메뉴 건너뛰기




Volumn 92, Issue 1, 2015, Pages 105-113

Structural modifications of gluten proteins in strong and weak wheat dough during mixing

Author keywords

[No Author keywords available]

Indexed keywords

FOURIER TRANSFORM INFRARED SPECTROSCOPY; HYDROPHOBICITY; MIXING; MOLECULAR WEIGHT DISTRIBUTION; SULFUR COMPOUNDS;

EID: 84921672514     PISSN: 00090352     EISSN: 19433638     Source Type: Journal    
DOI: 10.1094/CCHEM-10-13-0212-R     Document Type: Article
Times cited : (84)

References (36)
  • 1
    • 0003439867 scopus 로고
    • 11th Ed. Method 08-01.01. Ash - Basic method. Approved April 13, AACCI: St. Paul, MN
    • AACC International. Approved Methods of Analysis, 11th Ed. Method 08-01.01. Ash-Basic method. Approved April 13, 1961. Available online only. http://dx.doi.org/10.1094/AACCIntMethod-08-01.01. AACCI: St. Paul, MN.
    • (1961) Approved Methods of Analysis
    • AACC International1
  • 2
    • 0001920021 scopus 로고    scopus 로고
    • On the elasticity of wheat gluten
    • Belton, P.S. 1999. On the elasticity of wheat gluten. J. Cereal Sci. 29:103-107.
    • (1999) J. Cereal Sci. , vol.29 , pp. 103-107
    • Belton, P.S.1
  • 3
    • 84866880971 scopus 로고    scopus 로고
    • Unfolding gluten: An overview of research on gluten
    • Bock, J., and Seetharaman, K. 2012. Unfolding gluten: An overview of research on gluten. Cereal Foods World 57:209-214.
    • (2012) Cereal Foods World , vol.57 , pp. 209-214
    • Bock, J.1    Seetharaman, K.2
  • 4
    • 84881419793 scopus 로고    scopus 로고
    • Impact of bran addition on water properties and gluten secondary structure in wheat flour doughs studied by attenuated total reflectance Fourier transform infrared spectroscopy
    • Bock, J. E., Connelly, R. K., and Damodaran, S. 2013. Impact of bran addition on water properties and gluten secondary structure in wheat flour doughs studied by attenuated total reflectance Fourier transform infrared spectroscopy. Cereal Chem. 90:377-386.
    • (2013) Cereal Chem. , vol.90 , pp. 377-386
    • Bock, J.E.1    Connelly, R.K.2    Damodaran, S.3
  • 5
    • 84872413885 scopus 로고    scopus 로고
    • Bran-induced changes in water structure and gluten conformation in model gluten dough studied by Fourier transform infrared spectroscopy
    • Bock, J. E., and Damodaran, S. 2013. Bran-induced changes in water structure and gluten conformation in model gluten dough studied by Fourier transform infrared spectroscopy. Food Hydrocolloids 31:146-155.
    • (2013) Food Hydrocolloids , vol.31 , pp. 146-155
    • Bock, J.E.1    Damodaran, S.2
  • 7
    • 84881436729 scopus 로고    scopus 로고
    • The performing protein: Beyond wheat proteomics?
    • Bonomi, F., Iametti, S., Mamone, G., and Ferranti, P. 2013. The performing protein: Beyond wheat proteomics? Cereal Chem. 90:358-366.
    • (2013) Cereal Chem. , vol.90 , pp. 358-366
    • Bonomi, F.1    Iametti, S.2    Mamone, G.3    Ferranti, P.4
  • 8
    • 2342527129 scopus 로고    scopus 로고
    • Probing structural features of water-insoluble proteins by front-face fluorescence
    • Bonomi, F., Mora, G., Pagani, M. A., and Iametti, S. 2004. Probing structural features of water-insoluble proteins by front-face fluorescence. Anal. Biochem. 329:104-111.
    • (2004) Anal. Biochem. , vol.329 , pp. 104-111
    • Bonomi, F.1    Mora, G.2    Pagani, M.A.3    Iametti, S.4
  • 9
    • 0030772434 scopus 로고    scopus 로고
    • Effect of mechanical dough development on the extractability of wheat storage proteins from bread dough
