메뉴 건너뛰기




Volumn 518, Issue , 2017, Pages 46-56

Mixtures of Quillaja saponin and beta-lactoglobulin at the oil/water-interface: Adsorption, interfacial rheology and emulsion properties

Author keywords

Aggregation; Emulsion; Flocculation; Interfacial rheology; Lissajous plot; Protein surfactant interaction

Indexed keywords

AGGLOMERATION; BINARY MIXTURES; DROPS; EMULSIFICATION; EMULSIONS; FLOCCULATION; INTERFACES (MATERIALS); METABOLITES; MIXTURES; SHEAR FLOW;

EID: 85009160437     PISSN: 09277757     EISSN: 18734359     Source Type: Journal    
DOI: 10.1016/j.colsurfa.2016.12.041     Document Type: Article
Times cited : (64)

References (55)
  • 1
    • 33846219958 scopus 로고    scopus 로고
    • Saponins, classification and occurrence in the plant kingdom
    • [1] Vincken, J.-P., Heng, L., de Groot, A., Gruppen, H., Saponins, classification and occurrence in the plant kingdom. Phytochemistry 68:3 (2007), 275–297.
    • (2007) Phytochemistry , vol.68 , Issue.3 , pp. 275-297
    • Vincken, J.-P.1    Heng, L.2    de Groot, A.3    Gruppen, H.4
  • 2
    • 33947415314 scopus 로고    scopus 로고
    • Saponins: properties, applications and processing
    • [2] Güçlü-Üstündağ, Ö., Mazza, G., Saponins: properties, applications and processing. Crit. Rev. Food Sci. Nutr. 47:3 (2007), 231–258.
    • (2007) Crit. Rev. Food Sci. Nutr. , vol.47 , Issue.3 , pp. 231-258
    • Güçlü-Üstündağ, Ö.1    Mazza, G.2
  • 3
    • 84896540119 scopus 로고    scopus 로고
    • Characterization of quillaja bark extracts and evaluation of their purity using liquid chromatography–high resolution mass spectrometry
    • [3] Thalhamer, B., Himmelsbach, M., Characterization of quillaja bark extracts and evaluation of their purity using liquid chromatography–high resolution mass spectrometry. Phytochem. Lett. 8 (2014), 97–100.
    • (2014) Phytochem. Lett. , vol.8 , pp. 97-100
    • Thalhamer, B.1    Himmelsbach, M.2
  • 4
    • 84855552984 scopus 로고    scopus 로고
    • Electrospray ionization ion-trap multiple-stage mass spectrometry of Quillaja saponins
    • [4] Bankefors, J., Broberg, S., Nord, L.I., Kenne, L., Electrospray ionization ion-trap multiple-stage mass spectrometry of Quillaja saponins. J. Mass Spectrom. 46:7 (2011), 658–665.
    • (2011) J. Mass Spectrom. , vol.46 , Issue.7 , pp. 658-665
    • Bankefors, J.1    Broberg, S.2    Nord, L.I.3    Kenne, L.4
  • 5
    • 74349085109 scopus 로고    scopus 로고
    • Multidimensional profiling of components in complex mixtures of natural products for metabolic analysis, proof of concept: application to Quillaja saponins
    • [5] Bankefors, J., Nord, L.I., Kenne, L., Multidimensional profiling of components in complex mixtures of natural products for metabolic analysis, proof of concept: application to Quillaja saponins. J. Chromatogr. B 878:3–4 (2010), 471–476.
    • (2010) J. Chromatogr. B , vol.878 , Issue.3-4 , pp. 471-476
    • Bankefors, J.1    Nord, L.I.2    Kenne, L.3
  • 6
    • 84875626935 scopus 로고    scopus 로고
    • Surface activity of saponin from Quillaja bark at the air/water and oil/water interfaces
    • [6] Wojciechowski, K., Surface activity of saponin from Quillaja bark at the air/water and oil/water interfaces. Colloids Surf. B: Biointerfaces 108 (2013), 95–102.
