi, M.2    Richou, J.3    Bois, A.4
  • 16
    • 25844500998 scopus 로고    scopus 로고
    • Factors determining the physical properties of protein foams
    • Foegeding, E.A., Luck, P.J., Davis, J.P., Factors determining the physical properties of protein foams. Food Hydrocollods 20 (2006), 284–292.
    • (2006) Food Hydrocollods , vol.20 , pp. 284-292
    • Foegeding, E.A.1    Luck, P.J.2    Davis, J.P.3
  • 17
    • 84859395433 scopus 로고    scopus 로고
    • Interactions at the interface between hydrophobic and hydrophilic emulsifiers : Polyglycerol polyricinoleate (PGPR) and milk proteins, studied by drop shape tensiometry
    • Gülseren, I., Corredig, M., Interactions at the interface between hydrophobic and hydrophilic emulsifiers : Polyglycerol polyricinoleate (PGPR) and milk proteins, studied by drop shape tensiometry. Food Hydrocolloids 29 (2012), 193–198.
    • (2012) Food Hydrocolloids , vol.29 , pp. 193-198
    • Gülseren, I.1    Corredig, M.2
  • 18
    • 84865452727 scopus 로고    scopus 로고
    • Thermal Stability of the iron-lactoferrin complex in aqueous solution is improved by soluble soybean polysaccharide
    • Hiroshi, 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 Biophysics 7 (2012), 183–189.
    • (2012) Food Biophysics , vol.7 , pp. 183-189
    • Hiroshi, M.1    Ueda, N.2    Morita, M.3    Kakehi, Y.4    Kobayashi, T.5
  • 19
    • 34447632834 scopus 로고    scopus 로고
    • Formation of hydrogel particles by thermal treatment of β-lactoglobulin-chitosan complexes
    • Hong, Y.H., McClements, D.J., Formation of hydrogel particles by thermal treatment of β-lactoglobulin-chitosan complexes. Journal of Agricultural and Food Chemistry 55 (2007), 5653–5660.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 5653-5660
    • Hong, Y.H.1    McClements, D.J.2
  • 20
    • 84958955693 scopus 로고    scopus 로고
    • Conjugation of polyphenols prevents lactoferrin from thermal aggregation at neutral pH
    • Liu, F., Wang, D., Ma, C., Gao, Y., Conjugation of polyphenols prevents lactoferrin from thermal aggregation at neutral pH. Food Hydrocolloids 58 (2016), 49–59.
    • (2016) Food Hydrocolloids , vol.58 , pp. 49-59
    • Liu, F.1    Wang, D.2    Ma, C.3    Gao, Y.4
  • 21
    • 0036403301 scopus 로고    scopus 로고
    • Network forming properties of various proteins adsorbed at the air/water interface in relation to foam stability
    • Martin, A.H., Grolle, K., Bos, M.A., Cohen Stuart, M.A., van Vliet, T., Network forming properties of various proteins adsorbed at the air/water interface in relation to foam stability. Journal of Colloid and Interface Science 254 (2002), 175–183.
    • (2002) Journal of Colloid and Interface Science , vol.254 , pp. 175-183
    • Martin, A.H.1    Grolle, K.2    Bos, M.A.3    Cohen Stuart, M.A.4    van Vliet, T.5
  • 22
    • 84863443527 scopus 로고    scopus 로고
    • Interfacial rheology: an overview of measuring techniques and its role in dispersions and electrospinning
    • Pelipenko, J., Kristl, J., Rošic, R., Baumgartner, S., Kocbek, P., Interfacial rheology: an overview of measuring techniques and its role in dispersions and electrospinning. Acta Pharmacologica Sinica 62 (2012), 123–140.
    • (2012) Acta Pharmacologica Sinica , vol.62 , pp. 123-140
    • Pelipenko, J.1    Kristl, J.2    Rošic, R.3    Baumgartner, S.4    Kocbek, P.5
  • 24
    • 84961626007 scopus 로고    scopus 로고
    • Impact on morphological characterization and emulsion stability of lactoferrin–beet pectin electrostatic complexes
    • Su, J., He, X., Guo, Z., Jian, J., Gao, Y., Yuan, F., Impact on morphological characterization and emulsion stability of lactoferrin–beet pectin electrostatic complexes. Journal of Dispersion Science and Technology 37 (2015), 927–940.