    • Bushuk, W., Hay, R. L., Larsen, N. G., Sara, R. G., Simmons, L. D., and Sutton, K. H. 1997. Effect of mechanical dough development on the extractability of wheat storage proteins from bread dough. Cereal Chem. 74:389-395.
    • (1997) Cereal Chem. , vol.74 , pp. 389-395
    • Bushuk, W.1    Hay, R.L.2    Larsen, N.G.3    Sara, R.G.4    Simmons, L.D.5    Sutton, K.H.6
  • 10
    • 39549094669 scopus 로고    scopus 로고
    • Relevance of the flavin binding to the stability and folding of engineered cholesterol oxidase containing noncovalently bound FAD
    • Caldinelli, L., Iametti, S., Barbiroli, A., Fessas, D., Bonomi, F., Piubelli, L., Molla, G., and Pollegioni, L. 2008. Relevance of the flavin binding to the stability and folding of engineered cholesterol oxidase containing noncovalently bound FAD. Protein Sci. 17:409-419.
    • (2008) Protein Sci. , vol.17 , pp. 409-419
    • Caldinelli, L.1    Iametti, S.2    Barbiroli, A.3    Fessas, D.4    Bonomi, F.5    Piubelli, L.6    Molla, G.7    Pollegioni, L.8
  • 12
    • 0037217070 scopus 로고    scopus 로고
    • Glutenin macropolymer: A gel formed by glutenin particles
    • Don, C., Lichtendonk, W., Plijter, J. J., and Hamer, R. J. 2003. Glutenin macropolymer: A gel formed by glutenin particles. J. Cereal Sci. 37:1-7.
    • (2003) J. Cereal Sci. , vol.37 , pp. 1-7
    • Don, C.1    Lichtendonk, W.2    Plijter, J.J.3    Hamer, R.J.4
  • 13
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong, A., Huang, P., and Caughey, W. S. 1990. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29:3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 14
    • 0009535344 scopus 로고
    • Solubilization of glutenin in urea/SDS solutions at elevated temperature
    • Gao, L., and Bushuk, W. 1992. Solubilization of glutenin in urea/SDS solutions at elevated temperature. J. Cereal Sci. 16:81-89.
    • (1992) J. Cereal Sci. , vol.16 , pp. 81-89
    • Gao, L.1    Bushuk, W.2
  • 15
    • 40549087246 scopus 로고    scopus 로고
    • Effect of variety and environmental factors on gluten proteins: An analytical, spectroscopic, and rheological study
    • Georget, D. M. R., Underwood-Toscano, C., Powers, S. J., Shewry, P. R., and Belton, P. S. 2008. Effect of variety and environmental factors on gluten proteins: An analytical, spectroscopic, and rheological study. J. Agric. Food Chem. 56:1172-1179.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 1172-1179
    • Georget, D.M.R.1    Underwood-Toscano, C.2    Powers, S.J.3    Shewry, P.R.4    Belton, P.S.5
  • 16
    • 0035164832 scopus 로고    scopus 로고
    • Biochemical, genetic, and molecular characterization of wheat glutenin and its component subunits
    • Gianibelli, M. C., Larroque, O. R., MacRitchie, F., and Wrigley, C. W. 2001. Biochemical, genetic, and molecular characterization of wheat glutenin and its component subunits. Cereal Chem. 78:635-646.
    • (2001) Cereal Chem. , vol.78 , pp. 635-646
    • Gianibelli, M.C.1    Larroque, O.R.2    MacRitchie, F.3    Wrigley, C.W.4
  • 19
    • 0012171761 scopus 로고    scopus 로고
    • Understanding the structure and properties of gluten: An overview
    • P. R. Shewry and A. S. Tatham, eds. The Royal Society of Chemistry: Cambridge, U.K
    • Hamer, R. J., and van Vliet, T. 2000. Understanding the structure and properties of gluten: An overview. Pages 125-131 in: Wheat Gluten. P. R. Shewry and A. S. Tatham, eds. The Royal Society of Chemistry: Cambridge, U.K.
    • (2000) Wheat Gluten. , pp. 125-131
    • Hamer, R.J.1    Van Vliet, T.2
  • 20
    • 84858334112 scopus 로고    scopus 로고
