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Volumn 56, Issue 11, 2008, Pages 4236-4243

Determination of secondary structural changes in gluten proteins during mixing using fourier transform horizontal attenuated total reflectance spectroscopy

Author keywords

Amide III; Attenuated total reflectance; Rheology; Secondary structure

Indexed keywords

GLUTEN; WATER;

EID: 47049116839     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf703569b     Document Type: Article
Times cited : (37)

References (44)
  • 1
    • 0000651512 scopus 로고
    • Hydration as a factor in bread flour quality
    • Larsen, R. A. Hydration as a factor in bread flour quality. Cereal Chem. 1964, 41, 181-187.
    • (1964) Cereal Chem , vol.41 , pp. 181-187
    • Larsen, R.A.1
  • 2
    • 0001449696 scopus 로고
    • Effects of mixer speed, dough temperature, and water absorption on flour-water mixograms
    • Baig, M. M.; Hoseney, R. C. Effects of mixer speed, dough temperature, and water absorption on flour-water mixograms. Cereal Chem. 1977, 54, 605-615.
    • (1977) Cereal Chem , vol.54 , pp. 605-615
    • Baig, M.M.1    Hoseney, R.C.2
  • 3
    • 0002707249 scopus 로고
    • Factors affecting mechanical dough development. I. Effect of mixing intensity and work input
    • Kilborn, R. H.; Tipples, K. H. Factors affecting mechanical dough development. I. Effect of mixing intensity and work input. Cereal Chem. 1977, 49, 34-47.
    • (1977) Cereal Chem , vol.49 , pp. 34-47
    • Kilborn, R.H.1    Tipples, K.H.2
  • 4
    • 0042935687 scopus 로고
    • Development and "undevelopment" of wheat dough by mixing: Physicochemical studies
    • Paredes-Lopez, O.; Bushuk, W. Development and "undevelopment" of wheat dough by mixing: physicochemical studies. Cereal Chem. 1983, 60, 19-23.
    • (1983) Cereal Chem , vol.60 , pp. 19-23
    • Paredes-Lopez, O.1    Bushuk, W.2
  • 5
    • 0030851830 scopus 로고    scopus 로고
    • Rheological behavior of undeveloped and developed wheat dough
    • Campos, D. T.; Steffe, J. F.; Ng, P. K. W. Rheological behavior of undeveloped and developed wheat dough. Cereal Chem. 1997, 74 (4), 489-494.
    • (1997) Cereal Chem , vol.74 , Issue.4 , pp. 489-494
    • Campos, D.T.1    Steffe, J.F.2    Ng, P.K.W.3
  • 6
    • 0034958276 scopus 로고    scopus 로고
    • Relationship between rheological properties and microstructural characteristics of nondeveloped, partially developed, and developed doughs
    • Lee, L.; Ng, P. K. W.; Whallon, J. H.; Steffe, J. F. Relationship between rheological properties and microstructural characteristics of nondeveloped, partially developed, and developed doughs. Cereal Chem. 2001, 78 (4), 447-452.
    • (2001) Cereal Chem , vol.78 , Issue.4 , pp. 447-452
    • Lee, L.1    Ng, P.K.W.2    Whallon, J.H.3    Steffe, J.F.4
  • 7
    • 0012342479 scopus 로고    scopus 로고
    • Disulphide bonds in wheat gluten proteins
    • Shewry, P. R.; Tatham, A. S. Disulphide bonds in wheat gluten proteins. J. Cereal Sci. 1997, 25, 207-227.
    • (1997) J. Cereal Sci , vol.25 , pp. 207-227
    • Shewry, P.R.1    Tatham, A.S.2
  • 8
    • 0042428393 scopus 로고
    • Modification of flour proteins by dough mixing: Effects of sulfhydryl-blocking and oxidizing agents
    • Mecham, D. K.; Cole, E. G.; Sokol, H. A. Modification of flour proteins by dough mixing: Effects of sulfhydryl-blocking and oxidizing agents. Cereal Chem. 1963, 40, 1-9.
