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Volumn 440, Issue , 2014, Pages 136-144

The influence of polysaccharide on the stability of protein stabilized oil-in-water emulsion prepared by microchannel emulsification technique

Author keywords

Microchannel emulsification; Protein stabilized oil in water emulsion; Protein polysaccharide interaction; Uniformly sized emulsion

Indexed keywords

EMULSIFICATION; EMULSIONS; PROTEINS;

EID: 84889608020     PISSN: 09277757     EISSN: 18734359     Source Type: Journal    
DOI: 10.1016/j.colsurfa.2012.09.051     Document Type: Article
Times cited : (40)

References (27)
  • 3
    • 0002706526 scopus 로고    scopus 로고
    • Characteristics of milk
    • Marcel Dekker, New York, O.R. Fennema (Ed.)
    • Swaisgood H.E. Characteristics of milk. Food Chemistry 1996, 841-878. Marcel Dekker, New York. O.R. Fennema (Ed.).
    • (1996) Food Chemistry , pp. 841-878
    • Swaisgood, H.E.1
  • 4
    • 0030919241 scopus 로고    scopus 로고
    • Physical properties of whey protein stabilized emulsions as related to pH and NaCl
    • Demetriades K., Coupland J.N., McClements D.J. Physical properties of whey protein stabilized emulsions as related to pH and NaCl. J. Food Sci. 1997, 62:342-347.
    • (1997) J. Food Sci. , vol.62 , pp. 342-347
    • Demetriades, K.1    Coupland, J.N.2    McClements, D.J.3
  • 5
    • 0032197212 scopus 로고    scopus 로고
    • Structure technofunctional properties of protein-polysaccharide complexes: a review
    • Schmitt C., Sanchez C., Desobry-Banon S., Hardy J. Structure technofunctional properties of protein-polysaccharide complexes: a review. Crit. Rev. Food Sci. Nut. 1998, 38:689-753.
    • (1998) Crit. Rev. Food Sci. Nut. , vol.38 , pp. 689-753
    • Schmitt, C.1    Sanchez, C.2    Desobry-Banon, S.3    Hardy, J.4
  • 7
    • 0036189512 scopus 로고    scopus 로고
    • Emulsifying properties of whey protein-carboxymethylcellulose complexes
    • Girard M., Turgeon S.L., Paquin P. Emulsifying properties of whey protein-carboxymethylcellulose complexes. J. Food Sci. 2002, 67:113-119.
    • (2002) J. Food Sci. , vol.67 , pp. 113-119
    • Girard, M.1    Turgeon, S.L.2    Paquin, P.3
  • 8
    • 33646947847 scopus 로고    scopus 로고
    • Stability of emulsions containing a whey protein concentrate obtained from milk serum through carboxymethylcellulose complexation
    • Damianou K., Kiosseoglou V. Stability of emulsions containing a whey protein concentrate obtained from milk serum through carboxymethylcellulose complexation. Food Hydrocolloid 2006, 20:793-799.
    • (2006) Food Hydrocolloid , vol.20 , pp. 793-799
    • Damianou, K.1    Kiosseoglou, V.2
  • 9
    • 33746372109 scopus 로고    scopus 로고
    • Novel asymmetric through-hole array microfabricated on a silicon plate for formulating monodisperse emulsions
    • Kobayashi I., Mukataka S., Nakajima M. Novel asymmetric through-hole array microfabricated on a silicon plate for formulating monodisperse emulsions. Langmuir 2005, 21:7629-7632.
    • (2005) Langmuir , vol.21 , pp. 7629-7632
    • Kobayashi, I.1    Mukataka, S.2    Nakajima, M.3
  • 10
    • 14344251962 scopus 로고    scopus 로고
    • Preparation characteristics of monodispersed oil-in-water emulsions with large particles stabilized by proteins in straight-through microchannel emulsification
    • Saito M., Yin L., Kobayashi I., Nakajima M. Preparation characteristics of monodispersed oil-in-water emulsions with large particles stabilized by proteins in straight-through microchannel emulsification. Food Hydrocolloid 2005, 19:745-751.
    • (2005) Food Hydrocolloid , vol.19 , pp. 745-751
    • Saito, M.1    Yin, L.2    Kobayashi, I.3    Nakajima, M.4
  • 11
    • 0000179781 scopus 로고
