메뉴 건너뛰기




Volumn 516, Issue , 2017, Pages 286-295

Evaluation of structural characteristics determining surface and foaming properties of β-lactoglobulin aggregates

Author keywords

Foaming properties; Heat induced aggregation; pH; Surface charge; Surface properties; Lactoglobulin

Indexed keywords

AGGREGATES; PARTICLE SIZE; PH; SURFACE CHARGE;

EID: 85007504751     PISSN: 09277757     EISSN: 18734359     Source Type: Journal    
DOI: 10.1016/j.colsurfa.2016.12.045     Document Type: Article
Times cited : (59)

References (47)
  • 1
    • 79956272091 scopus 로고    scopus 로고
    • The composition of interfacial material from skim milk foams
    • [1] Kamath, S., Webb, R., Deeth, H., The composition of interfacial material from skim milk foams. J. Dairy Sci. 94 (2011), 2707–2718.
    • (2011) J. Dairy Sci. , vol.94 , pp. 2707-2718
    • Kamath, S.1    Webb, R.2    Deeth, H.3
  • 2
    • 66149125594 scopus 로고    scopus 로고
    • Effect of protein content, casein-whey protein ratio and pH value on the foaming properties of skimmed milk
    • [2] Borcherding, K., Lorenzen, P.C., Hoffmann, W., Effect of protein content, casein-whey protein ratio and pH value on the foaming properties of skimmed milk. Int. J. Dairy Technol. 62 (2009), 161–169.
    • (2009) Int. J. Dairy Technol. , vol.62 , pp. 161-169
    • Borcherding, K.1    Lorenzen, P.C.2    Hoffmann, W.3
  • 3
    • 67349238149 scopus 로고    scopus 로고
    • Physico-chemical factors controlling the foamability and foam stability of milk proteins: sodium caseinate and whey protein concentrates
    • [3] Marinova, K.G., Basheva, E.S., Nenova, B., Temelska, M., Mirarefi, A.Y., Campbell, B., Ivanov, I.B., Physico-chemical factors controlling the foamability and foam stability of milk proteins: sodium caseinate and whey protein concentrates. Food Hydrocoll. 23 (2009), 1864–1876.
    • (2009) Food Hydrocoll. , vol.23 , pp. 1864-1876
    • Marinova, K.G.1    Basheva, E.S.2    Nenova, B.3    Temelska, M.4    Mirarefi, A.Y.5    Campbell, B.6    Ivanov, I.B.7
  • 4
    • 3142571046 scopus 로고    scopus 로고
    • Foaming and interfacial properties of polymerized whey protein isolate
    • [4] Davis, J.P., Foegeding, E.A., Foaming and interfacial properties of polymerized whey protein isolate. J. Food Sci. 69 (2004), C404–C410.
    • (2004) J. Food Sci. , vol.69 , pp. C404-C410
    • Davis, J.P.1    Foegeding, E.A.2
  • 6
    • 84974055115 scopus 로고
    • Surface properties of the bovine casein components: relationships between structure and foaming properties
    • [6] Lorient, D., Closs, B., Courthaudon, J.-L., Surface properties of the bovine casein components: relationships between structure and foaming properties. J. Dairy Res. 56 (1989), 495–502.
    • (1989) J. Dairy Res. , vol.56 , pp. 495-502
    • Lorient, D.1    Closs, B.2    Courthaudon, J.-L.3
  • 7
    • 84965113836 scopus 로고    scopus 로고
    • Identification of critical concentrations determining foam ability and stability of β-lactoglobulin
    • [7] Lech, F.J., Delahaije, R.J.B.M., Meinders, M.B.J., Gruppen, H., Wierenga, P.A., Identification of critical concentrations determining foam ability and stability of β-lactoglobulin. Food Hydrocoll. 57 (2016), 46–54.