    • (1963) Cereal Chem , vol.40 , pp. 1-9
    • Mecham, D.K.1    Cole, E.G.2    Sokol, H.A.3
  • 9
    • 0000705073 scopus 로고
    • Effect of oxidizing and reducing agents on changes of flour proteins during dough mixing
    • Tsen, C. C. Effect of oxidizing and reducing agents on changes of flour proteins during dough mixing. Cereal Chem. 1969, 46, 435-442.
    • (1969) Cereal Chem , vol.46 , pp. 435-442
    • Tsen, C.C.1
  • 10
    • 0000190583 scopus 로고
    • Thiol and disulfide groups in dough rheology
    • Bloksma, A. H. Thiol and disulfide groups in dough rheology. Cereal Chem. 1975, 52, 170r-183r.
    • (1975) Cereal Chem , vol.52
    • Bloksma, A.H.1
  • 12
    • 0001042101 scopus 로고    scopus 로고
    • Amino acids, peptides, and proteins
    • Fennema, O, Ed, Marcel Dekker, Inc, New York, NY
    • Damodaran, S. Amino acids, peptides, and proteins. In Food Chemistry; Fennema, O., Ed.; Marcel Dekker, Inc.: New York, NY, 1996; pp 321-429.
    • (1996) Food Chemistry , pp. 321-429
    • Damodaran, S.1
  • 13
    • 0035138346 scopus 로고    scopus 로고
    • Changes in SDS solubility of glutenin polymers during dough mixing and resting (1)
    • Aussenac, T.; Carceller, J.; Kleiber, D. Changes in SDS solubility of glutenin polymers during dough mixing and resting (1). Cereal Chem. 2001, 78 (1), 39-45.
    • (2001) Cereal Chem , vol.78 , Issue.1 , pp. 39-45
    • Aussenac, T.1    Carceller, J.2    Kleiber, D.3
  • 14
    • 0001785082 scopus 로고
    • Infrared spectra of biological macromolecules and related systems
    • Timasheff, S, Fasman, G, Eds, Marcel Dekker, Inc, New York, NY
    • Susi, H. Infrared spectra of biological macromolecules and related systems. In Structure and Stability of Biological Macromolecules; Timasheff, S., Fasman, G., Eds.; Marcel Dekker, Inc.: New York, NY, 1969; pp 575-663.
    • (1969) Structure and Stability of Biological Macromolecules , pp. 575-663
    • Susi, H.1
  • 16
    • 84903963347 scopus 로고
    • Fourier transform infrared 15analysis of amide III bands of proteins for the secondary structure estimation
    • Jan 17-18, Los Angeles, CA, pp
    • Singh, B. R.; DeOliveira, D. B.; Fu, F. N.; Fuller, M. P. Fourier transform infrared 15analysis of amide III bands of proteins for the secondary structure estimation. Proceedings of Biomolecular Spectroscopy III, Jan 17-18, 1993, Los Angeles, CA, pp 47-55.
    • (1993) Proceedings of Biomolecular Spectroscopy , vol.3 , pp. 47-55
    • Singh, B.R.1    DeOliveira, D.B.2    Fu, F.N.3    Fuller, M.P.4
  • 17
    • 1542357647 scopus 로고    scopus 로고
    • A distinct utility of the amide III infrared band for secondary structure estimation of aqueous protein solutions using partial least squares
    • Shuowei, C.; Singh, B. R. A distinct utility of the amide III infrared band for secondary structure estimation of aqueous protein solutions using partial least squares. Biochemistry 2004, 43, 2541-2549.
