메뉴 건너뛰기




Volumn 61, Issue 44, 2013, Pages 10582-10589

Controllable self-assembly of sodium caseinate with a zwitterionic vitamin-derived bolaamphiphile

Author keywords

bolaamphiphile; orotic acid; self assembly; sodium caseinate; vesicles

Indexed keywords

BOLAAMPHIPHILES; ELECTROSTATIC REPULSION; FLUORESCENCE SPECTRA; HYDROPHOBIC INTERACTIONS; REVERSIBLE SELF ASSEMBLIES; SODIUM CASEINATE; TEMPERATURE DEPENDENT; VESICLES;

EID: 84887652921     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf403538y     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 0036866003 scopus 로고    scopus 로고
    • Casein structure, self-assembly and gelation
    • Horne, D. S. Casein structure, self-assembly and gelation Curr. Opin. Colloid Interface Sci. 2002, 7, 456-461
    • (2002) Curr. Opin. Colloid Interface Sci. , vol.7 , pp. 456-461
    • Horne, D.S.1
  • 2
    • 12344306653 scopus 로고    scopus 로고
    • Aggregation of casein micelles by interactions with chitosans: A study by Monte Carlo simulations
    • Narambuena, C. F.; Ausar, F. S.; Bianco, I. D.; Beltramo, D. M.; Leiva, E. P. M. Aggregation of casein micelles by interactions with chitosans: a study by Monte Carlo simulations J. Agric. Food Chem. 2005, 53, 459-463
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 459-463
    • Narambuena, C.F.1    Ausar, F.S.2    Bianco, I.D.3    Beltramo, D.M.4    Leiva, E.P.M.5
  • 3
    • 33845904590 scopus 로고    scopus 로고
    • Casein micelle structure: A concise review
    • Phadungath, C. Casein micelle structure: a concise review Songklanakarin J. Sci. Technol. 2005, 27, 201-212
    • (2005) Songklanakarin J. Sci. Technol. , vol.27 , pp. 201-212
    • Phadungath, C.1
  • 4
    • 34548818768 scopus 로고    scopus 로고
    • Interaction between casein and sodium dodecyl sulfate
    • Liu, Y.; Guo, R. Interaction between casein and sodium dodecyl sulfate J. Colloid Interface Sci. 2007, 315, 685-692
    • (2007) J. Colloid Interface Sci. , vol.315 , pp. 685-692
    • Liu, Y.1    Guo, R.2
  • 5
    • 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. Controlled Release 2011, 153, 206-216
    • (2011) J. Controlled Release , vol.153 , pp. 206-216
    • Elzoghby, A.O.1    Abo El-Fotoh, W.S.2    Elgindy, N.A.3
  • 6
    • 79961025299 scopus 로고    scopus 로고
    • Mixed biopolymers at interfaces: Competitive adsorption and multilayer structures
    • Dickinson, E. Mixed biopolymers at interfaces: Competitive adsorption and multilayer structures Food Hydrocolloids 2011, 25, 1966-1983
    • (2011) Food Hydrocolloids , vol.25 , pp. 1966-1983
    • Dickinson, E.1
  • 7
    • 40849116384 scopus 로고    scopus 로고
    • Effect of surfactants on casein structure: A spectroscopic study
    • Chakraborty, A.; Basak, S. Effect of surfactants on casein structure: a spectroscopic study Colloids Surf. B: Biointerfaces 2008, 63, 83-90
    • (2008) Colloids Surf. B: Biointerfaces , vol.63 , pp. 83-90
    • Chakraborty, A.1    Basak, S.2
  • 8
    • 34948886235 scopus 로고    scopus 로고
    • Interaction between casein and the oppositely charged surfactant
    • Liu, Y.; Guo, R. Interaction between casein and the oppositely charged surfactant Biomacromolecules 2007, 8, 2902-2908
    • (2007) Biomacromolecules , vol.8 , pp. 2902-2908
    • Liu, Y.1    Guo, R.2
  • 9
    • 1642335755 scopus 로고    scopus 로고
    • Reversible cold gelation of sodium caseinate solutions with added salt
    • Carr, A. J.; Munro, P. A. Reversible cold gelation of sodium caseinate solutions with added salt J. Dairy Res. 2004, 71, 126-128
    • (2004) J. Dairy Res. , vol.71 , pp. 126-128
    • Carr, A.J.1    Munro, P.A.2
  • 10
    • 70349764297 scopus 로고    scopus 로고
    • Influence of calcium on tensile, optical and water vapour permeability properties of sodium caseinate edible films
    • Fabra, M. J.; Talens, P.; Chiralt, A. Influence of calcium on tensile, optical and water vapour permeability properties of sodium caseinate edible films J. Food Eng. 2010, 96, 356-364
