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Volumn 55, Issue 18, 2007, Pages 7244-7251

Analysis of protein structures and interactions in complex food by near-infrared spectroscopy. 2. Hydrated gluten

Author keywords

Chemometrics; Extended multiplicative scatter correction (EMSC); Gluten; Hofmeister series; Near infrared spectroscopy (NIR); Principal component analysis (PCA); Protein interaction; Protein secondary structure; Spectral pretreatment

Indexed keywords

GLUTEN; SULFATE; WATER;

EID: 34848814730     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf063724o     Document Type: Article
Times cited : (24)

References (32)
  • 1
    • 0002527919 scopus 로고    scopus 로고
    • Structure-property relationships in foods
    • Parris, N, Kato, A, Creamer, L. K, Pearce, J, Eds, American Chemical Society: Washington, DC
    • Tolstoguzov, V. Structure-property relationships in foods. In Macromolecular Interactions in Food Technology; Parris, N., Kato, A., Creamer, L. K., Pearce, J., Eds.; American Chemical Society: Washington, DC, 1996; pp 2-14.
    • (1996) Macromolecular Interactions in Food Technology , pp. 2-14
    • Tolstoguzov, V.1
  • 2
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth, A.; Zscherp, C. What vibrations tell us about proteins. Q. Rev. Biophys. 2002, 35, 369-430.
    • (2002) Q. Rev. Biophys , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 3
    • 0026576158 scopus 로고
    • Functional and solution states as determined by infrared-spectroscopy
    • Pezolet, M.; Bonenfant, S.; Dousseau, F.; Popineau, Y. Functional and solution states as determined by infrared-spectroscopy. FEBS Lett. 1992, 299, 247-250.
    • (1992) FEBS Lett , vol.299 , pp. 247-250
    • Pezolet, M.1    Bonenfant, S.2    Dousseau, F.3    Popineau, Y.4
  • 4
    • 12544256285 scopus 로고    scopus 로고
    • New approaches to study the molecular basis of the mechanical properties of gluten
    • Belton, P. S. New approaches to study the molecular basis of the mechanical properties of gluten. J. Cereal Sci. 2005, 41, 203-211.
    • (2005) J. Cereal Sci , vol.41 , pp. 203-211
    • Belton, P.S.1
  • 5
    • 0001920021 scopus 로고    scopus 로고
    • On the elasticity of wheat gluten
    • Belton, P. S. On the elasticity of wheat gluten. J. Cereal Sci. 1999, 29, 103-107.
    • (1999) J. Cereal Sci , vol.29 , pp. 103-107
    • Belton, P.S.1
  • 6
    • 0037772186 scopus 로고    scopus 로고
    • Factors associated with dough stickiness as sensed by attenuated total reflectance infrared spectroscopy
    • Van Velzen, E. J. J.; van Duynhoven, J. P. M.; Weegels, P. L.; van der Maas, J. H. Factors associated with dough stickiness as sensed by attenuated total reflectance infrared spectroscopy. Cereal Chem. 2003, 80, 378-382.
    • (2003) Cereal Chem , vol.80 , pp. 378-382
    • Van Velzen, E.J.J.1    van Duynhoven, J.P.M.2    Weegels, P.L.3    van der Maas, J.H.4
  • 8
    • 34848857912 scopus 로고    scopus 로고
    • Analysis of protein structures and interactions in complex food by near-infrared spectroscopy. 1. Gluten powder
    • Bruun, S.; Søndergaard, I.; Jacobsen, S. Analysis of protein structures and interactions in complex food by near-infrared spectroscopy. 1. Gluten powder. J. Agrie. Food Chem. 2007, 55, 7234-7243.
    • (2007) J. Agrie. Food Chem , vol.55 , pp. 7234-7243
    • Bruun, S.1    Søndergaard, I.2    Jacobsen, S.3
  • 9
    • 0033075461 scopus 로고    scopus 로고
    • Monitoring the secondary structure of proteins by near-infrared spectroscopy