    • (2004) Biochemistry , vol.43 , pp. 2541-2549
    • Shuowei, C.1    Singh, B.R.2
  • 18
    • 0033584169 scopus 로고    scopus 로고
    • Identification of beta-turn and random coil amide III infrared bands for secondary structure estimation of proteins
    • Cai, S.; Singh, B. R. Identification of beta-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.1    Singh, B.R.2
  • 19
    • 47049093189 scopus 로고    scopus 로고
    • Mathewson, P. R. Fourier transform infrared spectroscopic analysis of protein secondary structure. Development of Enzymological and Fourier transform Infrared Spectroscopic Methods for Analysis of Proteolytic Activity; Ph.D. Thesis, Kansas State University, Manhattan, KS, 1985; pp 96-224.
    • Mathewson, P. R. Fourier transform infrared spectroscopic analysis of protein secondary structure. Development of Enzymological and Fourier transform Infrared Spectroscopic Methods for Analysis of Proteolytic Activity; Ph.D. Thesis, Kansas State University, Manhattan, KS, 1985; pp 96-224.
  • 20
    • 0024997389 scopus 로고
    • Determination of the secondary structure of proteins in aqueous solutions from amide I and amide II infrared bands. Comparison between classical and partial least-square methods
    • Dousseau, F.; Pézolet, M. Determination of the secondary structure of proteins in aqueous solutions from amide I and amide II infrared bands. Comparison between classical and partial least-square methods. Biochemistry 1990, 29, 8771-8779.
    • (1990) Biochemistry , vol.29 , pp. 8771-8779
    • Dousseau, F.1    Pézolet, M.2
  • 21
    • 0023288712 scopus 로고
    • A study of the amide III band by FT-IR spectrometry of the secondary structure of albumin, myoglobin, and gamma-globulin
    • Kaiden, K.; Matsui, T.; Tanaka, S. A study of the amide III band by FT-IR spectrometry of the secondary structure of albumin, myoglobin, and gamma-globulin. Appl. Spectrosc. 1987, 41, 180-184.
    • (1987) Appl. Spectrosc , vol.41 , pp. 180-184
    • Kaiden, K.1    Matsui, T.2    Tanaka, S.3
  • 22
    • 0025838069 scopus 로고
    • Protein secondary structure of the isolated photosystem II reaction center and conformational changes studied by Fourier transform infrared spectroscopy
    • He, W. Z.; Newell, W. R.; Haris, P. I.; Chapman, D.; Barber, J. Protein secondary structure of the isolated photosystem II reaction center and conformational changes studied by Fourier transform infrared spectroscopy. Biochemistry 1991, 30, 4552-4559.
    • (1991) Biochemistry , vol.30 , pp. 4552-4559
    • He, W.Z.1    Newell, W.R.2    Haris, P.I.3    Chapman, D.4    Barber, J.5
  • 23
    • 0027482684 scopus 로고
    • Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra
    • Pribic, R.; van Stokkum, I. H. M.; Chapman, D.; Haris, P. I.; Bloemdal, M. Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra. Anal. Biochem. 1993, 214, 366-378.
    • (1993) Anal. Biochem , vol.214 , pp. 366-378
    • Pribic, R.1    van Stokkum, I.H.M.2    Chapman, D.3    Haris, P.I.4    Bloemdal, M.5
  • 24
    • 0025298487 scopus 로고
    • Molecular structure of tetanus neurotoxin as revealed by Fourier transform infrared and circular dichroic spectroscopy
    • Singh, B. R.; Fuller, M. P.; Schiavo, G. Molecular structure of tetanus neurotoxin as revealed by Fourier transform infrared and circular dichroic spectroscopy. Biophys. Chem. 1990, 36, 155-166.
    • (1990) Biophys. Chem , vol.36 , pp. 155-166
    • Singh, B.R.1    Fuller, M.P.2    Schiavo, G.3
  • 25
    • 0028539766 scopus 로고
    • Secondary structure estimation of proteins using the amide III region of Fourier transform infrared spectroscopy: Application to analyze calcium-binding-induced structural changes in calse-questrin
    • Fu, F. D.; DeOliveira, D. B.; Trumble, W. R.; Sarkar, H. K.; Singh, B. R. Secondary structure estimation of proteins using the amide III region of Fourier transform infrared spectroscopy: Application to analyze calcium-binding-induced structural changes in calse-questrin. Appl. Spectrosc. 1994, 48, 1432-1441.
