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Volumn 90, Issue 2, 2009, Pages 207-211

Rheological behavior of wheat gliadins in 50% (v/v) aqueous propanol

Author keywords

Gliadin; Intrinsic viscosity; Rheological properties

Indexed keywords

CONCENTRATION (PROCESS);

EID: 49749144748     PISSN: 02608774     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jfoodeng.2008.06.024     Document Type: Article
Times cited : (4)

References (66)
  • 1
    • 0015986089 scopus 로고
    • Influence of temperature on the intrinsic viscosities of proteins in random coil conformation
    • Ahmad F., and Salahuddin A. Influence of temperature on the intrinsic viscosities of proteins in random coil conformation. Biochemistry 13 (1974) 245-249
    • (1974) Biochemistry , vol.13 , pp. 245-249
    • Ahmad, F.1    Salahuddin, A.2
  • 3
    • 0035364761 scopus 로고    scopus 로고
    • Two-state protein model with water interactions: Influence of temperature on the intrinsic viscosity of myoglobin
    • Bakk A. Two-state protein model with water interactions: Influence of temperature on the intrinsic viscosity of myoglobin. Physical Review E 63 (2001) 0619061-0629065
    • (2001) Physical Review E , vol.63 , pp. 0619061-0629065
    • Bakk, A.1
  • 4
    • 0000339927 scopus 로고
    • Functional properties of glycosylated derivatives of the 11S storage protein from pea (Pisum sativum L.)
    • Baniel A., Caer D., Colas B., and Gueguen J. Functional properties of glycosylated derivatives of the 11S storage protein from pea (Pisum sativum L.). Journal of Agricultural and Food Chemistry 40 (1992) 200-205
    • (1992) Journal of Agricultural and Food Chemistry , vol.40 , pp. 200-205
    • Baniel, A.1    Caer, D.2    Colas, B.3    Gueguen, J.4
  • 6
    • 0000680248 scopus 로고    scopus 로고
    • Coil-globule transition of poly(methyl methacrylate) by intrinsic viscosity
    • Baysal B.M., and Kayaman N. Coil-globule transition of poly(methyl methacrylate) by intrinsic viscosity. Journal of Chemical Physics 109 (1998) 8701-8707
    • (1998) Journal of Chemical Physics , vol.109 , pp. 8701-8707
    • Baysal, B.M.1    Kayaman, N.2
  • 7
    • 0038290455 scopus 로고    scopus 로고
    • New insight into the solution structures of wheat gluten proteins from Raman optical activity
    • Blanch E.W., Kasarda D.D., Hecht L., Nielsen K., and Barron L.D. New insight into the solution structures of wheat gluten proteins from Raman optical activity. Biochemistry 42 (2003) 5665-5673
    • (2003) Biochemistry , vol.42 , pp. 5665-5673
    • Blanch, E.W.1    Kasarda, D.D.2    Hecht, L.3    Nielsen, K.4    Barron, L.D.5
  • 8
    • 0031974150 scopus 로고    scopus 로고
    • Light scattering and viscosity study of heat aggregation of insulin
    • Bohidar H.B. Light scattering and viscosity study of heat aggregation of insulin. Biopolymers 45 (1998) 1-8
    • (1998) Biopolymers , vol.45 , pp. 1-8
    • Bohidar, H.B.1
  • 9
    • 0035183519 scopus 로고    scopus 로고
    • Acid-induced gelation of whey protein polymers: effects of pH and calcium concentration during polymerization
    • Britten M., and Giroux H.J. Acid-induced gelation of whey protein polymers: effects of pH and calcium concentration during polymerization. Food Hydrocolloids 15 (2001) 609-617
    • (2001) Food Hydrocolloids , vol.15 , pp. 609-617
    • Britten, M.1    Giroux, H.J.2
  • 11
    • 0021176063 scopus 로고
    • The conformational structure of A-gliadin: intrinsic viscosities under conditions approaching the native state and under denaturing conditions
    • Cole E.W., Kasarda D.D., and Lafiandra D. The conformational structure of A-gliadin: intrinsic viscosities under conditions approaching the native state and under denaturing conditions. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 787 (1984) 244-251
