메뉴 건너뛰기




Volumn 60, Issue 12, 2012, Pages 3302-3310

Adsorption and dilatational rheology of heat-treated soy protein at the oil-water interface: Relationship to structural properties

Author keywords

adsorption; heat treatment; oil water interface; soy protein; structural properties; surface dilatational rheology

Indexed keywords

ADSORBED LAYERS; DILATATIONAL MODULUS; DILATATIONAL RHEOLOGY; DISULFIDE BONDS; FLEXIBLE CONFORMATION; HEATING TEMPERATURES; HYDROPHOBIC GROUPS; INTERFACIAL BEHAVIORS; INTERFACIAL LAYER; INTERFACIAL PROPERTY; INTERFACIAL RHEOLOGY; INTERMOLECULAR INTERACTIONS; NATIVE PROTEINS; OIL WATER INTERFACES; PARTIAL UNFOLDING; PROTEIN UNFOLDING; RAPID DEVELOPMENT; SOY PROTEIN; SOY PROTEIN ISOLATES; STRUCTURE DEPENDENCE; SULFHYDRYL GROUPS; SURFACE ACTIVITIES; SURFACE HYDROPHOBICITY; SURFACE PRESSURES;

EID: 84859139092     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf205128v     Document Type: Article
Times cited : (292)