    • (2013) Colloids Surf. B: Biointerfaces , vol.108 , pp. 95-102
    • Wojciechowski, K.1
  • 7
    • 84923260941 scopus 로고    scopus 로고
    • Phenolic constituents in commercial aqueous quillaja (Quillaja saponaria molina) wood extracts
    • [7] Maier, C., Conrad, J., Carle, R., Weiss, J., Schweiggert, R.M., Phenolic constituents in commercial aqueous quillaja (Quillaja saponaria molina) wood extracts. J. Agric. Food Chem. 63:6 (2015), 1756–1762.
    • (2015) J. Agric. Food Chem. , vol.63 , Issue.6 , pp. 1756-1762
    • Maier, C.1    Conrad, J.2    Carle, R.3    Weiss, J.4    Schweiggert, R.M.5
  • 8
    • 84865511899 scopus 로고    scopus 로고
    • Surface shear rheology of saponin adsorption layers
    • [8] Golemanov, K., Tcholakova, S., Denkov, N., Pelan, E., Stoyanov, S.D., Surface shear rheology of saponin adsorption layers. Langmuir 28:33 (2012), 12071–12084.
    • (2012) Langmuir , vol.28 , Issue.33 , pp. 12071-12084
    • Golemanov, K.1    Tcholakova, S.2    Denkov, N.3    Pelan, E.4    Stoyanov, S.D.5
  • 10
    • 84979518928 scopus 로고    scopus 로고
    • Mixtures of saponins and beta-lactoglobulin differ from classical protein/surfactant-systems at the air-water interface
    • [10] Böttcher, S., Scampicchio, M., Drusch, S., Mixtures of saponins and beta-lactoglobulin differ from classical protein/surfactant-systems at the air-water interface. Colloids Surf. A: Physicochem. Eng. Aspects 506 (2016), 765–773.
    • (2016) Colloids Surf. A: Physicochem. Eng. Aspects , vol.506 , pp. 765-773
    • Böttcher, S.1    Scampicchio, M.2    Drusch, S.3
  • 11
    • 0035958458 scopus 로고    scopus 로고
    • Interfacial rheological properties of adsorbed protein layers and surfactants: a review
    • [11] Bos, M.A., van Vliet, T., Interfacial rheological properties of adsorbed protein layers and surfactants: a review. Adv. Colloid Interface Sci. 91:3 (2001), 437–471.
    • (2001) Adv. Colloid Interface Sci. , vol.91 , Issue.3 , pp. 437-471
    • Bos, M.A.1    van Vliet, T.2
  • 12
    • 84906663403 scopus 로고    scopus 로고
    • The role of the hydrophobic phase in the unique rheological properties of saponin adsorption layers
    • [12] Golemanov, K., Tcholakova, S., Denkov, N., Pelan, E., Stoyanov, S.D., The role of the hydrophobic phase in the unique rheological properties of saponin adsorption layers. Soft Matter 10 (2014), 7034–7044.
    • (2014) Soft Matter , vol.10 , pp. 7034-7044
    • Golemanov, K.1    Tcholakova, S.2    Denkov, N.3    Pelan, E.4    Stoyanov, S.D.5
  • 14
    • 84944323735 scopus 로고    scopus 로고
    • Formation, optical property and stability of orange oil nanoemulsions stabilized by Quallija saponins
    • [14] Zhang, J., Bing, L., Reineccius, G.A., Formation, optical property and stability of orange oil nanoemulsions stabilized by Quallija saponins. LWT—Food Sci. Technol. 64:2 (2015), 1063–1070.