    • (1984) Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology , vol.787 , pp. 244-251
    • Cole, E.W.1    Kasarda, D.D.2    Lafiandra, D.3
  • 13
  • 15
    • 0345578674 scopus 로고    scopus 로고
    • Molecular structures and interactions of repetitive peptides based on wheat glutenin subunits depend on chain length
    • Feeney K.A., Wellner N., Gilbert S.M., Halford N.G., Tatham A.S., Shewry P.R., and Belton P.S. Molecular structures and interactions of repetitive peptides based on wheat glutenin subunits depend on chain length. Biopolymers 72 (2003) 123-131
    • (2003) Biopolymers , vol.72 , pp. 123-131
    • Feeney, K.A.1    Wellner, N.2    Gilbert, S.M.3    Halford, N.G.4    Tatham, A.S.5    Shewry, P.R.6    Belton, P.S.7
  • 18
    • 33644606321 scopus 로고    scopus 로고
    • Effects of temperature and water content on the secondary structure of wheat gluten studied by FTIR spectroscopy
    • Georget D.M.R., and Belton P.S. Effects of temperature and water content on the secondary structure of wheat gluten studied by FTIR spectroscopy. Biomacromolecules 7 (2006) 469-475
    • (2006) Biomacromolecules , vol.7 , pp. 469-475
    • Georget, D.M.R.1    Belton, P.S.2
  • 19
    • 33748472742 scopus 로고    scopus 로고
    • Intrinsic viscosity of proteins and platonic solids by boundary element methods
    • Hahn D.K., and Aragon S.R. Intrinsic viscosity of proteins and platonic solids by boundary element methods. Journal of Chemical Theory and Computation 2 (2006) 1416-1428
    • (2006) Journal of Chemical Theory and Computation , vol.2 , pp. 1416-1428
    • Hahn, D.K.1    Aragon, S.R.2
  • 20
    • 0031580203 scopus 로고    scopus 로고
    • The equilibrium intermediate of β-lactoglobulin with non-native alpha-helical structure
    • Hamada D., and Goto Y. The equilibrium intermediate of β-lactoglobulin with non-native alpha-helical structure. Journal of Molecular Biology 269 (1997) 479-487
    • (1997) Journal of Molecular Biology , vol.269 , pp. 479-487
    • Hamada, D.1    Goto, Y.2
  • 22
    • 7144264367 scopus 로고
    • The viscosity of dilute solutions of long-chain molecules. IV. Dependence of concentration
    • Huggins M.L. The viscosity of dilute solutions of long-chain molecules. IV. Dependence of concentration. Journal of the American Chemical Society 64 (1942) 2716-2718
    • (1942) Journal of the American Chemical Society , vol.64 , pp. 2716-2718
    • Huggins, M.L.1
  • 23
    • 0036314614 scopus 로고    scopus 로고
    • Functional properties of wheat gliadins. II. Effects on dynamic rheological properties of wheat gluten
    • Khatkar B.S., Fido R.J., Tatham A.S., and Schofield J.D. Functional properties of wheat gliadins. II. Effects on dynamic rheological properties of wheat gluten. Journal of Cereal Science 35 (2002) 307-313
    • (2002) Journal of Cereal Science , vol.35 , pp. 307-313
    • Khatkar, B.S.1    Fido, R.J.2    Tatham, A.S.3    Schofield, J.D.4
  • 24
    • 34047259662 scopus 로고    scopus 로고
    • Effect of hydrostatic pressure and temperature on the chemical and functional properties of wheat gluten: studies on gluten, gliadin and glutenin
    • Kieffer R., Schurer F., Kohler P., and Wieser H. Effect of hydrostatic pressure and temperature on the chemical and functional properties of wheat gluten: studies on gluten, gliadin and glutenin. Journal of Cereal Science 45 (2007) 285-292
    • (2007) Journal of Cereal Science , vol.45 , pp. 285-292
    • Kieffer, R.1    Schurer, F.2    Kohler, P.3    Wieser, H.4
  • 25
    • 0034894250 scopus 로고    scopus 로고