    • Comparison of lipid effects on structural features of hard and soft wheat flour proteins assessed by front-face fluorescence
    • Huschka, B., Bonomi, F., Marengo, M., Miriani, M., and Seetharaman, K. 2012. Comparison of lipid effects on structural features of hard and soft wheat flour proteins assessed by front-face fluorescence. Food Chem. 133:1011-1016.
    • (2012) Food Chem. , vol.133 , pp. 1011-1016
    • Huschka, B.1    Bonomi, F.2    Marengo, M.3    Miriani, M.4    Seetharaman, K.5
  • 22
    • 84921662572 scopus 로고
    • Comparison of the effects of N-ethylmaleimide and urea on rheological properties of dough
    • Jankiewicz, M., and Pomeranz, Y. 1965. Comparison of the effects of N-ethylmaleimide and urea on rheological properties of dough. Cereal Chem. 42:37-43.
    • (1965) Cereal Chem. , vol.42 , pp. 37-43
    • Jankiewicz, M.1    Pomeranz, Y.2
  • 23
    • 0034342637 scopus 로고    scopus 로고
    • Effect of composition of glutenin subfractions on rheological properties of wheat
    • Jood, S., Schofield, J. D., Tsiami, A. A., and Bollecker, S. 2000. Effect of composition of glutenin subfractions on rheological properties of wheat. J. Agric. Food Chem. 24:275-298.
    • (2000) J. Agric. Food Chem. , vol.24 , pp. 275-298
    • Jood, S.1    Schofield, J.D.2    Tsiami, A.A.3    Bollecker, S.4
  • 24
    • 26244452711 scopus 로고    scopus 로고
    • The impact of heating and cooling on the physico-chemical properties of wheat gluten-water suspensions
    • Lagrain, B., Brijs, K., Veraverbeke, W. S., and Delcour, J. A. 2005. The impact of heating and cooling on the physico-chemical properties of wheat gluten-water suspensions. J. Cereal Sci. 42:327-333.
    • (2005) J. Cereal Sci. , vol.42 , pp. 327-333
    • Lagrain, B.1    Brijs, K.2    Veraverbeke, W.S.3    Delcour, J.A.4
  • 25
    • 34447303330 scopus 로고    scopus 로고
    • Impact of redox agents on the extractability of gluten proteins during bread making
    • Lagrain, B., Thewissen, B. G., Brijs, K., and Delcour, J. A. 2007. Impact of redox agents on the extractability of gluten proteins during bread making. J. Agric. Food Chem. 55:5320-5325.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 5320-5325
    • Lagrain, B.1    Thewissen, B.G.2    Brijs, K.3    Delcour, J.A.4
  • 26
    • 34047245978 scopus 로고    scopus 로고
    • Similarities and differences in secondary structure of viscoelastic polymers of maize αzein and wheat gluten proteins
    • Mejia, C. D., Mauer, L. J., and Hamaker, B. R. 2007. Similarities and differences in secondary structure of viscoelastic polymers of maize αzein and wheat gluten proteins. J. Cereal Sci. 45:353-359.
    • (2007) J. Cereal Sci. , vol.45 , pp. 353-359
    • Mejia, C.D.1    Mauer, L.J.2    Hamaker, B.R.3
  • 27
    • 84868199163 scopus 로고    scopus 로고
    • Using the gluten peak tester as a tool to measure physical properties of gluten
    • Melnyk, J. P., Dreisoerner, J., Marcone, M. F., and Seetharaman, K. 2012. Using the gluten peak tester as a tool to measure physical properties of gluten. J. Cereal Sci. 56:561-567.
    • (2012) J. Cereal Sci. , vol.56 , pp. 561-567
    • Melnyk, J.P.1    Dreisoerner, J.2    Marcone, M.F.3    Seetharaman, K.4
  • 28
    • 33645837443 scopus 로고    scopus 로고
    • Changes in secondary protein structures during mixing development of high absorption (90%) flour and water mixtures
    • Robertson, G. H., Gregorski, K. S., and Cao, T. K. 2006. Changes in secondary protein structures during mixing development of high absorption (90%) flour and water mixtures. Cereal Chem. 83:136-142.