    • (2010) J. Food Eng. , vol.96 , pp. 356-364
    • Fabra, M.J.1    Talens, P.2    Chiralt, A.3
  • 11
    • 79961031918 scopus 로고    scopus 로고
    • Polysaccharide-protein interactions in dairy matrices, control and design of structures
    • Corredig, M.; Sharafbafi, N.; Kristo, E. Polysaccharide-protein interactions in dairy matrices, control and design of structures Food Hydrocolloids 2011, 25, 1833-1841
    • (2011) Food Hydrocolloids , vol.25 , pp. 1833-1841
    • Corredig, M.1    Sharafbafi, N.2    Kristo, E.3
  • 12
    • 0032197212 scopus 로고    scopus 로고
    • Structure and technofunctional properties of protein-polysaccharide complexes: A review
    • Schmitt, C.; Sanchez, C.; Desobry-Banon, S.; Hardy, J. Structure and technofunctional properties of protein-polysaccharide complexes: a review J. Crit. Rev. Food Sci. 1998, 38, 689-753
    • (1998) J. Crit. Rev. Food Sci. , vol.38 , pp. 689-753
    • Schmitt, C.1    Sanchez, C.2    Desobry-Banon, S.3    Hardy, J.4
  • 13
    • 10044249752 scopus 로고    scopus 로고
    • Recovery of phenytoin from feeding formulas and protein mixtures
    • Hennessy, D. D. Recovery of phenytoin from feeding formulas and protein mixtures Am. J. Health-Syst. Pharm. 2003, 60, 1850-1852
    • (2003) Am. J. Health-Syst. Pharm. , vol.60 , pp. 1850-1852
    • Hennessy, D.D.1
  • 14
    • 79951963842 scopus 로고    scopus 로고
    • Molecular recognition of melamine by vesicles spontaneously formed from orotic acid derived bolaamphiphiles
    • Chen, Z. X.; Su, X. X.; Deng, S. P. Molecular recognition of melamine by vesicles spontaneously formed from orotic acid derived bolaamphiphiles J. Phys. Chem. B 2011, 115, 1798-1806
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1798-1806
    • Chen, Z.X.1    Su, X.X.2    Deng, S.P.3
  • 15
    • 84861302913 scopus 로고    scopus 로고
    • Chaotrope-assisted color visualization mechanism and thermodynamics involved in molecular recognition of melamine by bolaamphiphiles embedded in polydiacetylene vesicles
    • Chen, Z. X.; Cao, C.; Deng, S. P. Chaotrope-assisted color visualization mechanism and thermodynamics involved in molecular recognition of melamine by bolaamphiphiles embedded in polydiacetylene vesicles Acta Phys. Chim. Sin. 2012, 28, 1320-1328
    • (2012) Acta Phys. Chim. Sin. , vol.28 , pp. 1320-1328
    • Chen, Z.X.1    Cao, C.2    Deng, S.P.3
  • 16
    • 84868091765 scopus 로고    scopus 로고
    • Realization of the reversible vesicle-micelle transition of vitamin-derived bolaamphiphiles by heat change monitoring
    • Sun, Y. L.; Wang, S. S.; Han, X.; Chen, Z. X. Realization of the reversible vesicle-micelle transition of vitamin-derived bolaamphiphiles by heat change monitoring J. Phys. Chem. B 2012, 116, 12372-12380
    • (2012) J. Phys. Chem. B , vol.116 , pp. 12372-12380
    • Sun, Y.L.1    Wang, S.S.2    Han, X.3    Chen, Z.X.4
  • 18
    • 12344310391 scopus 로고    scopus 로고
    • Simulating the self-association of caseins
    • Euston, S. R.; Horne, D. S. Simulating the self-association of caseins Food Hydrocolloids 2005, 19, 379-386
    • (2005) Food Hydrocolloids , vol.19 , pp. 379-386
    • Euston, S.R.1    Horne, D.S.2
  • 19
    • 33746215812 scopus 로고    scopus 로고
    • Colloid science of mixed ingredients
    • Dickinson, E. Colloid science of mixed ingredients Soft Matter 2006, 2, 642-652
    • (2006) Soft Matter , vol.2 , pp. 642-652
    • Dickinson, E.1
  • 20
    • 84859298220 scopus 로고    scopus 로고
    • (Kees). Co-acervates of lactoferrin and caseins
    • Anema, S. G.; de Kruif, C. G. (Kees). Co-acervates of lactoferrin and caseins Soft Matter 2012, 8, 4471-4478
    • (2012) Soft Matter , vol.8 , pp. 4471-4478
    • Anema, S.G.1    De Kruif, C.G.2
  • 21
    • 84872380723 scopus 로고    scopus 로고
    • Influence of xanthan gum on physical characteristics of sodium caseinate solutions and emulsions