References (40)
  • 1
    • 0000654216 scopus 로고
    • Proteins at liquid interfaces. III. Molecular structures of adsorbed films
    • Graham, D. E.; Phillips, M. C. Proteins at liquid interfaces. III. Molecular structures of adsorbed films J. Colloid Interface Sci. 1979, 70, 427-439
    • (1979) J. Colloid Interface Sci. , vol.70 , pp. 427-439
    • Graham, D.E.1    Phillips, M.C.2
  • 2
    • 0032809028 scopus 로고    scopus 로고
    • Adsorbed protein layers at fluid interfaces: Interactions, structure and surface rheology
    • Dickinson, E. Adsorbed protein layers at fluid interfaces: Interactions, structure and surface rheology Colloids Surf., B 1999, 15, 161-176
    • (1999) Colloids Surf., B , vol.15 , pp. 161-176
    • Dickinson, E.1
  • 3
    • 0036867705 scopus 로고    scopus 로고
    • Interfacial rheology of food emulsifiers and proteins
    • Murray, B. S. Interfacial rheology of food emulsifiers and proteins Curr. Opin. Colloid Interface Sci. 2002, 7, 426-431
    • (2002) Curr. Opin. Colloid Interface Sci. , vol.7 , pp. 426-431
    • Murray, B.S.1
  • 4
    • 1842637382 scopus 로고    scopus 로고
    • Interfacial rheology of globular and flexible proteins at the hexadecane/water interface: Comparison of shear and dilatation deformation
    • Freer, E. M.; Yim, K. S.; Fuller, G. G.; Radke, C. J. Interfacial rheology of globular and flexible proteins at the hexadecane/water interface: comparison of shear and dilatation deformation J. Phys. Chem. B 2004, 108, 3835-3844
    • (2004) J. Phys. Chem. B , vol.108 , pp. 3835-3844
    • Freer, E.M.1    Yim, K.S.2    Fuller, G.G.3    Radke, C.J.4
  • 5
    • 0242314936 scopus 로고    scopus 로고
    • Adsorption of whey protein isolate at the oil-water interface as a function of processing conditions: A rheokinetic study
    • Patino, J. M. R.; Nino, M. R. R.; Sanchez, C. C. Adsorption of whey protein isolate at the oil-water interface as a function of processing conditions: A rheokinetic study J. Agric. Food Chem. 1999, 47, 2241-2248
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 2241-2248
    • Patino, J.M.R.1    Nino, M.R.R.2    Sanchez, C.C.3
  • 7
    • 79961023076 scopus 로고    scopus 로고
    • β-Lactoglobulin and WPI aggregates: Formation, structure and applications
    • Nicolai, T.; Britten, M.; Schmitt, C. β-Lactoglobulin and WPI aggregates: Formation, structure and applications Food Hydrocolloids 2011, 25, 1945-1962
    • (2011) Food Hydrocolloids , vol.25 , pp. 1945-1962
    • Nicolai, T.1    Britten, M.2    Schmitt, C.3
  • 8
    • 79952534829 scopus 로고    scopus 로고
    • Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties
    • Moro, A.; Báez, G. D.; Busti, P. A.; Ballerini, G. A.; Delorenzi, N. J. Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties Food Hydrocolloids 2011, 25, 1009-1015
    • (2011) Food Hydrocolloids , vol.25 , pp. 1009-1015
    • Moro, A.1    Báez, G.D.2    Busti, P.A.3    Ballerini, G.A.4    Delorenzi, N.J.5
  • 9
    • 4444265418 scopus 로고    scopus 로고
    • Emulsifying properties and surface behavior of native and denatured whey soy proteins in comparison with other proteins. Creaming stability of oil-in-water emulsions
    • Palazolo, G. G.; Sorgentini, D. A.; Wagner, J. R. Emulsifying properties and surface behavior of native and denatured whey soy proteins in comparison with other proteins. Creaming stability of oil-in-water emulsions J. Am. Oil Chem. Soc. 2004, 81, 625-632
    • (2004) J. Am. Oil Chem. Soc. , vol.81 , pp. 625-632
    • Palazolo, G.G.1    Sorgentini, D.A.2    Wagner, J.R.3
  • 10
    • 1642418993 scopus 로고    scopus 로고
    • Relationship between interfacial behaviour of native and denatured soybean isolates and microstructure and coalescence of oil in water emulsions-Effect of salt and protein concentration
    • Palazolo, G. G.; Mitidieri, F. E.; Wagner, J. R. Relationship between interfacial behaviour of native and denatured soybean isolates and microstructure and coalescence of oil in water emulsions-Effect of salt and protein concentration Food Sci. Technol. Int. 2003, 9, 409-411
    • (2003) Food Sci. Technol. Int. , vol.9 , pp. 409-411
    • Palazolo, G.G.1    Mitidieri, F.E.2    Wagner, J.R.3
  • 11
    • 34548285780 scopus 로고    scopus 로고
    • Heat treatment of bovine α-lactalbumin results in partially folded, disulfide bond shuffled states with enhanced surface activity
    • Wijesinha-Bettoni, R.; Gao, C.; Jenkins, J. A.; Mackie, A. R.; Wilde, P. J.; Mills, E. N. C.; Smith, L. J. Heat treatment of bovine α-lactalbumin results in partially folded, disulfide bond shuffled states with enhanced surface activity Biochemistry 2007, 46, 9774-9784
    • (2007) Biochemistry , vol.46 , pp. 9774-9784
    • Wijesinha-Bettoni, R.1    Gao, C.2    Jenkins, J.A.3    MacKie, A.R.4    Wilde, P.J.5    Mills, E.N.C.6    Smith, L.J.7
  • 12
    • 25144518570 scopus 로고    scopus 로고