    • (2016) Food Hydrocoll. , vol.57 , pp. 46-54
    • Lech, F.J.1    Delahaije, R.J.B.M.2    Meinders, M.B.J.3    Gruppen, H.4    Wierenga, P.A.5
  • 8
    • 84884232301 scopus 로고    scopus 로고
    • pH Effects on the molecular structure of β-lactoglobulin modified air-water interfaces and its impact on foam rheology
    • [8] Engelhardt, K., Lexis, M., Gochev, G., Konnerth, C., Miller, R., Willenbacher, N., Peukert, W., Braunschweig, B., pH Effects on the molecular structure of β-lactoglobulin modified air-water interfaces and its impact on foam rheology. Langmuir 29 (2013), 11646–11655.
    • (2013) Langmuir , vol.29 , pp. 11646-11655
    • Engelhardt, K.1    Lexis, M.2    Gochev, G.3    Konnerth, C.4    Miller, R.5    Willenbacher, N.6    Peukert, W.7    Braunschweig, B.8
  • 9
    • 84907055626 scopus 로고    scopus 로고
    • Electrostatic stabilization of foam films from β-Lactoglobulin solutions
    • [9] Gochev, G., Retzlaff, I., Exerowa, D., Miller, R., Electrostatic stabilization of foam films from β-Lactoglobulin solutions. Coll. Surf. A 460 (2014), 272–279.
    • (2014) Coll. Surf. A , vol.460 , pp. 272-279
    • Gochev, G.1    Retzlaff, I.2    Exerowa, D.3    Miller, R.4
  • 10
    • 84973480997 scopus 로고    scopus 로고
    • Correlation between bulk characteristics of aggregated β-lactoglobulin and its surface and foaming properties
    • [10] Dombrowski, J., Johler, F., Warncke, M., Kulozik, U., Correlation between bulk characteristics of aggregated β-lactoglobulin and its surface and foaming properties. Food Hydrocoll. 61 (2016), 318–328.
    • (2016) Food Hydrocoll. , vol.61 , pp. 318-328
    • Dombrowski, J.1    Johler, F.2    Warncke, M.3    Kulozik, U.4
  • 11
    • 79952534829 scopus 로고    scopus 로고
    • Effects of heat-treated á-lactoglobulin and its aggregates on foaming properties
    • [11] Moro, A., Báez, G.D., Busti, P.A., Ballerini, G.A., Delorenzi, N.J., Effects of heat-treated á-lactoglobulin and its aggregates on foaming properties. Food Hydrocoll. 25 (2011), 1009–1015.
    • (2011) Food Hydrocoll. , vol.25 , pp. 1009-1015
    • Moro, A.1    Báez, G.D.2    Busti, P.A.3    Ballerini, G.A.4    Delorenzi, N.J.5
  • 12
    • 74449092339 scopus 로고    scopus 로고
    • β-Lactoglobulin aggregates in foam films: effect of the concentration and size of the protein aggregates
    • [12] Rullier, B., Axelos, M.A.V., Langevin, D., Novales, B., β-Lactoglobulin aggregates in foam films: effect of the concentration and size of the protein aggregates. J. Colloid Interface Sci. 343 (2010), 330–337.
    • (2010) J. Colloid Interface Sci. , vol.343 , pp. 330-337
    • Rullier, B.1    Axelos, M.A.V.2    Langevin, D.3    Novales, B.4
  • 13
    • 54149089640 scopus 로고    scopus 로고
    • Effect of protein aggregates on foaming properties of β-lactoglobulin
    • [13] Rullier, B., Novales, B., Axelos, M.A.V., Effect of protein aggregates on foaming properties of β-lactoglobulin. Coll. Surf. A 330 (2008), 96–102.
    • (2008) Coll. Surf. A , vol.330 , pp. 96-102
    • Rullier, B.1    Novales, B.2    Axelos, M.A.V.3
  • 15
    • 84914665340 scopus 로고    scopus 로고
    • Pickering stabilization of foams and emulsions with particles of biological origin
    • [15] Lam, S., Velikov, K., Velev, O., Pickering stabilization of foams and emulsions with particles of biological origin. Curr. Opin. Colloid Interface Sci. 19 (2014), 490–500.
