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Volumn 516, Issue , 2017, Pages 94-105

Gliadin nanoparticles stabilized by a combination of thermally denatured ovalbumin with gemini dodecyl O-glucoside: The modulating effect of cosurfactant

Author keywords

Gemini dodecyl O glucoside; Gliadin nanoparticles; Ovalbumin; Redispersibility; Storage stability

Indexed keywords

CARBOHYDRATES; CIRCULAR DICHROISM SPECTROSCOPY; CRITICAL MICELLE CONCENTRATION; DICHROISM; FLUORESCENCE SPECTROSCOPY; LIQUIDS; MICELLES; NANOPARTICLES; PHASE INTERFACES;

EID: 85006434848     PISSN: 09277757     EISSN: 18734359     Source Type: Journal    
DOI: 10.1016/j.colsurfa.2016.12.024     Document Type: Article
Times cited : (25)

References (41)
  • 1
    • 84919797922 scopus 로고    scopus 로고
    • Encapsulation of resveratrol in biopolymer particles produced using liquid antisolvent precipitation. Part 1: preparation and characterization
    • [1] Davidov-Pardo, G., Joye, I.J., McClements, D.J., Encapsulation of resveratrol in biopolymer particles produced using liquid antisolvent precipitation. Part 1: preparation and characterization. Food Hydrocoll. 45 (2015), 309–316.
    • (2015) Food Hydrocoll. , vol.45 , pp. 309-316
    • Davidov-Pardo, G.1    Joye, I.J.2    McClements, D.J.3
  • 2
    • 84926391585 scopus 로고    scopus 로고
    • Encapsulation of resveratrol in biopolymer particles produced using liquid antisolvent precipitation. Part 2: stability and functionality
    • [2] Joye, I.J., Davidov-Pardo, G., McClements, D.J., Encapsulation of resveratrol in biopolymer particles produced using liquid antisolvent precipitation. Part 2: stability and functionality. Food Hydrocoll. 49 (2015), 127–134.
    • (2015) Food Hydrocoll. , vol.49 , pp. 127-134
    • Joye, I.J.1    Davidov-Pardo, G.2    McClements, D.J.3
  • 4
    • 84908395186 scopus 로고    scopus 로고
    • Gliadin-based nanoparticles: stabilization by post-production polysaccharide coating
    • [4] Joye, I.J., Nelis, V.A., McClements, D.J., Gliadin-based nanoparticles: stabilization by post-production polysaccharide coating. Food Hydrocoll. 43 (2015), 236–242.
    • (2015) Food Hydrocoll. , vol.43 , pp. 236-242
    • Joye, I.J.1    Nelis, V.A.2    McClements, D.J.3
  • 5
    • 84907637716 scopus 로고    scopus 로고
    • Gliadin-based nanoparticles: fabrication and stability of food-grade colloidal delivery systems
    • [5] Joye, I.J., Nelis, V.A., McClements, D.J., Gliadin-based nanoparticles: fabrication and stability of food-grade colloidal delivery systems. Food Hydrocoll. 44 (2015), 86–93.
    • (2015) Food Hydrocoll. , vol.44 , pp. 86-93
    • Joye, I.J.1    Nelis, V.A.2    McClements, D.J.3
  • 6
    • 84856355692 scopus 로고    scopus 로고
    • Liquid antisolvent precipitation and stabilization of nanoparticles of poorly water soluble drugs in aqueous suspensions: recent developments and future perspective
    • [6] Thorat, A.A., Dalvi, S.V., Liquid antisolvent precipitation and stabilization of nanoparticles of poorly water soluble drugs in aqueous suspensions: recent developments and future perspective. Chem. Eng. J. 181 (2012), 1–34.
    • (2012) Chem. Eng. J. , vol.181 , pp. 1-34
    • Thorat, A.A.1    Dalvi, S.V.2
  • 7
    • 84937604690 scopus 로고    scopus 로고
    • Controlled formation and stabilization of nanosized colloidal suspensions by combination of soy protein and biosurfactant stevioside as stabilizers
    • [7] Wan, Z.-L., Wang, L.-Y., Yang, X.-Q., Wang, J.-M., Wang, L.-J., Controlled formation and stabilization of nanosized colloidal suspensions by combination of soy protein and biosurfactant stevioside as stabilizers. Food Hydrocoll. 52 (2016), 317–328.