    • Rheology of sodium hyaluronate under physiological conditions
    • Krause W.E., Bellomo E.G., and Colby R.H. Rheology of sodium hyaluronate under physiological conditions. Biomacromolecules 2 (2001) 65-69
    • (2001) Biomacromolecules , vol.2 , pp. 65-69
    • Krause, W.E.1    Bellomo, E.G.2    Colby, R.H.3
  • 27
    • 27944445476 scopus 로고    scopus 로고
    • Intrinsic viscosity of polymers and biopolymers measured by microchip
    • Lee J., and Tripathi A. Intrinsic viscosity of polymers and biopolymers measured by microchip. Analytical Chemistry 77 (2005) 7137-7147
    • (2005) Analytical Chemistry , vol.77 , pp. 7137-7147
    • Lee, J.1    Tripathi, A.2
  • 28
    • 33746498447 scopus 로고    scopus 로고
    • Polymer conformation structure of wheat proteins and gluten subfractions revealed by ATR-FTIR
    • Li W., Dobraszczky B.J., Dias A., and Gil A.M. Polymer conformation structure of wheat proteins and gluten subfractions revealed by ATR-FTIR. Cereal Chemistry 83 (2006) 407-410
    • (2006) Cereal Chemistry , vol.83 , pp. 407-410
    • Li, W.1    Dobraszczky, B.J.2    Dias, A.3    Gil, A.M.4
  • 29
    • 2042468797 scopus 로고    scopus 로고
    • Viscoelastic and small angle neutron scattering studies of concentrated protein solutions
    • Lonetti B., Fratini E., Chen S.H., and Baglioni P. Viscoelastic and small angle neutron scattering studies of concentrated protein solutions. Physical Chemistry Chemical Physics 6 (2004) 1388-1395
    • (2004) Physical Chemistry Chemical Physics , vol.6 , pp. 1388-1395
    • Lonetti, B.1    Fratini, E.2    Chen, S.H.3    Baglioni, P.4
  • 30
    • 1542357641 scopus 로고    scopus 로고
    • Effect of moisture content on viscoelastic properties of hydrated gliadin
    • Martling S.E., Mulvaney S.J., and Cohen C. Effect of moisture content on viscoelastic properties of hydrated gliadin. Cereal Chemistry 81 (2004) 207-219
    • (2004) Cereal Chemistry , vol.81 , pp. 207-219
    • Martling, S.E.1    Mulvaney, S.J.2    Cohen, C.3
  • 34
    • 0030025770 scopus 로고    scopus 로고
    • Viscosity of bovine serum albumin aqueous solutions as a function of temperature and concentration
    • Monkos K. Viscosity of bovine serum albumin aqueous solutions as a function of temperature and concentration. International Journal of Biological Macromolecules 18 (1996) 61-68
    • (1996) International Journal of Biological Macromolecules , vol.18 , pp. 61-68
    • Monkos, K.1
  • 37
    • 0034737923 scopus 로고    scopus 로고
    • Viscosity analysis of the temperature dependence of the solution conformation of ovalbumin
    • Monkos K. Viscosity analysis of the temperature dependence of the solution conformation of ovalbumin. Biophysical Chemistry 85 (2000) 7-16
    • (2000) Biophysical Chemistry , vol.85 , pp. 7-16
    • Monkos, K.1
  • 38
    • 2942738911 scopus 로고    scopus 로고
    • On the hydrodynamics and temperature dependence of the solution conformation of human serum albumin from viscometry approach
    • Monkos K. On the hydrodynamics and temperature dependence of the solution conformation of human serum albumin from viscometry approach. Biochimica et Biophysica Acta - Proteins and Proteomics 1700 (2004) 27-34
    • (2004) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1700 , pp. 27-34
    • Monkos, K.1
  • 39
    • 14744293870 scopus 로고    scopus 로고
    • A comparison of solution conformation and hydrodynamic properties of equine, porcine and rabbit serum albumin using viscometric measurements
    • Monkos K. A comparison of solution conformation and hydrodynamic properties of equine, porcine and rabbit serum albumin using viscometric measurements. Biochimica et Biophysica Acta - Proteins and Proteomics 1748 (2005) 100-109