    • (2014) Curr. Opin. Colloid Interface Sci. , vol.19 , pp. 490-500
    • Lam, S.1    Velikov, K.2    Velev, O.3
  • 16
    • 84896689195 scopus 로고    scopus 로고
    • Bulk self-aggregation drives foam stabilization properties of whey protein microgels
    • [16] Schmitt, C., Bovay, C., Rouvet, M., Bulk self-aggregation drives foam stabilization properties of whey protein microgels. Food Hydrocoll. 42 (2014), 139–148.
    • (2014) Food Hydrocoll. , vol.42 , pp. 139-148
    • Schmitt, C.1    Bovay, C.2    Rouvet, M.3
  • 17
    • 75849137203 scopus 로고    scopus 로고
    • Food emulsions and foams: stabilization by particles
    • [17] Dickinson, E., Food emulsions and foams: stabilization by particles. Curr. Opin. Colloid Interface Sci. 15 (2010), 40–49.
    • (2010) Curr. Opin. Colloid Interface Sci. , vol.15 , pp. 40-49
    • Dickinson, E.1
  • 18
    • 77649188797 scopus 로고    scopus 로고
    • Self-similar assemblies of globular whey proteins at the air–water interface: effect of the structure
    • [18] Mahmoudi, N., Gaillard, C., Boué, F., Axelos, M.A.V., Riaublanc, A., Self-similar assemblies of globular whey proteins at the air–water interface: effect of the structure. J. Colloid Interface Sci. 345 (2010), 54–63.
    • (2010) J. Colloid Interface Sci. , vol.345 , pp. 54-63
    • Mahmoudi, N.1    Gaillard, C.2    Boué, F.3    Axelos, M.A.V.4    Riaublanc, A.5
  • 19
    • 34247360046 scopus 로고    scopus 로고
    • Whey protein soluble aggregates from heating with NaCl: physicochemical, interfacial, and foaming properties
    • [19] Schmitt, C., Bovay, C., Rouvet, M., Shojaei-Rami, S., Kolodziejczyk, E., Whey protein soluble aggregates from heating with NaCl: physicochemical, interfacial, and foaming properties. Langmuir 23 (2007), 4155–4166.
    • (2007) Langmuir , vol.23 , pp. 4155-4166
    • Schmitt, C.1    Bovay, C.2    Rouvet, M.3    Shojaei-Rami, S.4    Kolodziejczyk, E.5
  • 21
    • 43049114185 scopus 로고    scopus 로고
    • Foams and foam films stabilised by solid particles
    • [21] Horozov, T.S., Foams and foam films stabilised by solid particles. Curr. Opin. Colloid Interface Sci. 13 (2008), 134–140.
    • (2008) Curr. Opin. Colloid Interface Sci. , vol.13 , pp. 134-140
    • Horozov, T.S.1
  • 22
    • 33745446411 scopus 로고    scopus 로고
    • On the equation of the maximum capillary pressure induced by solid particles to stabilize emulsions and foams and on the emulsion stability diagrams
    • [22] Kaptay, G., On the equation of the maximum capillary pressure induced by solid particles to stabilize emulsions and foams and on the emulsion stability diagrams. Coll. Surf. A 282–283 (2006), 387–401.
    • (2006) Coll. Surf. A , vol.282-283 , pp. 387-401
    • Kaptay, G.1
  • 23
    • 0036267602 scopus 로고    scopus 로고
    • Particles as surfactants – similarities and differences
    • [23] Binks, B.P., Particles as surfactants – similarities and differences. Curr. Opin. Colloid Interface Sci. 7 (2002), 21–41.
    • (2002) Curr. Opin. Colloid Interface Sci. , vol.7 , pp. 21-41
    • Binks, B.P.1
  • 24
    • 80051532786 scopus 로고    scopus 로고
    • Influence of microgel architecture and oil polarity on stabilization of emulsions by stimuli-sensitive core-shell Poly(N-isopropylacrylamideco-methacrylic acid) microgels: mickering versus pickering behavior?