    • Interactions between food stabilizers and β-lactoglobulin
    • Hidalgo J., Hansen P.M.T. Interactions between food stabilizers and β-lactoglobulin. J. Agric. Food Chem. 1969, 17:1089-1092.
    • (1969) J. Agric. Food Chem. , vol.17 , pp. 1089-1092
    • Hidalgo, J.1    Hansen, P.M.T.2
  • 12
    • 34248355091 scopus 로고    scopus 로고
    • Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin
    • Capitani C., Perez O.E., Pacheco B., Teresa M., Pilosof A.M.R. Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin. Food Hydrocolloid 2007, 21:1344-1354.
    • (2007) Food Hydrocolloid , vol.21 , pp. 1344-1354
    • Capitani, C.1    Perez, O.E.2    Pacheco, B.3    Teresa, M.4    Pilosof, A.M.R.5
  • 13
    • 0000487970 scopus 로고    scopus 로고
    • Effect of ι-carrageenan on flocculation, creaming, and rheology of a protein-stabilized emulsion
    • Dickinson E., Pawlowsky K. Effect of ι-carrageenan on flocculation, creaming, and rheology of a protein-stabilized emulsion. J. Agric. Food Chem. 1997, 45:3799-3806.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 3799-3806
    • Dickinson, E.1    Pawlowsky, K.2
  • 14
    • 0037237311 scopus 로고    scopus 로고
    • Hydrocolloids at interfaces and the influence on the properties of dispersed system
    • Dickinson E. Hydrocolloids at interfaces and the influence on the properties of dispersed system. Food Hydrocolloid 2003, 17:25-39.
    • (2003) Food Hydrocolloid , vol.17 , pp. 25-39
    • Dickinson, E.1
  • 15
    • 2542480268 scopus 로고    scopus 로고
    • Influence of pH and iota-carrageenan concentration on physicochemical properties and stability of β-lactoglobulin-stabilized oil-in-water emulsions
    • Gu Y.S., Decker E.A., McClements D.J. Influence of pH and iota-carrageenan concentration on physicochemical properties and stability of β-lactoglobulin-stabilized oil-in-water emulsions. J. Agric. Food Chem. 2004, 52:3626-3632.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 3626-3632
    • Gu, Y.S.1    Decker, E.A.2    McClements, D.J.3
  • 16
    • 54049135147 scopus 로고    scopus 로고
    • Effect of chitosan on the stability and properties of modified lecithin stabilized oil-in-water monodisperse emulsion prepared by microchannel emulsification
    • Chuah A.M., Kuroiwa T., Kobayashi I., Nakajima M. Effect of chitosan on the stability and properties of modified lecithin stabilized oil-in-water monodisperse emulsion prepared by microchannel emulsification. Food Hydrocolloid 2009, 23:600-610.
    • (2009) Food Hydrocolloid , vol.23 , pp. 600-610
    • Chuah, A.M.1    Kuroiwa, T.2    Kobayashi, I.3    Nakajima, M.4
  • 17
    • 0002147835 scopus 로고
    • Dimensions and possible structures of milk proteins at oil/water interfaces
    • Royal Society of Chemistry, Cambridge, UK, E. Dickinson (Ed.)
    • Dalgleish D., Leaver J. Dimensions and possible structures of milk proteins at oil/water interfaces. Food Polymers, Gels and Colloids 1991, 113-122. Royal Society of Chemistry, Cambridge, UK. E. Dickinson (Ed.).
    • (1991) Food Polymers, Gels and Colloids , pp. 113-122
    • Dalgleish, D.1    Leaver, J.2
  • 18
    • 0006379589 scopus 로고    scopus 로고
    • Effect of high-methoxy pectin on properties of casein-stabilized emulsions
    • Dickinson E., Semenova M., Antipova A.S., Pelan E.G. Effect of high-methoxy pectin on properties of casein-stabilized emulsions. Food Hydrocolloid 1998, 12:425-432.
    • (1998) Food Hydrocolloid , vol.12 , pp. 425-432
    • Dickinson, E.1    Semenova, M.2    Antipova, A.S.3    Pelan, E.G.4
  • 19
    • 85052705975 scopus 로고    scopus 로고
    • Structure-function relationships of whey proteins
    • Marcel Dekker Inc, New York, NY, S. Damodaran, A. Paraf (Eds.)