    • (2016) Food Hydrocoll. , vol.52 , pp. 317-328
    • Wan, Z.-L.1    Wang, L.-Y.2    Yang, X.-Q.3    Wang, J.-M.4    Wang, L.-J.5
  • 8
    • 84888864210 scopus 로고    scopus 로고
    • Production of nanoparticles by anti-solvent precipitation for use in food systems
    • [8] Joye, I.J., McClements, D.J., Production of nanoparticles by anti-solvent precipitation for use in food systems. Trends Food Sci. Technol. 34 (2013), 109–123.
    • (2013) Trends Food Sci. Technol. , vol.34 , pp. 109-123
    • Joye, I.J.1    McClements, D.J.2
  • 9
    • 0001257270 scopus 로고    scopus 로고
    • Polymer-surfactant interaction and stability of amorphous colloidal particles
    • [9] Chari, K., Antalek, B., Kowalczyk, J., Eachus, R.S., Chen, T., Polymer-surfactant interaction and stability of amorphous colloidal particles. J. Phys. Chem. B 103 (1999), 9867–9872.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 9867-9872
    • Chari, K.1    Antalek, B.2    Kowalczyk, J.3    Eachus, R.S.4    Chen, T.5
  • 10
    • 69249164683 scopus 로고    scopus 로고
    • Controlling particle size of a poorly water-soluble drug using ultrasound and stabilizers in antisolvent precipitation
    • [10] Dalvi, S.V., Dave, R.N., Controlling particle size of a poorly water-soluble drug using ultrasound and stabilizers in antisolvent precipitation. Ind. Eng. Chem. Res. 48 (2009), 7581–7593.
    • (2009) Ind. Eng. Chem. Res. , vol.48 , pp. 7581-7593
    • Dalvi, S.V.1    Dave, R.N.2
  • 11
    • 84880145656 scopus 로고    scopus 로고
    • A novel type of highly effective nonionic gemini alkyl O-glucoside surfactants: a versatile strategy of design
    • [11] Liu, S., Sang, R., Hong, S., Cai, Y., Wang, H., A novel type of highly effective nonionic gemini alkyl O-glucoside surfactants: a versatile strategy of design. Langmuir 29 (2013), 8511–8516.
    • (2013) Langmuir , vol.29 , pp. 8511-8516
    • Liu, S.1    Sang, R.2    Hong, S.3    Cai, Y.4    Wang, H.5
  • 12
    • 84960353215 scopus 로고    scopus 로고
    • Decoration of gemini alkyl O-glucosides based vesicles by electrostatic deposition of sodium carboxymethyl cellullose: mechanism, structure and improved stability
    • [12] Feng, J., Lin, C., Wang, H., Liu, S., Decoration of gemini alkyl O-glucosides based vesicles by electrostatic deposition of sodium carboxymethyl cellullose: mechanism, structure and improved stability. Food Hydrocoll. 58 (2016), 284–297.
    • (2016) Food Hydrocoll. , vol.58 , pp. 284-297
    • Feng, J.1    Lin, C.2    Wang, H.3    Liu, S.4
  • 13
    • 84973168527 scopus 로고    scopus 로고
    • Stability of trianionic curcumin enhanced by gemini alkyl O-glucosides and alkyl trimethyl ammonium halides mixed micelles
    • [13] Feng, J., Wu, S., Wang, H., Liu, S., Stability of trianionic curcumin enhanced by gemini alkyl O-glucosides and alkyl trimethyl ammonium halides mixed micelles. Colloids Surf. A: Physicochem. Eng. Asp. 504 (2016), 190–200.
    • (2016) Colloids Surf. A: Physicochem. Eng. Asp. , vol.504 , pp. 190-200
    • Feng, J.1    Wu, S.2    Wang, H.3    Liu, S.4
  • 15
    • 84924129379 scopus 로고    scopus 로고
    • Impact of environment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs
    • [15] Sponton, O.E., Perez, A.A., Carrara, C.R., Santiago, L.G., Impact of environment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs. Food Hydrocoll. 48 (2015), 165–173.