    • Long, Z.; Zhao, Q. Z.; Liu, T. L.; Kuang, W.; Xu, J.; Zhao, M. Influence of xanthan gum on physical characteristics of sodium caseinate solutions and emulsions Food Hydrocolloids 2013, 32, 123-129
    • (2013) Food Hydrocolloids , vol.32 , pp. 123-129
    • Long, Z.1    Zhao, Q.Z.2    Liu, T.L.3    Kuang, W.4    Xu, J.5    Zhao, M.6
  • 22
    • 0031549624 scopus 로고    scopus 로고
    • Effect of aqueous alcohol solutions on the thermal transition of lysozyme: A calorimetric study
    • Cinelli, S.; Onori, G.; Santucci, A. Effect of aqueous alcohol solutions on the thermal transition of lysozyme: a calorimetric study J. Phys. Chem. B 1997, 101, 8029-8034
    • (1997) J. Phys. Chem. B , vol.101 , pp. 8029-8034
    • Cinelli, S.1    Onori, G.2    Santucci, A.3
  • 23
    • 54049146615 scopus 로고    scopus 로고
    • Light scattering study of sodium caseinate-dextran sulfate in aqueous solution: Relationship to emulsion stability
    • Semenova, M. G.; Belyakova, L. E.; Polikarpov, Y. N.; Antipova, A. S.; Dickinson, E. Light scattering study of sodium caseinate-dextran sulfate in aqueous solution: relationship to emulsion stability Food Hydrocolloids 2009, 23, 629-639
    • (2009) Food Hydrocolloids , vol.23 , pp. 629-639
    • Semenova, M.G.1    Belyakova, L.E.2    Polikarpov, Y.N.3    Antipova, A.S.4    Dickinson, E.5
  • 26
    • 79961170121 scopus 로고    scopus 로고
    • Temperature-dependent complexation between sodium caseinate and gum arabic
    • Ye, A.; Edwards, P. J. B.; Gilliland, J.; Jameson, G. B.; Singh, H. Temperature-dependent complexation between sodium caseinate and gum arabic Food Hydrocolloids 2012, 26, 82-88
    • (2012) Food Hydrocolloids , vol.26 , pp. 82-88
    • Ye, A.1    Edwards, P.J.B.2    Gilliland, J.3    Jameson, G.B.4    Singh, H.5
  • 27
    • 33645297214 scopus 로고    scopus 로고
    • Temperature-induced micelle to vesicle transition in the sodium dodecylsulfate/dodecyltriethylammonium bromide system
    • Yin, H.; Zhou, Z.; Huang, J.; Zheng, R.; Zhang, Y. Temperature-induced micelle to vesicle transition in the sodium dodecylsulfate/ dodecyltriethylammonium bromide system Angew. Chem. 2003, 115, 2238-2241
    • (2003) Angew. Chem. , vol.115 , pp. 2238-2241
    • Yin, H.1    Zhou, Z.2    Huang, J.3    Zheng, R.4    Zhang, Y.5
  • 28
    • 34247376036 scopus 로고    scopus 로고
    • Temperature-induced vesicle aggregation in catanionic surfactant systems: The effects of the headgroup and counterion
    • Yin, H.; Lin, Y.; Huang, J.; Ye, J. Temperature-induced vesicle aggregation in catanionic surfactant systems: the effects of the headgroup and counterion Langmuir 2007, 23, 4225-4230
    • (2007) Langmuir , vol.23 , pp. 4225-4230
    • Yin, H.1    Lin, Y.2    Huang, J.3    Ye, J.4
  • 29
    • 15544365807 scopus 로고    scopus 로고
    • Heating-induced micelle to vesicle transition in the cationic-anionic surfactant systems: Comprehensive study and understanding
    • Yin, H.; Huang, J.; Lin, Y.; Zhang, Y.; Qiu, S.; Ye, J. Heating-induced micelle to vesicle transition in the cationic-anionic surfactant systems: comprehensive study and understanding J. Phys. Chem. B 2005, 109, 4104-4110
    • (2005) J. Phys. Chem. B , vol.109 , pp. 4104-4110
    • Yin, H.1    Huang, J.2    Lin, Y.3    Zhang, Y.4    Qiu, S.5    Ye, J.6
  • 30
    • 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
  • 31
    • 0020161197 scopus 로고
    • A scanning calorimetric study of small molecule-lipid bilayer mixtures
    • Sturtevant, J. M. A scanning calorimetric study of small molecule-lipid bilayer mixtures Proc. Natl. Acad. Sci. U.S.A. 1982, 79, 3963-3967
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 3963-3967
    • Sturtevant, J.M.1
  • 34
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein, E. A.; Vedenkina, N. S.; Ivkva, M. N. Fluorescence and the location of tryptophan residues in protein molecules Photochem. Photobiol. 1973, 18, 263-279
    • (1973) Photochem. Photobiol. , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkva, M.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.