    • [24] Schmidt, S., Liu, T., Rütten, S., Phan, K.-H., Möller, M., Richtering, W., Influence of microgel architecture and oil polarity on stabilization of emulsions by stimuli-sensitive core-shell Poly(N-isopropylacrylamideco-methacrylic acid) microgels: mickering versus pickering behavior?. Langmuir 27 (2011), 9801–9806.
    • (2011) Langmuir , vol.27 , pp. 9801-9806
    • Schmidt, S.1    Liu, T.2    Rütten, S.3    Phan, K.-H.4    Möller, M.5    Richtering, W.6
  • 25
    • 84928824139 scopus 로고    scopus 로고
    • Microgels – an alternative colloidal ingredient for stabilization of food emulsions
    • [25] Dickinson, E., Microgels – an alternative colloidal ingredient for stabilization of food emulsions. Trend Food Sci. Technol. 43 (2015), 178–188.
    • (2015) Trend Food Sci. Technol. , vol.43 , pp. 178-188
    • Dickinson, E.1
  • 26
    • 67649243772 scopus 로고    scopus 로고
    • β-Lactoglobulin aggregates in foam films: correlation between foam films and foaming properties
    • [26] Rullier, B., Axelos, M.A.V., Langevin, D., Novales, B., β-Lactoglobulin aggregates in foam films: correlation between foam films and foaming properties. J. Colloid Interface Sci. 336 (2009), 750–755.
    • (2009) J. Colloid Interface Sci. , vol.336 , pp. 750-755
    • Rullier, B.1    Axelos, M.A.V.2    Langevin, D.3    Novales, B.4
  • 27
    • 25144518570 scopus 로고    scopus 로고
    • Effect of thermal treatment on interfacial properties of β-lactoglobulin
    • [27] Kim, D.A., Cornec, M., Narsimhan, G., Effect of thermal treatment on interfacial properties of β-lactoglobulin. J. Colloid Interface Sci. 285 (2005), 100–109.
    • (2005) J. Colloid Interface Sci. , vol.285 , pp. 100-109
    • Kim, D.A.1    Cornec, M.2    Narsimhan, G.3
  • 28
    • 84874513386 scopus 로고    scopus 로고
    • Fractionation of α-lactalbumin and β-lactoglobulin from whey protein isolate using selective thermal aggregation, an optimized membrane separation procedure and resolubilization techniques at pilot plant scale
    • [28] Toro-Sierra, J., Tolkach, A., Kulozik, U., Fractionation of α-lactalbumin and β-lactoglobulin from whey protein isolate using selective thermal aggregation, an optimized membrane separation procedure and resolubilization techniques at pilot plant scale. Food Bioprocess Technol. 6:4 (2013), 1032–1043.
    • (2013) Food Bioprocess Technol. , vol.6 , Issue.4 , pp. 1032-1043
    • Toro-Sierra, J.1    Tolkach, A.2    Kulozik, U.3
  • 29
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a flourescence probe method and its correlation with surface properties of proteins
    • [29] Kato, A., Nakai, S., Hydrophobicity determined by a flourescence probe method and its correlation with surface properties of proteins. Biochim. Biophys. Acta 624:1 (1980), 13–20.
    • (1980) Biochim. Biophys. Acta , vol.624 , Issue.1 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 30
    • 84956602918 scopus 로고    scopus 로고
    • Multiscale approach to characterize bulk, surface and foaming behavior of casein micelles as a function of alkalinisation
    • [30] Dombrowski, J., Dechau, J., Kulozik, U., Multiscale approach to characterize bulk, surface and foaming behavior of casein micelles as a function of alkalinisation. Food Hydrocoll. 57 (2016), 92–102.