    • Effect of thermal treatment on interfacial properties of β-lactoglobulin
    • Kim, D. A.; Cornec, M.; Narsimhan, G. Effect of thermal treatment on interfacial properties of β-lactoglobulin J. Colloid Interface Sci. 2005, 285, 100-109
    • (2005) J. Colloid Interface Sci. , vol.285 , pp. 100-109
    • Kim, D.A.1    Cornec, M.2    Narsimhan, G.3
  • 14
    • 34247360046 scopus 로고    scopus 로고
    • Whey protein soluble aggregates from heating with NaCl: Physicochemical, interfacial, and foaming properties
    • 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 2007, 23, 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
  • 15
    • 79952112477 scopus 로고    scopus 로고
    • Interfacial activity and interfacial shear rheology of native β-lactoglobulin monomers and their heat-induced fibers
    • Jung, J. M.; Gunes, D. Z.; Mezzenga, R. Interfacial activity and interfacial shear rheology of native β-lactoglobulin monomers and their heat-induced fibers Langmuir 2010, 26, 15366-15375
    • (2010) Langmuir , vol.26 , pp. 15366-15375
    • Jung, J.M.1    Gunes, D.Z.2    Mezzenga, R.3
  • 16
    • 84857329292 scopus 로고    scopus 로고
    • Interfacial properties of fractal and spherical whey protein aggregates
    • Mahmoudi, N.; Axelos, M. A. V.; Riaublanc, A. Interfacial properties of fractal and spherical whey protein aggregates Soft Matter 2011, 7, 7643-7654
    • (2011) Soft Matter , vol.7 , pp. 7643-7654
    • Mahmoudi, N.1    Axelos, M.A.V.2    Riaublanc, A.3
  • 17
    • 77957808647 scopus 로고    scopus 로고
    • Freeze-thaw stability of oil-in-water emulsions prepared with native and thermally-denatured soybean isolates
    • Palazolo, G. G.; Sobral, P. A.; Wagner, J. R. Freeze-thaw stability of oil-in-water emulsions prepared with native and thermally-denatured soybean isolates Food Hydrocolloids 2011, 25, 398-409
    • (2011) Food Hydrocolloids , vol.25 , pp. 398-409
    • Palazolo, G.G.1    Sobral, P.A.2    Wagner, J.R.3
  • 18
    • 0141607037 scopus 로고    scopus 로고
    • Effect of pH on structural, topographical, and dynamic characteristics of soy globulin films at the air-water interface
    • Sanchez, C. C.; Ortiz, S. E. M.; Niño, M. R. R.; Añón, M. C.; Patino, J. M. R. Effect of pH on structural, topographical, and dynamic characteristics of soy globulin films at the air-water interface Langmuir 2003, 19, 7478-7487
    • (2003) Langmuir , vol.19 , pp. 7478-7487
    • Sanchez, C.C.1    Ortiz, S.E.M.2    Niño, M.R.R.3    Añón, M.C.4    Patino, J.M.R.5
  • 19
    • 39149111921 scopus 로고    scopus 로고
    • Preparation of soluble soybean protein aggregates (SSPA) from insoluble soybean protein concentrates (SPC) and its functional properties
    • Zheng, H. G.; Yang, X. Q.; Tang, C. H.; Li, L.; Ahmad, I. Preparation of soluble soybean protein aggregates (SSPA) from insoluble soybean protein concentrates (SPC) and its functional properties Food Res. Int. 2008, 41, 154-164
    • (2008) Food Res. Int. , vol.41 , pp. 154-164
    • Zheng, H.G.1    Yang, X.Q.2    Tang, C.H.3    Li, L.4    Ahmad, I.5
  • 20
    • 30344460965 scopus 로고    scopus 로고
    • Effect of alkali on the refunctionalization of soy protein by hydrothermal cooking
    • Wang, H.; Wang, T.; Johnson, L. A. Effect of alkali on the refunctionalization of soy protein by hydrothermal cooking J. Am. Oil Chem. Soc. 2005, 82, 451-456
    • (2005) J. Am. Oil Chem. Soc. , vol.82 , pp. 451-456
    • Wang, H.1    Wang, T.2    Johnson, L.A.3
  • 21
    • 0024715168 scopus 로고
    • Interracial tensions of vegetable oil/water systems: Effect of oil purification
    • Gaonkar, A. G. Interracial tensions of vegetable oil/water systems: Effect of oil purification J. Am. Oil Chem. Soc. 1989, 66, 1090-1092
    • (1989) J. Am. Oil Chem. Soc. , vol.66 , pp. 1090-1092
    • Gaonkar, A.G.1
  • 23
    • 0002252081 scopus 로고
    • Data analysis in dynamic light scattering
    • In; Brown, W. Oxford University Press: Oxford
    • Stepanek, P. Data analysis in dynamic light scattering. In Dynamic Light Scattering, The Methods and Some Applications; Brown, W., Eds.; Oxford University Press: Oxford, 1993; pp 177-241.
    • (1993) Dynamic Light Scattering, the Methods and Some Applications , pp. 177-241
    • Stepanek, P.1
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of Bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of Bacteriophage T4 Nature 1970, 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 85032119438 scopus 로고
    • Determination of SH- and SS-groups in some food proteins using Ellman's reagent
    • Beveridge, T.; Toma, S. J.; Nakai, S. Determination of SH- and SS-groups in some food proteins using Ellman's reagent J. Food Sci. 1974, 39, 49-51
    • (1974) J. Food Sci. , vol.39 , pp. 49-51
    • Beveridge, T.1    Toma, S.J.2    Nakai, S.3
  • 27
    • 36849122851 scopus 로고