    • (1994) Appl. Spectrosc , vol.48 , pp. 1432-1441
    • Fu, F.D.1    DeOliveira, D.B.2    Trumble, W.R.3    Sarkar, H.K.4    Singh, B.R.5
  • 26
    • 0033003073 scopus 로고    scopus 로고
    • FTIR characterization of the secondary structure of proteins encapsulated within PLGA microspheres
    • Fu, K.; Griebenow, K.; Hsieh, L.; Klibanov, A. M.; Langer, R. FTIR characterization of the secondary structure of proteins encapsulated within PLGA microspheres. J. Controlled Release 1999, 58, 357-366.
    • (1999) J. Controlled Release , vol.58 , pp. 357-366
    • Fu, K.1    Griebenow, K.2    Hsieh, L.3    Klibanov, A.M.4    Langer, R.5
  • 28
    • 0031417508 scopus 로고    scopus 로고
    • Fourier-transform infrared spectroscopic analysis of the secondary structure of recombinant humanized immunoglobulin G
    • Costantino, H. R.; Andya, J. D.; Shire, S. J.; and Hsu, C. C. Fourier-transform infrared spectroscopic analysis of the secondary structure of recombinant humanized immunoglobulin G. J. Pharm. Sci. 1997, 3, 121-128.
    • (1997) J. Pharm. Sci , vol.3 , pp. 121-128
    • Costantino, H.R.1    Andya, J.D.2    Shire, S.J.3    Hsu, C.C.4
  • 29
    • 0026576158 scopus 로고
    • Conformation of wheat gluten proteins. Comparison between functional and solution states as determined by infrared spectroscopy
    • Pezolet, M.; Bononfant, S.; Dousseau, F.; Popineau, Y. Conformation of wheat gluten proteins. Comparison between functional and solution states as determined by infrared spectroscopy. Fed. Eur. Biochem. Soc. Lett. 1992, 299, 247-250.
    • (1992) Fed. Eur. Biochem. Soc. Lett , vol.299 , pp. 247-250
    • Pezolet, M.1    Bononfant, S.2    Dousseau, F.3    Popineau, Y.4
  • 30
    • 47049087800 scopus 로고    scopus 로고
    • Seabourn, B. W. Determination of protein secondary structure in wheat flour-water systems during mixing using Fourier transform horizontal attenuated total reflectance infrared spectroscopy. Ph.D. Thesis, Kansas State University, 2002; pp 1-151.
    • Seabourn, B. W. Determination of protein secondary structure in wheat flour-water systems during mixing using Fourier transform horizontal attenuated total reflectance infrared spectroscopy. Ph.D. Thesis, Kansas State University, 2002; pp 1-151.
  • 32
    • 34848857912 scopus 로고    scopus 로고
    • Analysis of protein structures and interactions in complex food by near-infrared spectroscopy. 1. Gluten powder
    • Bruun, S. W.; Sondergaard, I.; Jacobsen, S. Analysis of protein structures and interactions in complex food by near-infrared spectroscopy. 1. Gluten powder. J. Agric. Food Chem. 2007, 55, 7234-7243.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 7234-7243
    • Bruun, S.W.1    Sondergaard, I.2    Jacobsen, S.3
  • 33
    • 34848814730 scopus 로고    scopus 로고
    • Analysis of protein structures and interactions in complex food by near-infrared spectroscopy. 2. Hydrated gluten
    • Bruun, S. W.; Sondergaard, I.; Jacobsen, S. Analysis of protein structures and interactions in complex food by near-infrared spectroscopy. 2. Hydrated gluten. J. Agric. Food Chem. 2007, 55, 7244-7251.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 7244-7251
    • Bruun, S.W.1    Sondergaard, I.2    Jacobsen, S.3
  • 34
    • 0004136913 scopus 로고    scopus 로고
    • American Association of Cereal Chemists, 10th ed, The Association: St. Paul, MN
    • American Association of Cereal Chemists. Approved Methods of the AACC, 10th ed.; The Association: St. Paul, MN, 2000.