    • (2015) LWT—Food Sci. Technol. , vol.64 , Issue.2 , pp. 1063-1070
    • Zhang, J.1    Bing, L.2    Reineccius, G.A.3
  • 15
    • 84936870889 scopus 로고    scopus 로고
    • Comparison of modified starch and Quillaja saponins in the formation and stabilization of flavor nanoemulsions
    • [15] Zhang, J., Bing, L., Reineccius, G.A., Comparison of modified starch and Quillaja saponins in the formation and stabilization of flavor nanoemulsions. Food Chem. 192 (2016), 53–59.
    • (2016) Food Chem. , vol.192 , pp. 53-59
    • Zhang, J.1    Bing, L.2    Reineccius, G.A.3
  • 16
    • 0004269862 scopus 로고    scopus 로고
    • Coupling of coalescence and flocculation in dilute O/W emulsions
    • J. Sjöblom Marc Dekker New York, Basel
    • [16] Dukhin, S., Saezther, O., Sjöblom, J., Coupling of coalescence and flocculation in dilute O/W emulsions. Sjöblom, J., (eds.) Encyclopedic Handbook of Emulsion Technology, 2001, Marc Dekker, New York, Basel.
    • (2001) Encyclopedic Handbook of Emulsion Technology
    • Dukhin, S.1    Saezther, O.2    Sjöblom, J.3
  • 17
    • 79955087652 scopus 로고    scopus 로고
    • Elucidation of the binding sites of sodium dodecyl sulfate to β-lactoglobulin using hydrogen/deuterium exchange mass spectrometry combined with docking simulation
    • [17] Hu, W., Liu, J., Luo, Q., Han, Y., Wu, K., Lv, S., Xiong, S., Wang, F., Elucidation of the binding sites of sodium dodecyl sulfate to β-lactoglobulin using hydrogen/deuterium exchange mass spectrometry combined with docking simulation. Rapid Commun. Mass Spectrom. 25:10 (2011), 1429–1436.
    • (2011) Rapid Commun. Mass Spectrom. , vol.25 , Issue.10 , pp. 1429-1436
    • Hu, W.1    Liu, J.2    Luo, Q.3    Han, Y.4    Wu, K.5    Lv, S.6    Xiong, S.7    Wang, F.8
  • 19
    • 42149100435 scopus 로고    scopus 로고
    • Microscopy, microstructure and displacement of proteins from interfaces: implications for food quality and digestion
    • p. 943
    • [19] Morris, V.J., Gunning, A.P., Microscopy, microstructure and displacement of proteins from interfaces: implications for food quality and digestion. Soft Matter, 4(5), 2008 p. 943.
    • (2008) Soft Matter , vol.4 , Issue.5
    • Morris, V.J.1    Gunning, A.P.2
  • 20
    • 84940001807 scopus 로고    scopus 로고
    • Tensiometry and dilational rheology of mixed (-lactoglobulin/ionic surfactant adsorption layers at water/air and water/hexane interfaces
    • [20] Da, A., Gochev, G., Miller, R., Tensiometry and dilational rheology of mixed (-lactoglobulin/ionic surfactant adsorption layers at water/air and water/hexane interfaces. J. Colloid Interface Sci. 449 (2015), 383–391.
    • (2015) J. Colloid Interface Sci. , vol.449 , pp. 383-391
    • Da, A.1    Gochev, G.2    Miller, R.3
  • 21
    • 33750516080 scopus 로고    scopus 로고
    • Reversibility and irreversibility of adsorption of surfactants and proteins at liquid interfaces
    • [21] Fainerman, V.B., Miller, R., Ferri, J.K., Watzke, H., Leser, M.E., Michel, M., Reversibility and irreversibility of adsorption of surfactants and proteins at liquid interfaces. Adv. Colloid Interface Sci. 123–126 (2006), 163–171.