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1748 , pp. 100-109
    • Monkos, K.1
  • 40
    • 23844451240 scopus 로고    scopus 로고
    • Determination of some hydrodynamic parameters of ovine serum albumin solutions using viscometric measurements
    • Monkos K. Determination of some hydrodynamic parameters of ovine serum albumin solutions using viscometric measurements. Journal of Biological Physics 31 (2005) 219-232
    • (2005) Journal of Biological Physics , vol.31 , pp. 219-232
    • Monkos, K.1
  • 41
    • 0032819751 scopus 로고    scopus 로고
    • A comparative study on viscosity of human, bovine and pig IgG immunoglobulins in aqueous solutions
    • Monkos K., and Turczynski B. A comparative study on viscosity of human, bovine and pig IgG immunoglobulins in aqueous solutions. International Journal of Biological Macromolecules 26 (1999) 155-159
    • (1999) International Journal of Biological Macromolecules , vol.26 , pp. 155-159
    • Monkos, K.1    Turczynski, B.2
  • 42
    • 12144272437 scopus 로고    scopus 로고
    • Rheological properties of a surfactant-induced gel for the lysozyme-sodium dodecyl sulfate-water system
    • Montalvo G., and Khan A. Rheological properties of a surfactant-induced gel for the lysozyme-sodium dodecyl sulfate-water system. Colloid and Polymer Science 283 (2005) 402-412
    • (2005) Colloid and Polymer Science , vol.283 , pp. 402-412
    • Montalvo, G.1    Khan, A.2
  • 44
    • 0026576158 scopus 로고
    • Conformation of wheat gluten proteins - Comparison between functional and solution states as determined by infrared spectroscopy
    • Pezolet M., Bonenfant S., Dousseau F., and Popineau Y. Conformation of wheat gluten proteins - Comparison between functional and solution states as determined by infrared spectroscopy. FEBS Letters 299 (1992) 247-250
    • (1992) FEBS Letters , vol.299 , pp. 247-250
    • Pezolet, M.1    Bonenfant, S.2    Dousseau, F.3    Popineau, Y.4
  • 46
    • 0001688114 scopus 로고
    • Blackie Academic and Professional, New York
    • Ross-Murphy S.B. Rheological method (1994), Blackie Academic and Professional, New York
    • (1994) Rheological method
    • Ross-Murphy, S.B.1
  • 48
    • 84982585010 scopus 로고
    • Modification of the oligomeric structure of 11s globulins from sunflower (Helianthus annus L.) and rape (Brassica napus L.) seeds by succinylation
    • Schwenke K.D., Linow K.J., and Zirwer D. Modification of the oligomeric structure of 11s globulins from sunflower (Helianthus annus L.) and rape (Brassica napus L.) seeds by succinylation. Nahrung 30 (1986) 263-270
    • (1986) Nahrung , vol.30 , pp. 263-270
    • Schwenke, K.D.1    Linow, K.J.2    Zirwer, D.3
  • 49
    • 33847797569 scopus 로고
    • Solubility profile, intrinsic viscosity, and optical rotation studies of acid precipitated soy protein and of commercial soy isolate
    • Shen J.L. Solubility profile, intrinsic viscosity, and optical rotation studies of acid precipitated soy protein and of commercial soy isolate. Journal of Agricultural and Food Chemistry 24 (1976) 748-788
    • (1976) Journal of Agricultural and Food Chemistry , vol.24 , pp. 748-788
    • Shen, J.L.1
  • 52
    • 54849412818 scopus 로고    scopus 로고
    • Sun, S., Song, Y., Zheng, Q., in press. Morphology and mechanical properties of thermo-molded bioplastics based on glycerol-plasticized wheat gliadins. Journal of Cereal Science doi:10.1016/j.jcs.2008.01.005.
    • Sun, S., Song, Y., Zheng, Q., in press. Morphology and mechanical properties of thermo-molded bioplastics based on glycerol-plasticized wheat gliadins. Journal of Cereal Science doi:10.1016/j.jcs.2008.01.005.