    • Cayot P., Lorient D. Structure-function relationships of whey proteins. Food Proteins and Their Applications 1997, 225-256. Marcel Dekker Inc, New York, NY. S. Damodaran, A. Paraf (Eds.).
    • (1997) Food Proteins and Their Applications , pp. 225-256
    • Cayot, P.1    Lorient, D.2
  • 20
    • 0032969273 scopus 로고    scopus 로고
    • Emulsification using micro porous glass (MPG): surface behavior of milk proteins
    • Scherze I., Marzilger K., Muschiolik G. Emulsification using micro porous glass (MPG): surface behavior of milk proteins. Colloid Surf. B: Biointerfaces 1999, 12:213-221.
    • (1999) Colloid Surf. B: Biointerfaces , vol.12 , pp. 213-221
    • Scherze, I.1    Marzilger, K.2    Muschiolik, G.3
  • 21
    • 0141631424 scopus 로고    scopus 로고
    • Evidence that homogenization of BSA-stabilized hexadecane-in-water emulsions induces structure modification of the nonadsorbed protein
    • Rampon V., Riaublanc A., Anton M., Genot C., McClements D.J. Evidence that homogenization of BSA-stabilized hexadecane-in-water emulsions induces structure modification of the nonadsorbed protein. J. Agric. Food Chem. 2003, 51:5900-5908.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 5900-5908
    • Rampon, V.1    Riaublanc, A.2    Anton, M.3    Genot, C.4    McClements, D.J.5
  • 22
    • 1842637382 scopus 로고    scopus 로고
    • Interfacial rheology of globular and flexible proteins at the hexadecane/water interface: comparison of shear and dilation deformation
    • Freer E.M., Yim K.S., Fuller C.G., Radke C.J. Interfacial rheology of globular and flexible proteins at the hexadecane/water interface: comparison of shear and dilation deformation. J. Phy. B: Chem. 2004, 108:3835-3844.
    • (2004) J. Phy. B: Chem. , vol.108 , pp. 3835-3844
    • Freer, E.M.1    Yim, K.S.2    Fuller, C.G.3    Radke, C.J.4
  • 23
    • 0036812540 scopus 로고    scopus 로고
    • Role of postadsorption conformation changes of β-lactoglobulin on its ability to stabilize oil droplets against flocculation during heating at neutral pH
    • Kim H.J., Decker E.A., McClements D.J. Role of postadsorption conformation changes of β-lactoglobulin on its ability to stabilize oil droplets against flocculation during heating at neutral pH. Langmuir 2002, 18:7577-7583.
    • (2002) Langmuir , vol.18 , pp. 7577-7583
    • Kim, H.J.1    Decker, E.A.2    McClements, D.J.3
  • 24
    • 0001119293 scopus 로고
    • Thermal stability of whey proteins-a calorimetric study
    • Bernal V., Jelen P. Thermal stability of whey proteins-a calorimetric study. J. Dairy Sci. 1985, 68:2847-2852.
    • (1985) J. Dairy Sci. , vol.68 , pp. 2847-2852
    • Bernal, V.1    Jelen, P.2
  • 25
    • 0029924648 scopus 로고    scopus 로고
    • Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin
    • Iametti S., De Gregori B., Vecchio G., Bonomi F. Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. Eur. J. Biochem. 1996, 237:106-112.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 106-112
    • Iametti, S.1    De Gregori, B.2    Vecchio, G.3    Bonomi, F.4
  • 26
    • 0000295322 scopus 로고    scopus 로고
    • Kinetics of heat induced aggregation of β-lactoglobulin
    • Verheul M., Roefs S., de Kruif K. Kinetics of heat induced aggregation of β-lactoglobulin. J. Agric. Food Chem. 1998, 46:896-903.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 896-903
    • Verheul, M.1    Roefs, S.2    de Kruif, K.3
  • 27
    • 0032843334 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin: as a function of pH
    • Hoffmann M.A.M., Van Mil P.J.J.M. Heat-induced aggregation of β-lactoglobulin: as a function of pH. J. Agric. Food Chem. 1999, 47:1898-1905.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 1898-1905
    • Hoffmann, M.A.M.1    Van Mil, P.J.J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.