    • (2006) Adv. Colloid Interface Sci. , vol.123-126 , pp. 163-171
    • Fainerman, V.B.1    Miller, R.2    Ferri, J.K.3    Watzke, H.4    Leser, M.E.5    Michel, M.6
  • 23
    • 84867103434 scopus 로고    scopus 로고
    • Adsorption and shear rheology of β-lactoglobulin/SDS mixtures at water/hexane and water/MCT interfaces
    • [23] Ulaganathan, V., Bergenstahl, B., Krägel, J., Miller, R., Adsorption and shear rheology of β-lactoglobulin/SDS mixtures at water/hexane and water/MCT interfaces. Colloids Surf. A: Physicochem. Eng. Aspects 413 (2012), 136–141.
    • (2012) Colloids Surf. A: Physicochem. Eng. Aspects , vol.413 , pp. 136-141
    • Ulaganathan, V.1    Bergenstahl, B.2    Krägel, J.3    Miller, R.4
  • 25
    • 54249154546 scopus 로고    scopus 로고
    • Interfacial shear rheology of protein–surfactant layers
    • [25] Krägel, J., Derkatch, S.R., Miller, R., Interfacial shear rheology of protein–surfactant layers. Adv. Colloid Interface Sci. 144:1–2 (2008), 38–53.
    • (2008) Adv. Colloid Interface Sci. , vol.144 , Issue.1-2 , pp. 38-53
    • Krägel, J.1    Derkatch, S.R.2    Miller, R.3
  • 26
    • 84860271228 scopus 로고    scopus 로고
    • Biosurfactant–protein mixtures: Quillaja bark saponin at water/air and water/oil interfaces in presence of β-lactoglobulin
    • [26] Piotrowski, M., Lewandowska, J., Wojciechowski, K., Biosurfactant–protein mixtures: Quillaja bark saponin at water/air and water/oil interfaces in presence of β-lactoglobulin. J. Phys. Chem. B 116:16 (2012), 4843–4850.
    • (2012) J. Phys. Chem. B , vol.116 , Issue.16 , pp. 4843-4850
    • Piotrowski, M.1    Lewandowska, J.2    Wojciechowski, K.3
  • 27
    • 84973662325 scopus 로고    scopus 로고
    • Molecular dynamics simulation of β-lactoglobulin at different oil/water interfaces
    • [27] Zare, D., Allison, J.R., McGrath, K.M., Molecular dynamics simulation of β-lactoglobulin at different oil/water interfaces. Biomacromolecules 17:5 (2016), 1572–1581.
    • (2016) Biomacromolecules , vol.17 , Issue.5 , pp. 1572-1581
    • Zare, D.1    Allison, J.R.2    McGrath, K.M.3
  • 29
    • 84899946156 scopus 로고    scopus 로고
    • Characterization of the covalent binding of allyl isothiocyanate to β-lactoglobulin by fluorescence quenching, equilibrium measurement, and mass spectrometry
    • [29] Keppler, J.K., Koudelka, T., Palani, K., Stuhldreier, M.C., Temps, F., Tholey, A., Schwarz, K., Characterization of the covalent binding of allyl isothiocyanate to β-lactoglobulin by fluorescence quenching, equilibrium measurement, and mass spectrometry. J. Biomol. Struct. Dyn. 32:7 (2014), 1103–1117, 10.1080/07391102.2013.809605.
    • (2014) J. Biomol. Struct. Dyn. , vol.32 , Issue.7 , pp. 1103-1117
    • Keppler, J.K.1    Koudelka, T.2    Palani, K.3    Stuhldreier, M.C.4    Temps, F.5    Tholey, A.6    Schwarz, K.7
  • 31
    • 84982217591 scopus 로고    scopus 로고
    • Impact of enzymatic hydrolysis on the interfacial rheology of whey protein/pectin interfacial layers at the oil/water-interface
    • [31] Tamm, F., Drusch, S., Impact of enzymatic hydrolysis on the interfacial rheology of whey protein/pectin interfacial layers at the oil/water-interface. Food Hydrocoll. 63 (2017), 8–18.