    • (2016) Food Hydrocoll. , vol.57 , pp. 92-102
    • Dombrowski, J.1    Dechau, J.2    Kulozik, U.3
  • 31
    • 84911897774 scopus 로고    scopus 로고
    • Relating foam and interfacial rheological properties of β-lactoglobulin solutions
    • [31] Lexis, M., Willenbacher, N., Relating foam and interfacial rheological properties of β-lactoglobulin solutions. Soft Matter. 48:10 (2014), 9626–9636.
    • (2014) Soft Matter. , vol.48 , Issue.10 , pp. 9626-9636
    • Lexis, M.1    Willenbacher, N.2
  • 33
    • 0642298935 scopus 로고
    • Dynamic measurements of dilational properties of a liquid interface
    • [33] Lucassen, J., van den Tempel, M., Dynamic measurements of dilational properties of a liquid interface. Chem. Eng. Sci. 27 (1972), 1283–1291.
    • (1972) Chem. Eng. Sci. , vol.27 , pp. 1283-1291
    • Lucassen, J.1    van den Tempel, M.2
  • 34
    • 84907051965 scopus 로고    scopus 로고
    • Temperature effect on foamability, foam stability, and foam structure of milk
    • [34] Oetjen, K., Bilke-Krause, C., Madani, M., Willers, T., Temperature effect on foamability, foam stability, and foam structure of milk. Coll. Surf. A 460:20 (2014), 280–285.
    • (2014) Coll. Surf. A , vol.460 , Issue.20 , pp. 280-285
    • Oetjen, K.1    Bilke-Krause, C.2    Madani, M.3    Willers, T.4
  • 36
    • 0028569153 scopus 로고
    • Protein denaturation with guanidinium hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • [36] Monera, O.D., Kay, C.M., Hodges, R.S., Protein denaturation with guanidinium hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3 (1994), 1984–1991.
    • (1994) Protein Sci. , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 37
    • 45849084663 scopus 로고    scopus 로고
    • Urea and guanidinium chloride denature protein L in different ways in molecular dynamics simulations
    • [37] Camilloni, C., Guerini Rocco, A., Eberini, I., Gianazza, E., Broglia, R.A., Tiana, G., Urea and guanidinium chloride denature protein L in different ways in molecular dynamics simulations. Biophys. J. 94 (2008), 4654–4661.
    • (2008) Biophys. J. , vol.94 , pp. 4654-4661
    • Camilloni, C.1    Guerini Rocco, A.2    Eberini, I.3    Gianazza, E.4    Broglia, R.A.5    Tiana, G.6
  • 38
    • 77956131588 scopus 로고    scopus 로고
    • Kinetics of formation and physicochemical characterization of thermally-induced ú-lactoglobulin aggregates
    • [38] Zúñiga, R.N., Tolkach, A., Kulozik, U., Aguilera, J.M., Kinetics of formation and physicochemical characterization of thermally-induced ú-lactoglobulin aggregates. J. Food Sci., 75(5), 2010, E261.
    • (2010) J. Food Sci. , vol.75 , Issue.5 , pp. E261
    • Zúñiga, R.N.1    Tolkach, A.2    Kulozik, U.3    Aguilera, J.M.4
  • 39
    • 0142216171 scopus 로고    scopus 로고
    • Protein exposed hydrophobicity reduces the kinetic barrier for adsorption of ovalbumin to the air–water interface
    • [39] Wierenga, P.A., Meinders, M.B.J., Egmond, M.R., Voragen, F.A.G.J., de Jongh, H.H.J., Protein exposed hydrophobicity reduces the kinetic barrier for adsorption of ovalbumin to the air–water interface. Langmuir 19 (2003), 8964–8970.
    • (2003) Langmuir , vol.19 , pp. 8964-8970
    • Wierenga, P.A.1    Meinders, M.B.J.2    Egmond, M.R.3    Voragen, F.A.G.J.4    de Jongh, H.H.J.5
  • 40
    • 0023934323 scopus 로고
    • Kinetics of adsorption of proteins at interfaces: role of protein conformation in diffusional adsorption
    • [40] Damodaran, S., Song, K.B., Kinetics of adsorption of proteins at interfaces: role of protein conformation in diffusional adsorption. Biochim. Biophys. Acta 954 (1988), 253–264.