    • (2015) Journal of Dispersion Science and Technology , vol.37 , pp. 927-940
    • Su, J.1    He, X.2    Guo, Z.3    Jian, J.4    Gao, Y.5    Yuan, F.6
  • 25
    • 32944475467 scopus 로고    scopus 로고
    • Influence of pH and pectin type on properties and stability of sodium-caseinate stabilized oil-in-water emulsions
    • Surh, J., Decker, E.A., Mcclements, D.J., Influence of pH and pectin type on properties and stability of sodium-caseinate stabilized oil-in-water emulsions. Food Hydrocolloids 20 (2006), 607–618.
    • (2006) Food Hydrocolloids , vol.20 , pp. 607-618
    • Surh, J.1    Decker, E.A.2    Mcclements, D.J.3
  • 27
    • 2142776684 scopus 로고    scopus 로고
    • On the mechanism of stabilisation of acidified milk drinks by pectin
    • Tromp, R., de Kruif, C.G., van Eijk, M., Rolin, C., On the mechanism of stabilisation of acidified milk drinks by pectin. Food Hydrocolloids 18 (2008), 565–572.
    • (2008) Food Hydrocolloids , vol.18 , pp. 565-572
    • Tromp, R.1    de Kruif, C.G.2    van Eijk, M.3    Rolin, C.4
  • 28
    • 18844398622 scopus 로고    scopus 로고
    • Interfacial dilatational elasticity and viscosity of β-lactoglobulin at air-water interface using pulsating bubble tensiometry
    • Wang, Z., Narsimhan, G., Interfacial dilatational elasticity and viscosity of β-lactoglobulin at air-water interface using pulsating bubble tensiometry. Langmuir 21 (2005), 4482–4489.
    • (2005) Langmuir , vol.21 , pp. 4482-4489
    • Wang, Z.1    Narsimhan, G.2
  • 30
    • 67349118128 scopus 로고    scopus 로고
    • Thermodynamic characterization of the interactions between the immunoregulatory proteins osteopontin and lactoferrin
    • Yamniuk, A.P., Burling, H., Vogel, H.J., Thermodynamic characterization of the interactions between the immunoregulatory proteins osteopontin and lactoferrin. Molecular Immunology 46 (2009), 2395–2402.
    • (2009) Molecular Immunology , vol.46 , pp. 2395-2402
    • Yamniuk, A.P.1    Burling, H.2    Vogel, H.J.3
  • 31
    • 84861575610 scopus 로고    scopus 로고
    • Formation of interfacial milk protein complexation to stabilize oil-in-water emulsions against calcium
    • Ye, A., Lo, J., Singh, H., Formation of interfacial milk protein complexation to stabilize oil-in-water emulsions against calcium. Journal of Colloid and Interface Science 378 (2012), 184–190.
    • (2012) Journal of Colloid and Interface Science , vol.378 , pp. 184-190
    • Ye, A.1    Lo, J.2    Singh, H.3
  • 32
    • 36549043509 scopus 로고    scopus 로고
    • Formation of multilayers at the interface of oil-in-water emulsion via interactions between lactoferrin and β-lactoglobulin
    • Ye, A., Singh, H., Formation of multilayers at the interface of oil-in-water emulsion via interactions between lactoferrin and β-lactoglobulin. Food Biophysics 2 (2007), 125–132.
    • (2007) Food Biophysics , vol.2 , pp. 125-132
    • Ye, A.1    Singh, H.2
  • 33
    • 1642361351 scopus 로고    scopus 로고
    • Preparation and release behaviour of carboxymethylated chitosan/alginate microspheres encapsulating bovine serum albumin
    • Zhang, L., Guo, J., Peng, X., Li, Y., Preparation and release behaviour of carboxymethylated chitosan/alginate microspheres encapsulating bovine serum albumin. Journal of Applied Polymer Science 92 (2004), 878–882.
    • (2004) Journal of Applied Polymer Science , vol.92 , pp. 878-882
    • Zhang, L.1    Guo, J.2    Peng, X.3    Li, Y.4
  • 34
    • 84982921652 scopus 로고    scopus 로고
    • Effect of chitosan on the heat stability of whey protein solution as a function of pH
    • Zhao, Z., Xiao, Q., Effect of chitosan on the heat stability of whey protein solution as a function of pH. Journal of the scienceof the food and agriculture, 2016, 10.1002/jsfa.7904.
    • (2016) Journal of the scienceof the food and agriculture
    • Zhao, Z.1    Xiao, Q.2


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