    • (2017) Food Hydrocoll. , vol.63 , pp. 8-18
    • Tamm, F.1    Drusch, S.2
  • 32
    • 84926251183 scopus 로고    scopus 로고
    • Nonlinear rheology of complex fluid?fluid interfaces
    • [32] Sagis, L.M., Fischer, P., Nonlinear rheology of complex fluid?fluid interfaces. Curr. Opin. Colloid Interface Sci. 19:6 (2014), 520–529.
    • (2014) Curr. Opin. Colloid Interface Sci. , vol.19 , Issue.6 , pp. 520-529
    • Sagis, L.M.1    Fischer, P.2
  • 33
    • 56049098182 scopus 로고    scopus 로고
    • New measures for characterizing nonlinear viscoelasticity in large amplitude oscillatory shear
    • [33] Ewoldt, R.H., Hosoi, A.E., McKinley, G.H., New measures for characterizing nonlinear viscoelasticity in large amplitude oscillatory shear. J. Rheol., 52(6), 2008, 1427.
    • (2008) J. Rheol. , vol.52 , Issue.6 , pp. 1427
    • Ewoldt, R.H.1    Hosoi, A.E.2    McKinley, G.H.3
  • 34
    • 84884799934 scopus 로고    scopus 로고
    • Non-linear surface dilatational rheology as a tool for understanding microstructures of air/water interfaces stabilized by oligofructose fatty acid esters
    • p. 9579
    • [34] van Kempen, Silvia E.H.J., Schols, H.A., van der Linden, Erik, Sagis, Leonard M.C., Non-linear surface dilatational rheology as a tool for understanding microstructures of air/water interfaces stabilized by oligofructose fatty acid esters. Soft Matter, 9, 2013, 40 p. 9579.
    • (2013) Soft Matter , vol.9 , pp. 40
    • van Kempen, S.E.H.J.1    Schols, H.A.2    van der Linden, E.3    Sagis, L.M.C.4
  • 37
    • 9144241823 scopus 로고    scopus 로고
    • Shear and dilatational relaxation mechanisms of globular and flexible proteins at the hexadecane/water interface
    • [37] Freer, E.M., Yim, K.S., Fuller, G.G., Radke, C.J., Shear and dilatational relaxation mechanisms of globular and flexible proteins at the hexadecane/water interface. Langmuir 20:23 (2004), 10159–10167, 10.1021/la0485226.
    • (2004) Langmuir , vol.20 , Issue.23 , pp. 10159-10167
    • Freer, E.M.1    Yim, K.S.2    Fuller, G.G.3    Radke, C.J.4
  • 38
    • 84966311919 scopus 로고    scopus 로고
    • Nonlinear surface dilatational rheology and foaming behavior of protein and protein fibrillar aggregates in the presence of natural surfactant
    • [38] Wan, Z., Yang, X., Sagis, Leonard M.C., Nonlinear surface dilatational rheology and foaming behavior of protein and protein fibrillar aggregates in the presence of natural surfactant. Langmuir 32:15 (2016), 3679–3690.
    • (2016) Langmuir , vol.32 , Issue.15 , pp. 3679-3690
    • Wan, Z.1    Yang, X.2    Sagis, L.M.C.3
  • 39
    • 36849122851 scopus 로고
    • Time-dependence of boundary tensions of solutions I. The role of diffusion in time-Effects
    • p. 453
    • [39] Ward, A.F.H., Tordai, L., Time-dependence of boundary tensions of solutions I. The role of diffusion in time-Effects. J. Chem. Phys., 14(7), 1946 p. 453.
    • (1946) J. Chem. Phys. , vol.14 , Issue.7
    • Ward, A.F.H.1    Tordai, L.2
  • 40
    • 84901038631 scopus 로고    scopus 로고
    • Influence of mathematical models and correction factors on binding results of polyphenols and retinol with β-lactoglobulin measured with fluorescence quenching
    • [40] Keppler, J.K., Stuhldreier, M.C., Temps, F., Schwarz, K., Influence of mathematical models and correction factors on binding results of polyphenols and retinol with β-lactoglobulin measured with fluorescence quenching. Food Biophys. 9:2 (2014), 158–168, 10.1007/s11483-013-9328-x.