    • (2000) Approved Methods of the AACC
  • 35
    • 77954625547 scopus 로고    scopus 로고
    • Thermo Electron Corporation Application Note; Thermo Electron Corporation: Madison, WI
    • Nunn, S.; Nishikida, K. Advanced ATR Correction Algorithm; Thermo Electron Corporation Application Note; Thermo Electron Corporation: Madison, WI, 2003.
    • (2003) Advanced ATR Correction Algorithm
    • Nunn, S.1    Nishikida, K.2
  • 36
    • 0021115861 scopus 로고
    • Protein structure by Fourier transform infrared spectroscopy: Second derivative spectra
    • Susi, H.; Byler, D. M. Protein structure by Fourier transform infrared spectroscopy: second derivative spectra. Biochem. Biophys. Res. Commun. 1983, 115, 391-397.
    • (1983) Biochem. Biophys. Res. Commun , vol.115 , pp. 391-397
    • Susi, H.1    Byler, D.M.2
  • 37
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least squares procedures
    • Savitsky, A.; Golay, M. J. E. Smoothing and differentiation of data by simplified least squares procedures. Anal. Chem. 1964, 36, 1627-1639.
    • (1964) Anal. Chem , vol.36 , pp. 1627-1639
    • Savitsky, A.1    Golay, M.J.E.2
  • 38
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S.; Bandekar, J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 1986, 38, 181-364.
    • (1986) Adv. Protein Chem , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 39
    • 0034660017 scopus 로고    scopus 로고
    • Related expression and characterisation of a highly repetitive peptide derived from a wheat seed storage protein
    • Gilbert, S. M.; Wellner, N.; Belton, P. S.; Greenfield, J. A.; Siligardi, G.; Shewry, P. R.; Tatham, A. S. Related expression and characterisation of a highly repetitive peptide derived from a wheat seed storage protein. Biochim. Biophys. Acta 2000, 1479 (1-2), 135-146.
    • (2000) Biochim. Biophys. Acta , vol.1479 , Issue.1-2 , pp. 135-146
    • Gilbert, S.M.1    Wellner, N.2    Belton, P.S.3    Greenfield, J.A.4    Siligardi, G.5    Shewry, P.R.6    Tatham, A.S.7
  • 40
    • 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.; Belton, P. S. Molecular structures and interactions of repetitive peptides based on wheat glutenin subunits depend on chain length. Biopolymers 2003, 72, 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
  • 41
    • 0002239160 scopus 로고
    • A study by infrared spectroscopy of the conformations of gluten proteins differing in their gliadin and glutenin compositions
    • Popineau, Y.; Bonenfant, S.; Cornec, M.; Pezolet, M. A study by infrared spectroscopy of the conformations of gluten proteins differing in their gliadin and glutenin compositions. J. Cereal Sci. 1994, 20, 15-22.
    • (1994) J. Cereal Sci , vol.20 , pp. 15-22
    • Popineau, Y.1    Bonenfant, S.2    Cornec, M.3    Pezolet, M.4
  • 42
    • 0022032067 scopus 로고
    • A conformational study of a glutamine- and proline-rich cereal seed protein, C hordein
    • Tatham, A. S.; Drakek, A. F.; Shewry, P. R. A conformational study of a glutamine- and proline-rich cereal seed protein, C hordein. Biochem. J. 1985, 1226 (2), 557-562.
    • (1985) Biochem. J , vol.1226 , Issue.2 , pp. 557-562
    • Tatham, A.S.1    Drakek, A.F.2    Shewry, P.R.3


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