    • (2015) Food Hydrocoll. , vol.48 , pp. 165-173
    • Sponton, O.E.1    Perez, A.A.2    Carrara, C.R.3    Santiago, L.G.4
  • 17
    • 84907215678 scopus 로고    scopus 로고
    • Efficient improvement of surface activity of tea saponin through gemini-like modification by straightforward esterification
    • [17] Feng, J., Chen, Y., Liu, X., Liu, S., Efficient improvement of surface activity of tea saponin through gemini-like modification by straightforward esterification. Food Chem. 171 (2015), 272–279.
    • (2015) Food Chem. , vol.171 , pp. 272-279
    • Feng, J.1    Chen, Y.2    Liu, X.3    Liu, S.4
  • 19
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • [19] Whitmore, L., Wallace, B.A., DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32 (2004), W668–W673.
    • (2004) Nucleic Acids Res. , vol.32 , pp. W668-W673
    • Whitmore, L.1    Wallace, B.A.2
  • 20
    • 34249868995 scopus 로고    scopus 로고
    • Macroscopic modeling of the surface tension of polymer-surfactant systems
    • [20] Bell, C.G., Breward, C.J.W., Howell, P.D., Penfold, J., Thomas, R.K., Macroscopic modeling of the surface tension of polymer-surfactant systems. Langmuir 23 (2007), 6042–6052.
    • (2007) Langmuir , vol.23 , pp. 6042-6052
    • Bell, C.G.1    Breward, C.J.W.2    Howell, P.D.3    Penfold, J.4    Thomas, R.K.5
  • 21
    • 65949093954 scopus 로고    scopus 로고
    • A thermodynamic analysis of the binding interaction between polysorbate 20 and 80 with human serum albumins and immunoglobulins: a contribution to understand colloidal protein stabilisation
    • [21] Garidel, P., Hoffmann, C., Blume, A., A thermodynamic analysis of the binding interaction between polysorbate 20 and 80 with human serum albumins and immunoglobulins: a contribution to understand colloidal protein stabilisation. Biophys. Chem. 143 (2009), 70–78.
    • (2009) Biophys. Chem. , vol.143 , pp. 70-78
    • Garidel, P.1    Hoffmann, C.2    Blume, A.3
  • 22
    • 0020193418 scopus 로고
    • Interaction between hydrophilic proteins and non-ionic detergents studied by surface-tension measurements
    • [22] Nishikido, N., Takahara, T., Kobayashi, H., Tanaka, M., Interaction between hydrophilic proteins and non-ionic detergents studied by surface-tension measurements. Bull. Chem. Soc. Jpn. 55 (1982), 3085–3088.
    • (1982) Bull. Chem. Soc. Jpn. , vol.55 , pp. 3085-3088
    • Nishikido, N.1    Takahara, T.2    Kobayashi, H.3    Tanaka, M.4
  • 23
    • 84933512974 scopus 로고    scopus 로고
    • Adsorption of proteins at the solution/air interface influenced by added non-ionic surfactants at very low concentrations for both components. 1. Dodecyl dimethyl phospine oxide
    • [23] Lotfi, M., Jayadi, A., Lylyk, S.V., Bastani, D., Fainerman, V.B., Miller, R., Adsorption of proteins at the solution/air interface influenced by added non-ionic surfactants at very low concentrations for both components. 1. Dodecyl dimethyl phospine oxide. Colloids Surf. A: Physicochem. Eng. Asp. 475 (2015), 62–68.
    • (2015) Colloids Surf. A: Physicochem. Eng. Asp. , vol.475 , pp. 62-68
    • Lotfi, M.1    Jayadi, A.2    Lylyk, S.V.3    Bastani, D.4    Fainerman, V.B.5    Miller, R.6
  • 24
    • 61849129303 scopus 로고    scopus 로고
    • Equilibrium of adsorption of mixed milk protein/surfactant solutions at the water/air interface
    • [24] Kotsmar, C., Grigoriev, D.O., Xu, F., Aksenenko, E.V., Fainerman, V.B., Leser, M.E., Millert, R., Equilibrium of adsorption of mixed milk protein/surfactant solutions at the water/air interface. Langmuir 24 (2008), 13977–13984.