    • (2014) Food Biophys. , vol.9 , Issue.2 , pp. 158-168
    • Keppler, J.K.1    Stuhldreier, M.C.2    Temps, F.3    Schwarz, K.4
  • 41
    • 84957433669 scopus 로고    scopus 로고
    • Interfacial properties of saponin extracts and their impact on foam characteristics
    • [41] Böttcher, S., Drusch, S., Interfacial properties of saponin extracts and their impact on foam characteristics. Food Biophys. 11:1 (2016), 91–100.
    • (2016) Food Biophys. , vol.11 , Issue.1 , pp. 91-100
    • Böttcher, S.1    Drusch, S.2
  • 42
    • 0035824880 scopus 로고    scopus 로고
    • Characterization of pH-induced transitions of β-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies
    • [42] Taulier, N., Chalikian, T.V., Characterization of pH-induced transitions of β-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies. J. Mol. Biol. 314:4 (2001), 873–889.
    • (2001) J. Mol. Biol. , vol.314 , Issue.4 , pp. 873-889
    • Taulier, N.1    Chalikian, T.V.2
  • 43
    • 0042463114 scopus 로고    scopus 로고
    • Physical Chemistry of Foods
    • Marcel Dekker New York
    • [43] Walstra, P., Physical Chemistry of Foods. 2003, Marcel Dekker, New York.
    • (2003)
    • Walstra, P.1
  • 44
    • 0038309868 scopus 로고    scopus 로고
    • Physico-chemical stability of colloidal lipid particles
    • [44] Heurtault, B., Saulnier, P., Pech, B., Proust, J.-E., Benoit, J.-P., Physico-chemical stability of colloidal lipid particles. Biomaterials 24:23 (2003), 4283–4300.
    • (2003) Biomaterials , vol.24 , Issue.23 , pp. 4283-4300
    • Heurtault, B.1    Saulnier, P.2    Pech, B.3    Proust, J.-E.4    Benoit, J.-P.5
  • 45
    • 84978544503 scopus 로고    scopus 로고
    • Fabrication of oil-in-water nanoemulsions by dual-channel microfluidization using natural emulsifiers: saponins, phospholipids, proteins, and polysaccharides
    • [45] Bai, L., Huan, S., Gu, J., McClements, D.J., Fabrication of oil-in-water nanoemulsions by dual-channel microfluidization using natural emulsifiers: saponins, phospholipids, proteins, and polysaccharides. Food Hydrocoll. 61 (2016), 703–711.
    • (2016) Food Hydrocoll. , vol.61 , pp. 703-711
    • Bai, L.1    Huan, S.2    Gu, J.3    McClements, D.J.4
  • 46
    • 84949599577 scopus 로고    scopus 로고
    • Formulation of saponin stabilized nanoemulsion by ultrasonic method and its role to protect the degradation of quercitin from UV light
    • [46] Kaur, K., Kumar, R., Mehta, S.K., Formulation of saponin stabilized nanoemulsion by ultrasonic method and its role to protect the degradation of quercitin from UV light. Ultrason. Sonochem. 31 (2016), 29–38.
    • (2016) Ultrason. Sonochem. , vol.31 , pp. 29-38
    • Kaur, K.1    Kumar, R.2    Mehta, S.K.3
  • 47
    • 84939624826 scopus 로고    scopus 로고
    • Cross-linking oppositely charged oil-in-water emulsions to enhance heteroaggregate stability
    • [47] Maier, C., Oechsle, A.M., Weiss, J., Cross-linking oppositely charged oil-in-water emulsions to enhance heteroaggregate stability. Colloids Surf. B: Biointerfaces 135 (2015), 525–532.