    • Robert, P.; Devaux, M. F.; Mouhous, N.; Dufour, E. Monitoring the secondary structure of proteins by near-infrared spectroscopy. Appl. Spectrosc. 1999, 53, 226-232.
    • (1999) Appl. Spectrosc , vol.53 , pp. 226-232
    • Robert, P.1    Devaux, M.F.2    Mouhous, N.3    Dufour, E.4
  • 10
    • 27644477359 scopus 로고    scopus 로고
    • Noninvasive determination of protein conformation in the solid state using near infrared (NIR) spectroscopy
    • Bai, S. J.; Nayar, R.; Carpenter, J. F.; Manning, M. C. Noninvasive determination of protein conformation in the solid state using near infrared (NIR) spectroscopy. J. Pharm. Sci. 2005, 94, 2030-2038.
    • (2005) J. Pharm. Sci , vol.94 , pp. 2030-2038
    • Bai, S.J.1    Nayar, R.2    Carpenter, J.F.3    Manning, M.C.4
  • 11
    • 0000857228 scopus 로고    scopus 로고
    • Two-dimensional Fourier transform near-infrared spectroscopy study of heat denaturation of ovalbumin in aqueous solutions
    • Wang, Y.; Murayama, K.; Myojo, Y.; Tsenkova, R.; Hayashi, N.; Ozaki, Y. Two-dimensional Fourier transform near-infrared spectroscopy study of heat denaturation of ovalbumin in aqueous solutions. J. Phys. Chem. B 1998, 102, 6655-6662.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 6655-6662
    • Wang, Y.1    Murayama, K.2    Myojo, Y.3    Tsenkova, R.4    Hayashi, N.5    Ozaki, Y.6
  • 12
    • 0033700031 scopus 로고    scopus 로고
    • Two-dimensional near-infrared spectroscopy study of human serum albumin in aqueous solutions: Using overtones and combination modes to monitor temperature-dependent changes in the secondary structure
    • Wu, Y. Q.; Czarnik-Matusewicz, B.; Murayama, K.; Ozaki, Y. Two-dimensional near-infrared spectroscopy study of human serum albumin in aqueous solutions: Using overtones and combination modes to monitor temperature-dependent changes in the secondary structure. J. Phys. Chem. B 2000, 104, 5840-5847.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 5840-5847
    • Wu, Y.Q.1    Czarnik-Matusewicz, B.2    Murayama, K.3    Ozaki, Y.4
  • 13
    • 0035985093 scopus 로고    scopus 로고
    • Wheat protein composition and properties of wheat glutenin in relation to breadmaking functionality
    • Veraverbeke, W. S.; Delcour, J. A. Wheat protein composition and properties of wheat glutenin in relation to breadmaking functionality. Crit. Rev. Food Sci. 2002, 42, 179-208.
    • (2002) Crit. Rev. Food Sci , vol.42 , pp. 179-208
    • Veraverbeke, W.S.1    Delcour, J.A.2
  • 14
    • 0001807851 scopus 로고    scopus 로고
    • Interactions in wheat doughs
    • Chapter 1, Hamer, R. J, Hoseney, R. C, Eds, AACC: St. Paul, MN
    • Bushuk, W. Interactions in wheat doughs. Chapter 1. In Interactions: The Key to Cereal Quality; Hamer, R. J., Hoseney, R. C., Eds.; AACC: St. Paul, MN, 1998; pp 1-16.
    • (1998) Interactions: The Key to Cereal Quality , pp. 1-16
    • Bushuk, W.1
  • 15
    • 0001173905 scopus 로고
    • Hydrophobic associations and gluten consistency: Effects of specific anions
    • Kinsella, J. E.; Hale, M. L. Hydrophobic associations and gluten consistency: effects of specific anions. J. Agric. Food Chem. 1984, 32, 1054-1056.
    • (1984) J. Agric. Food Chem , vol.32 , pp. 1054-1056
    • Kinsella, J.E.1    Hale, M.L.2
  • 16
    • 0000130336 scopus 로고
    • Effects of neutral salts of the lyotropic series on the physical dough properties of a Canadian red spring wheatflour