    • (2008) Langmuir , vol.24 , pp. 13977-13984
    • Kotsmar, C.1    Grigoriev, D.O.2    Xu, F.3    Aksenenko, E.V.4    Fainerman, V.B.5    Leser, M.E.6    Millert, R.7
  • 25
    • 84901602167 scopus 로고    scopus 로고
    • Interaction of Quillaja bark saponins with food-relevant proteins
    • [25] Kezwon, A., Wojciechowski, K., Interaction of Quillaja bark saponins with food-relevant proteins. Adv. Colloid Interface Sci. 209 (2014), 185–195.
    • (2014) Adv. Colloid Interface Sci. , vol.209 , pp. 185-195
    • Kezwon, A.1    Wojciechowski, K.2
  • 26
    • 84904409324 scopus 로고    scopus 로고
    • Synergistic foaming and surface properties of a weakly interacting mixture of soy glycinin and biosurfactant stevioside
    • [26] Wan, Z.-L., Wang, L.-Y., Wang, J.-M., Yuan, Y., Yang, X.-Q., Synergistic foaming and surface properties of a weakly interacting mixture of soy glycinin and biosurfactant stevioside. J. Agric. Food. Chem. 62 (2014), 6834–6843.
    • (2014) J. Agric. Food. Chem. , vol.62 , pp. 6834-6843
    • Wan, Z.-L.1    Wang, L.-Y.2    Wang, J.-M.3    Yuan, Y.4    Yang, X.-Q.5
  • 27
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: can low affinity systems be studied by isothermal titration calorimetry?
    • [27] Turnbull, W.B., Daranas, A.H., On the value of c: can low affinity systems be studied by isothermal titration calorimetry?. J. Am. Chem. Soc. 125 (2003), 14859–14866.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 28
    • 84874841799 scopus 로고    scopus 로고
    • Interaction between beta-casein micelles and imidazolium-based ionic liquid surfactant
    • [28] Liu, Y., Yang, L., Guo, R., Interaction between beta-casein micelles and imidazolium-based ionic liquid surfactant. Soft Matter 9 (2013), 3671–3680.
    • (2013) Soft Matter , vol.9 , pp. 3671-3680
    • Liu, Y.1    Yang, L.2    Guo, R.3
  • 29
    • 84900992924 scopus 로고    scopus 로고
    • Interaction of a hydrophobic-functionalized PAMAM dendrimer with bovine serum albumin: thermodynamic and structural changes
    • [29] Zhang, H.-M., Lou, K., Cao, J., Wang, Y.-Q., Interaction of a hydrophobic-functionalized PAMAM dendrimer with bovine serum albumin: thermodynamic and structural changes. Langmuir 30 (2014), 5536–5544.
    • (2014) Langmuir , vol.30 , pp. 5536-5544
    • Zhang, H.-M.1    Lou, K.2    Cao, J.3    Wang, Y.-Q.4
  • 30
    • 84955288838 scopus 로고    scopus 로고
    • Enhancement of colour stability of anthocyanins in model beverages by gum arabic addition
    • [30] Chung, C., Rojanasasithara, T., Mutilangi, W., McClements, D.J., Enhancement of colour stability of anthocyanins in model beverages by gum arabic addition. Food Chem. 201 (2016), 14–22.
    • (2016) Food Chem. , vol.201 , pp. 14-22
    • Chung, C.1    Rojanasasithara, T.2    Mutilangi, W.3    McClements, D.J.4
  • 31
    • 40549127817 scopus 로고    scopus 로고
    • A fluorescence analysis of ANS bound to bovine serum albumin: binding properties revisited by using energy transfer
    • [31] Togashi, D.M., Ryder, A.G., A fluorescence analysis of ANS bound to bovine serum albumin: binding properties revisited by using energy transfer. J. Fluoresc. 18 (2008), 519–526.
    • (2008) J. Fluoresc. , vol.18 , pp. 519-526
    • Togashi, D.M.1    Ryder, A.G.2
  • 32
    • 11244303574 scopus 로고    scopus 로고
    • Interaction of flavonoids with bovine serum albumin: a fluorescence quenching study
    • [32] Papadopoulou, A., Green, R.J., Frazier, R.A., Interaction of flavonoids with bovine serum albumin: a fluorescence quenching study. J. Agric. Food. Chem. 53 (2005), 158–163.