    • (2015) Colloids Surf. B: Biointerfaces , vol.135 , pp. 525-532
    • Maier, C.1    Oechsle, A.M.2    Weiss, J.3
  • 48
    • 84994048503 scopus 로고    scopus 로고
    • Composition of Quillaja saponin extract affects lipid oxidation in oil-in-water emulsions
    • [48] Tippel, J., Gies, K., Harbaum-Piayda, B., Steffen-Heins, A., Drusch, S., Composition of Quillaja saponin extract affects lipid oxidation in oil-in-water emulsions. Food Chem. 221 (2017), 386–394.
    • (2017) Food Chem. , vol.221 , pp. 386-394
    • Tippel, J.1    Gies, K.2    Harbaum-Piayda, B.3    Steffen-Heins, A.4    Drusch, S.5
  • 49
    • 84886308072 scopus 로고    scopus 로고
    • Green tea polyphenols-β-lactoglobulin nanocomplexes: interfacial behavior, emulsification and oxidation stability of fish oil
    • [49] von Staszewski, M., Ruiz-Henestrosa, Pizones, Victor, M., Pilosof, A.M., Green tea polyphenols-β-lactoglobulin nanocomplexes: interfacial behavior, emulsification and oxidation stability of fish oil. Food Hydrocoll. 35 (2014), 505–511.
    • (2014) Food Hydrocoll. , vol.35 , pp. 505-511
    • von Staszewski, M.1    Ruiz-Henestrosa, P.2    Victor, M.3    Pilosof, A.M.4
  • 51
    • 77956012747 scopus 로고    scopus 로고
    • Flocculation of protein-stabilized oil-in-water emulsions
    • [51] Dickinson, E., Flocculation of protein-stabilized oil-in-water emulsions. Colloids Surf. B: Biointerfaces 81:1 (2010), 130–140.
    • (2010) Colloids Surf. B: Biointerfaces , vol.81 , Issue.1 , pp. 130-140
    • Dickinson, E.1
  • 53
    • 33751421851 scopus 로고    scopus 로고
    • Electrostatically driven protein aggregation: β-lactoglobulin at low ionic strength
    • [53] Majhi, P.R., Ganta, R.R., Vanam, R.P., Seyrek, E., Giger, K., Dubin, P.L., Electrostatically driven protein aggregation: β-lactoglobulin at low ionic strength. Langmuir 22:22 (2006), 9150–9159.
    • (2006) Langmuir , vol.22 , Issue.22 , pp. 9150-9159
    • Majhi, P.R.1    Ganta, R.R.2    Vanam, R.P.3    Seyrek, E.4    Giger, K.5    Dubin, P.L.6
  • 54
    • 84947046874 scopus 로고    scopus 로고
    • Miscibility of Quillaja saponins with other co-surfactants under different pH values
    • pp. E2495
    • [54] Reichert, C.L., Salminen, H., Leuenberger, B.H., Hinrichs, J., Weiss, J., Miscibility of Quillaja saponins with other co-surfactants under different pH values. J. Food Sci., 80(11), 2015 pp. E2495.
    • (2015) J. Food Sci. , vol.80 , Issue.11
    • Reichert, C.L.1    Salminen, H.2    Leuenberger, B.H.3    Hinrichs, J.4    Weiss, J.5
  • 55
    • 84861385656 scopus 로고    scopus 로고
    • Mixed protein–surfactant adsorption layers formed in a sequential and simultaneous way at water–air and water–oil interfaces
    • p. 6057
    • [55] Dan, A., Kotsmar, C., Ferri, J.K., Javadi, A., Karbaschi, M., Krägel, J., Wüstneck, R., Miller, R., Mixed protein–surfactant adsorption layers formed in a sequential and simultaneous way at water–air and water–oil interfaces. Soft Matter, 8, 2012, 22 p. 6057.
    • (2012) Soft Matter , vol.8 , pp. 22
    • Dan, A.1    Kotsmar, C.2    Ferri, J.K.3    Javadi, A.4    Karbaschi, M.5    Krägel, J.6    Wüstneck, R.7    Miller, R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.