  • 53
    • 40749156196 scopus 로고    scopus 로고
    • pH-induced rheological changes for semi-dilute solutions of wheat gliadins
    • Sun S., Song Y., and Zheng Q. pH-induced rheological changes for semi-dilute solutions of wheat gliadins. Food Hydrocolloids 22 (2008) 1090-1096
    • (2008) Food Hydrocolloids , vol.22 , pp. 1090-1096
    • Sun, S.1    Song, Y.2    Zheng, Q.3
  • 54
    • 0006546601 scopus 로고
    • Viscosity study of the collapse state of a polystyrene
    • Sun S.F., Chou C.-C., and Nash R.A. Viscosity study of the collapse state of a polystyrene. Journal of Chemical Physics 93 (1990) 7508-7509
    • (1990) Journal of Chemical Physics , vol.93 , pp. 7508-7509
    • Sun, S.F.1    Chou, C.-C.2    Nash, R.A.3
  • 56
    • 0000041974 scopus 로고
    • Intrinsic viscosity and kinematic viscosity
    • Tanford C. Intrinsic viscosity and kinematic viscosity. Journal of Physical Chemistry 59 (1955) 798-799
    • (1955) Journal of Physical Chemistry , vol.59 , pp. 798-799
    • Tanford, C.1
  • 57
    • 0000697562 scopus 로고
    • Proteins as random coils. I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride
    • Tanford C., Kawahara K., and Lapanje S. Proteins as random coils. I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride. Journal of the American Chemical Society 89 (1967) 729-736
    • (1967) Journal of the American Chemical Society , vol.89 , pp. 729-736
    • Tanford, C.1    Kawahara, K.2    Lapanje, S.3
  • 58
    • 0001211660 scopus 로고
    • The conformations of wheat gluten proteins. The secondary structures and thermal stabilities of the α-, β-, γ-, and ω-gliadins
    • Tatham A.S., and Shewry P.R. The conformations of wheat gluten proteins. The secondary structures and thermal stabilities of the α-, β-, γ-, and ω-gliadins. Journal of Cereal Science 3 (1985) 103-113
    • (1985) Journal of Cereal Science , vol.3 , pp. 103-113
    • Tatham, A.S.1    Shewry, P.R.2
  • 60
    • 0032876123 scopus 로고    scopus 로고
    • Rheological properties and characterization of polymerized whey protein isolates
    • Vardhanabhuti B., and Foegeding E.A. Rheological properties and characterization of polymerized whey protein isolates. Journal of Agricultural and Food Chemistry 47 (1999) 3649-3655
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , pp. 3649-3655
    • Vardhanabhuti, B.1    Foegeding, E.A.2
  • 62
    • 0037174466 scopus 로고    scopus 로고
    • Modification of the rheological properties of whey protein isolate through the use of an immobilized microbial transglutaminase
    • Wilcox C.P., and Swaisgood H.E. Modification of the rheological properties of whey protein isolate through the use of an immobilized microbial transglutaminase. Journal of Agricultural and Food Chemistry 50 (2002) 5546-5551
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , pp. 5546-5551
    • Wilcox, C.P.1    Swaisgood, H.E.2
  • 63
    • 0014209825 scopus 로고
    • Effect of ionic strength on the molecular weight and conformation of wheat gluten proteins in 3 M urea solutions
    • Wu Y.V., Cluskey J.E., and Sexson K.R. Effect of ionic strength on the molecular weight and conformation of wheat gluten proteins in 3 M urea solutions. Biochimica et Biophysica Acta (BBA) - Protein Structure 133 (1967) 83-90
    • (1967) Biochimica et Biophysica Acta (BBA) - Protein Structure , vol.133 , pp. 83-90
    • Wu, Y.V.1    Cluskey, J.E.2    Sexson, K.R.3
  • 64
    • 0000114965 scopus 로고
    • Conformational studies of wheat gluten, glutenin, and gliadin in urea solutions at various pH's
    • Wu Y.V., and Dimler R.J. Conformational studies of wheat gluten, glutenin, and gliadin in urea solutions at various pH's. Archives of Biochemistry and Biophysics 107 (1964) 435-440
    • (1964) Archives of Biochemistry and Biophysics , vol.107 , pp. 435-440
    • Wu, Y.V.1    Dimler, R.J.2
  • 65
    • 33748788515 scopus 로고    scopus 로고
    • Viscoelastic properties of wheat gliadin and glutenin suspensions
    • Xu J., Bietz J.A., and Carriere C.J. Viscoelastic properties of wheat gliadin and glutenin suspensions. Food Chemistry 101 (2007) 1025-1030
    • (2007) Food Chemistry , vol.101 , pp. 1025-1030
    • Xu, J.1    Bietz, J.A.2    Carriere, C.J.3
  • 66
    • 0242606894 scopus 로고    scopus 로고
    • Molecular modeling of various peptide sequences of gliadins and low-molecular-weight glutenin subunits
    • Yasar F., Celik S., and Koksel H. Molecular modeling of various peptide sequences of gliadins and low-molecular-weight glutenin subunits. Nahrung-Food 47 (2003) 238-242
    • (2003) Nahrung-Food , vol.47 , pp. 238-242
    • Yasar, F.1    Celik, S.2    Koksel, H.3


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