    • Time dependence of boundary tensions of solutions. I. The role of diffusion in time effects
    • Ward, A. F. H.; Tordai, L. Time dependence of boundary tensions of solutions. I. The role of diffusion in time effects J. Chem. Phys. 1946, 14, 453-461
    • (1946) J. Chem. Phys. , vol.14 , pp. 453-461
    • Ward, A.F.H.1    Tordai, L.2
  • 28
    • 79952535945 scopus 로고    scopus 로고
    • Dynamic surface pressure and dilatational viscoelasticity of sodium caseinate/xanthan gum mixtures at the oil-water interface
    • Liu, L. Y.; Zhao, Q. Z.; Liu, T. X.; Zhao, M. M. Dynamic surface pressure and dilatational viscoelasticity of sodium caseinate/xanthan gum mixtures at the oil-water interface Food Hydrocolloids 2011, 25, 921-927
    • (2011) Food Hydrocolloids , vol.25 , pp. 921-927
    • Liu, L.Y.1    Zhao, Q.Z.2    Liu, T.X.3    Zhao, M.M.4
  • 29
    • 0642298935 scopus 로고
    • Dynamic measurements of dilatational properties of a liquid interface
    • Lucassen, J.; Van den Tempel, M. Dynamic measurements of dilatational properties of a liquid interface Chem. Eng. Sci. 1972, 27, 1283-1291
    • (1972) Chem. Eng. Sci. , vol.27 , pp. 1283-1291
    • Lucassen, J.1    Van Den Tempel, M.2
  • 30
    • 84907421469 scopus 로고
    • Thermal aggregation of soy protein isolates
    • Petruccelli, S.; Añón, M. C. Thermal aggregation of soy protein isolates J. Agric. Food Chem. 1995, 43, 3035-3041
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 3035-3041
    • Petruccelli, S.1    Añón, M.C.2
  • 32
    • 0030324821 scopus 로고    scopus 로고
    • X-ray solution scattering studies of protein folding
    • Kataoka, M.; Goto, Y. X-ray solution scattering studies of protein folding Fold Des. 1996, 1, R107-R114
    • (1996) Fold Des. , vol.1
    • Kataoka, M.1    Goto, Y.2
  • 34
    • 79956319910 scopus 로고    scopus 로고
    • Structure of β-lactoglobulin microgels formed during heating as revealed by small-angle X-ray scattering and light scattering
    • Moitzi, C.; Donato, L.; Schmitt, C.; Bovetto, L.; Gillies, G.; Stradner, A. Structure of β-lactoglobulin microgels formed during heating as revealed by small-angle X-ray scattering and light scattering Food Hydrocolloids 2011, 25, 1766-1774
    • (2011) Food Hydrocolloids , vol.25 , pp. 1766-1774
    • Moitzi, C.1    Donato, L.2    Schmitt, C.3    Bovetto, L.4    Gillies, G.5    Stradner, A.6
  • 35
    • 79851478055 scopus 로고    scopus 로고
    • Denaturation of soy proteins in solution and at the oil/water interface: A fluorescence study
    • Miriani, M.; Keerati-u-rai, M.; Corredig, M.; Iametti, S.; Bonomi, F. Denaturation of soy proteins in solution and at the oil/water interface: A fluorescence study Food Hydrocolloids 2011, 25, 620-626
    • (2011) Food Hydrocolloids , vol.25 , pp. 620-626
    • Miriani, M.1    Keerati-U-Rai, M.2    Corredig, M.3    Iametti, S.4    Bonomi, F.5
  • 36
    • 0033934051 scopus 로고    scopus 로고
    • Heat denaturation of soy glycinin: Influence of pH and ionic strength on molecular structure
    • Lakemond, C. M. M.; De Jongh, H. H. J.; Hessing, M.; Gruppen, H.; Voragen, A. G. J. Heat denaturation of soy glycinin: Influence of pH and ionic strength on molecular structure J. Agric. Food Chem. 2000, 48, 1991-1995
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 1991-1995
    • Lakemond, C.M.M.1    De Jongh, H.H.J.2    Hessing, M.3    Gruppen, H.4    Voragen, A.G.J.5
  • 38
    • 0141828635 scopus 로고    scopus 로고
    • Dynamic interfacial rheology as a tool for the characterization of whey protein isolates gelation at the oil-water interface
    • Patino, J. M. R.; Niño, M. R. R.; Sanchez, C. C. Dynamic interfacial rheology as a tool for the characterization of whey protein isolates gelation at the oil-water interface J. Agric. Food Chem. 1999, 47, 3640-3648
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 3640-3648
    • Patino, J.M.R.1    Niño, M.R.R.2    Sanchez, C.C.3
  • 39
    • 0025505415 scopus 로고
    • Effect of heat denaturation on the adsorption of β -lactoglobulin at the oil/water interface and on coalescence stability of emulsions
    • Das, K. P.; Kinsella, J. E. Effect of heat denaturation on the adsorption of β -lactoglobulin at the oil/water interface and on coalescence stability of emulsions J. Colloid Interface Sci. 1990, 139, 551-560
    • (1990) J. Colloid Interface Sci. , vol.139 , pp. 551-560
    • Das, K.P.1    Kinsella, J.E.2
  • 40
    • 0035958458 scopus 로고    scopus 로고
    • Interfacial rheological properties of adsorbed protein layers and surfactants: A review
    • Bos, M. A.; van Vliet, T. Interfacial rheological properties of adsorbed protein layers and surfactants: A review Adv. Colloid Interface Sci. 2001, 91, 437-471
    • (2001) Adv. Colloid Interface Sci. , vol.91 , pp. 437-471
    • Bos, M.A.1    Van Vliet, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.