    • Preston, K. R. Effects of neutral salts of the lyotropic series on the physical dough properties of a Canadian red spring wheatflour. Cereal Chem. 1989, 66, 144-148.
    • (1989) Cereal Chem , vol.66 , pp. 144-148
    • Preston, K.R.1
  • 17
    • 0000864069 scopus 로고
    • Effect of nonchaotropic salts on flour bread-making properties
    • He, H.; Roach, R. R.; Hoseney, R. C. Effect of nonchaotropic salts on flour bread-making properties. Cereal Chem. 1992, 69, 366-371.
    • (1992) Cereal Chem , vol.69 , pp. 366-371
    • He, H.1    Roach, R.R.2    Hoseney, R.C.3
  • 18
    • 0037314976 scopus 로고    scopus 로고
    • Light scattering and light absorbance separated by extended multiplicative signal correction. Application to near-infrared transmission analysis of powder mixtures
    • Martens, H.; Nielsen, J. P.; Engelsen, S. B. Light scattering and light absorbance separated by extended multiplicative signal correction. Application to near-infrared transmission analysis of powder mixtures. Anal. Chem. 2003, 75, 394-404.
    • (2003) Anal. Chem , vol.75 , pp. 394-404
    • Martens, H.1    Nielsen, J.P.2    Engelsen, S.B.3
  • 19
    • 0035850349 scopus 로고    scopus 로고
    • Salting-in and salting-out of hydrophobic solutes in aqueous solutions
    • Kalra, A.; Tugcu, N.; Cramer, S. M.; Garde, S. Salting-in and salting-out of hydrophobic solutes in aqueous solutions. J. Phys. Chem. B 2001, 105, 6380-6386.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6380-6386
    • Kalra, A.1    Tugcu, N.2    Cramer, S.M.3    Garde, S.4
  • 20
    • 15844375871 scopus 로고    scopus 로고
    • Ionic regulation of proteins
    • Di Stasio, E. Ionic regulation of proteins. Ital. J. Biochem. 2004, 53, 112-119.
    • (2004) Ital. J. Biochem , vol.53 , pp. 112-119
    • Di Stasio, E.1
  • 21
    • 0004848605 scopus 로고    scopus 로고
    • Salt-induced disaggregation/solubilization of gliadin and glutenin proteins in water
    • Fu, B. X.; Sapirstein, H. D.; Bushuk, W. Salt-induced disaggregation/solubilization of gliadin and glutenin proteins in water. J. Cereal Sci. 1996, 24, 241-246.
    • (1996) J. Cereal Sci , vol.24 , pp. 241-246
    • Fu, B.X.1    Sapirstein, H.D.2    Bushuk, W.3
  • 22
    • 0036840903 scopus 로고    scopus 로고
    • Effects of different salts on mixing and extension parameters on a diverse group of wheat cultivars using 2-g mixograph and extensigraph methods
    • Butow, B. J.; Gras, P. W.; Haraszi, R.; Bekes, F. Effects of different salts on mixing and extension parameters on a diverse group of wheat cultivars using 2-g mixograph and extensigraph methods. Cereal Chem. 2002, 79, 826-833.
    • (2002) Cereal Chem , vol.79 , pp. 826-833
    • Butow, B.J.1    Gras, P.W.2    Haraszi, R.3    Bekes, F.4
  • 23
    • 0021755248 scopus 로고
    • Mechanism of protein salting in and salting out by divalent-cation salts-balance between hydration and salt binding
    • Arakawa, T.; Timasheff, S. N. Mechanism of protein salting in and salting out by divalent-cation salts-balance between hydration and salt binding. Biochemistry 1984, 23, 5912-5923.
    • (1984) Biochemistry , vol.23 , pp. 5912-5923
    • Arakawa, T.1    Timasheff, S.N.2
  • 24
    • 14544308307 scopus 로고    scopus 로고
    • Observation of the first hydration layer of isolated cations and anions through the FTIR-ATR difference spectra
    • Wei, Z.; Zhang, Y.; Zhao, L.; Liu, J.; Li., X. Observation of the first hydration layer of isolated cations and anions through the FTIR-ATR difference spectra. J. Phys. Chem. A 2005, 109, 1337-1342.