    • (2005) J. Agric. Food. Chem. , vol.53 , pp. 158-163
    • Papadopoulou, A.1    Green, R.J.2    Frazier, R.A.3
  • 33
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution – an experimental study of diffusion process
    • [33] Ware, W.R., Oxygen quenching of fluorescence in solution – an experimental study of diffusion process. J. Phys. Chem. 66 (1962), 455–458.
    • (1962) J. Phys. Chem. , vol.66 , pp. 455-458
    • Ware, W.R.1
  • 34
    • 84938267635 scopus 로고    scopus 로고
    • Interaction of bovine serum albumin with N-acyl amino acid based anionic surfactants: effect of head-group hydrophobicity
    • [34] Ghosh, S., Dey, J., Interaction of bovine serum albumin with N-acyl amino acid based anionic surfactants: effect of head-group hydrophobicity. J. Colloid Interface Sci. 458 (2015), 284–292.
    • (2015) J. Colloid Interface Sci. , vol.458 , pp. 284-292
    • Ghosh, S.1    Dey, J.2
  • 35
    • 84922771829 scopus 로고    scopus 로고
    • Stepwise unfolding of bovine and human serum albumin by an anionic surfactant: an investigation using the proton transfer probe norharmane
    • [35] Ghosh, S., Chakrabarty, S., Bhowmik, D., Kumar, G.S., Chattopadhyay, N., Stepwise unfolding of bovine and human serum albumin by an anionic surfactant: an investigation using the proton transfer probe norharmane. J. Phys. Chem. B 119 (2015), 2090–2102.
    • (2015) J. Phys. Chem. B , vol.119 , pp. 2090-2102
    • Ghosh, S.1    Chakrabarty, S.2    Bhowmik, D.3    Kumar, G.S.4    Chattopadhyay, N.5
  • 36
    • 84884290295 scopus 로고    scopus 로고
    • Bottom-up approaches for preparing drug nanocrystals: formulations and factors affecting particle size
    • [36] Sinha, B., Mueller, R.H., Moeschwitzer, J.P., Bottom-up approaches for preparing drug nanocrystals: formulations and factors affecting particle size. Int. J. Pharm. 453 (2013), 126–141.
    • (2013) Int. J. Pharm. , vol.453 , pp. 126-141
    • Sinha, B.1    Mueller, R.H.2    Moeschwitzer, J.P.3
  • 37
    • 0029488435 scopus 로고
    • Molecular-organization of surfactants at solid-liquid interfaces
    • [37] Manne, S., Gaub, H.E., Molecular-organization of surfactants at solid-liquid interfaces. Science 270 (1995), 1480–1482.
    • (1995) Science , vol.270 , pp. 1480-1482
    • Manne, S.1    Gaub, H.E.2
  • 38
    • 0009686807 scopus 로고    scopus 로고
    • Organization of sodium dodecyl sulfate at the graphite-solution interface
    • [38] Wanless, E.J., Ducker, W.A., Organization of sodium dodecyl sulfate at the graphite-solution interface. J. Phys. Chem. 100 (1996), 3207–3214.
    • (1996) J. Phys. Chem. , vol.100 , pp. 3207-3214
    • Wanless, E.J.1    Ducker, W.A.2
  • 40
    • 84904470855 scopus 로고    scopus 로고
    • Fabrication of surfactant-stabilized zein nanoparticles: a pH modulated antisolvent precipitation method
    • [40] Hu, K., McClements, D.J., Fabrication of surfactant-stabilized zein nanoparticles: a pH modulated antisolvent precipitation method. Food Res. Int. 64 (2014), 329–335.
    • (2014) Food Res. Int. , vol.64 , pp. 329-335
    • Hu, K.1    McClements, D.J.2
  • 41
    • 78649671551 scopus 로고    scopus 로고
    • Sodium caseinate stabilized zein colloidal particles
    • [41] Patel, A.R., Bouwens, E.C.M., Velikov, K.P., Sodium caseinate stabilized zein colloidal particles. J. Agric. Food Chem. 58 (2010), 12497–12503.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 12497-12503
    • Patel, A.R.1    Bouwens, E.C.M.2    Velikov, K.P.3


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