    • (1988) Biochim. Biophys. Acta , vol.954 , pp. 253-264
    • Damodaran, S.1    Song, K.B.2
  • 41
    • 25444511609 scopus 로고    scopus 로고
    • Quantitative description of the relation between protein net charge and protein adsorption to air-water interfaces
    • [41] Wierenga, P.A., Meinders, M.B.J., Egmond, M.R., Voragen, A.G.J., de Jongh, H.H.J., Quantitative description of the relation between protein net charge and protein adsorption to air-water interfaces. J. Phys. Chem. B 109 (2005), 16946–16952.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 16946-16952
    • Wierenga, P.A.1    Meinders, M.B.J.2    Egmond, M.R.3    Voragen, A.G.J.4    de Jongh, H.H.J.5
  • 42
    • 1242283892 scopus 로고    scopus 로고
    • Electrostatic effects on the yield stress of whey protein isolate foams
    • [42] Davis, J.P., Foegeding, E.A., Hansen, F.K., Electrostatic effects on the yield stress of whey protein isolate foams. Colloids Surf. B: Biointerfaces 34 (2004), 13–23.
    • (2004) Colloids Surf. B: Biointerfaces , vol.34 , pp. 13-23
    • Davis, J.P.1    Foegeding, E.A.2    Hansen, F.K.3
  • 43
    • 84906306142 scopus 로고    scopus 로고
    • Biomass-based particles for the formulation of Pickering type emulsions in food and topical applications
    • [43] Rayner, M., Marku, D., Eriksson, M., Sjöö, M., Dejmek, P., Wahlgren, M., Biomass-based particles for the formulation of Pickering type emulsions in food and topical applications. Coll. Surf. A 458 (2014), 48–62.
    • (2014) Coll. Surf. A , vol.458 , pp. 48-62
    • Rayner, M.1    Marku, D.2    Eriksson, M.3    Sjöö, M.4    Dejmek, P.5    Wahlgren, M.6
  • 44
    • 84979032209 scopus 로고    scopus 로고
    • Correlation between surface activity and foaming properties of individual milk proteins in dependence of solvent composition
    • [44] Dombrowski, J., Mattejat, C., Kulozik, U., Correlation between surface activity and foaming properties of individual milk proteins in dependence of solvent composition. Int. Dairy J. 61 (2016), 166–175.
    • (2016) Int. Dairy J. , vol.61 , pp. 166-175
    • Dombrowski, J.1    Mattejat, C.2    Kulozik, U.3
  • 45
    • 0032395999 scopus 로고    scopus 로고
    • Characterisation of foam properties using image analysis
    • [45] Sarker, D.K., Bertrand, D., Chtioui, Y., Popineau, Y., Characterisation of foam properties using image analysis. J. Texture Stud. 29:1 (1998), 15–42.
    • (1998) J. Texture Stud. , vol.29 , Issue.1 , pp. 15-42
    • Sarker, D.K.1    Bertrand, D.2    Chtioui, Y.3    Popineau, Y.4
  • 46
    • 0003587106 scopus 로고    scopus 로고
    • Interfaces and Colloids. Principles and Applications
    • 2nd ed. John Wiley & Sons, Inc New York
    • [46] Myers, D., Surfaces, Interfaces and Colloids. Principles and Applications. 2nd ed., 1999, John Wiley & Sons, Inc, New York.
    • (1999)
    • Myers, D.1    Surfaces2
  • 47
    • 84954965877 scopus 로고
    • Emulsifying and structural properties of β-lactoglobulin at different pHs
    • [47] Shimizu, M., Saito, M., Yamauchi, K., Emulsifying and structural properties of β-lactoglobulin at different pHs. Agric. Biol. Chem. 49:1 (1985), 189–194.
    • (1985) Agric. Biol. Chem. , vol.49 , Issue.1 , pp. 189-194
    • Shimizu, M.1    Saito, M.2    Yamauchi, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.