    • (2005) J. Phys. Chem. A , vol.109 , pp. 1337-1342
    • Wei, Z.1    Zhang, Y.2    Zhao, L.3    Liu, J.4    Li, X.5
  • 25
    • 0033584169 scopus 로고    scopus 로고
    • Identification of β-turn and random coil amide III infrared bands for secondary structure estimation of proteins
    • Cai, S. W.; Singh, B. R. Identification of β-turn and random coil amide III infrared bands for secondary structure estimation of proteins. Biophys. Chem. 1999, 80, 7-20.
    • (1999) Biophys. Chem , vol.80 , pp. 7-20
    • Cai, S.W.1    Singh, B.R.2
  • 26
    • 3242742115 scopus 로고    scopus 로고
    • The optimization of protein secondary structure determination with infrared and circular dichroism spectra
    • Oberg, K. A.; Ruysschaert, J. M.; Goormaghtigh, E. The optimization of protein secondary structure determination with infrared and circular dichroism spectra. Eur. J. Biochem. 2004, 271, 2937-2948.
    • (2004) Eur. J. Biochem , vol.271 , pp. 2937-2948
    • Oberg, K.A.1    Ruysschaert, J.M.2    Goormaghtigh, E.3
  • 27
    • 0141568214 scopus 로고    scopus 로고
    • Effect of selected Hofmeister anions on the secondary structure and dynamics of wheat prolamine in gluten
    • Wellner, N.; Bianchini, D.; Mills, E. N. C.; Belton, P. S. Effect of selected Hofmeister anions on the secondary structure and dynamics of wheat prolamine in gluten. Cereal Chem. 2003, 80, 596-600.
    • (2003) Cereal Chem , vol.80 , pp. 596-600
    • Wellner, N.1    Bianchini, D.2    Mills, E.N.C.3    Belton, P.S.4
  • 29
    • 0842276079 scopus 로고    scopus 로고
    • Origin of near-infrared absorption bands
    • Siesler, H. W, Ozaki, Y, Kawata, S, Heise, H. M, Eds, Wiley-VCH: Weinheim, Germany
    • Bokobza, L. Origin of near-infrared absorption bands. In Near-infrared Spectroscopy: Principles, Instruments, Applications; Siesler, H. W., Ozaki, Y., Kawata, S., Heise, H. M., Eds.; Wiley-VCH: Weinheim, Germany, 2002; pp 11-41.
    • (2002) Near-infrared Spectroscopy: Principles, Instruments, Applications , pp. 11-41
    • Bokobza, L.1
  • 30
    • 0038345578 scopus 로고    scopus 로고
    • Applications in chemistry
    • Siesler, H. W, Ozaki, Y, Kawata, S, Heise, H. M, Eds, Wiley-VCH: Weinheim, Germany
    • Ozaki, Y. Applications in chemistry. In Near-infrared Spectroscopy: Principles, Instruments, Applications; Siesler, H. W., Ozaki, Y., Kawata, S., Heise, H. M., Eds.; Wiley-VCH: Weinheim, Germany, 2002; pp 179-211.
    • (2002) Near-infrared Spectroscopy: Principles, Instruments, Applications , pp. 179-211
    • Ozaki, Y.1
  • 31
    • 0035128576 scopus 로고    scopus 로고
    • The determination of wheat breadmaking performance and bread dough mixing time by NIR spectroscopy for high speed mixers
    • Alava, J. M.; Millar, S. J.; Salmon, S. E. The determination of wheat breadmaking performance and bread dough mixing time by NIR spectroscopy for high speed mixers. J. Cereal Sci. 2001, 33, 71-81.
    • (2001) J. Cereal Sci , vol.33 , pp. 71-81
    • Alava, J.M.1    Millar, S.J.2    Salmon, S.E.3
  • 32
    • 0002178417 scopus 로고    scopus 로고
    • Noninvasive monitoring of dough mixing by near infrared spectroscopy
    • Wesley, I. J.; Larsen, N.; Osborne, B. G.; Skerritt, J. H. Noninvasive monitoring of dough mixing by near infrared spectroscopy. J. Cereal Sci. 1998, 27, 61-69.
    • (1998) J. Cereal Sci , vol.27 , pp. 61-69
    • Wesley, I.J.1    Larsen, N.2    Osborne, B.G.3    Skerritt, J.H.4


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