    • (2006) Cereal Chem. , vol.83 , pp. 136-142
    • Robertson, G.H.1    Gregorski, K.S.2    Cao, T.K.3
  • 29
    • 0031823869 scopus 로고    scopus 로고
    • Intercultivar variation in the quantity of monomeric proteins, soluble and insoluble glutenin, and residue protein in wheat flour and relationships to breadmaking quality
    • Sapirstein, H. D., and Fu, B. X. 1998. Intercultivar variation in the quantity of monomeric proteins, soluble and insoluble glutenin, and residue protein in wheat flour and relationships to breadmaking quality. Cereal Chem. 75:500-507.
    • (1998) Cereal Chem. , vol.75 , pp. 500-507
    • Sapirstein, H.D.1    Fu, B.X.2
  • 30
    • 51649104955 scopus 로고    scopus 로고
    • Evidence for varying interaction of gliadin and glutenin proteins as an explanation for differences in dough strength of different wheats
    • P. R. Shewry and A. S. Tatham, eds. The Royal Society of Chemistry: Cambridge, U.K
    • Sapirstein, H. D., and Fu, B. X. 2000. Evidence for varying interaction of gliadin and glutenin proteins as an explanation for differences in dough strength of different wheats. Pages 425-429 in: Wheat Gluten. P. R. Shewry and A. S. Tatham, eds. The Royal Society of Chemistry: Cambridge, U.K.
    • (2000) Wheat Gluten. , pp. 425-429
    • Sapirstein, H.D.1    Fu, B.X.2
  • 31
    • 0345643329 scopus 로고    scopus 로고
    • Depolymerization of the glutenin macropolymer during dough mixing: I. Changes in levels, molecular weight distribution, and overall composition
    • Skerritt, J. H., Hac, L., and Bekes, F. 1999a. Depolymerization of the glutenin macropolymer during dough mixing: I. Changes in levels, molecular weight distribution, and overall composition. Cereal Chem. 76:395-401.
    • (1999) Cereal Chem. , vol.76 , pp. 395-401
    • Skerritt, J.H.1    Hac, L.2    Bekes, F.3
  • 32
    • 0033025440 scopus 로고    scopus 로고
    • Depolymerization of the glutenin macropolymer during mixing: II. Differences in retention of specific glutenin subunits
    • Skerritt, J. H., Hac, L., Lindsay, M. P., and Bekes, F. 1999b. Depolymerization of the glutenin macropolymer during mixing: II. Differences in retention of specific glutenin subunits. Cereal Chem. 76:402-409.
    • (1999) Cereal Chem. , vol.76 , pp. 402-409
    • Skerritt, J.H.1    Hac, L.2    Lindsay, M.P.3    Bekes, F.4
  • 33
    • 0000243469 scopus 로고
    • The beta-turn conformation in wheat gluten proteins: Relationship to gluten elasticity
    • Tatham, A. S., Miflin, B. J., and Shewry, P. R. 1985. The beta-turn conformation in wheat gluten proteins: Relationship to gluten elasticity. Cereal Chem. 62:405-412.
    • (1985) Cereal Chem. , vol.62 , pp. 405-412
    • Tatham, A.S.1    Miflin, B.J.2    Shewry, P.R.3
  • 34
    • 0007242798 scopus 로고
    • Determination of sulfhydryl and disulfide groups in flour and their relation to wheat quality
    • Tsen, C. C., and Anderson, J. A. 1963. Determination of sulfhydryl and disulfide groups in flour and their relation to wheat quality. Cereal Chem. 40:314-323.
    • (1963) Cereal Chem. , vol.40 , pp. 314-323
    • Tsen, C.C.1    Anderson, J.A.2
  • 35
    • 0000904738 scopus 로고    scopus 로고
    • Depolymerisation and repolymerisation of wheat glutenin during dough processing. II. Changes in composition
    • Weegles, P. L., Hamer, R. J., and Schofield, J. D. 1997. Depolymerisation and repolymerisation of wheat glutenin during dough processing. II. Changes in composition. J. Cereal Sci. 25:155-163.
    • (1997) J. Cereal Sci. , vol.25 , pp. 155-163
    • Weegles, P.L.1    Hamer, R.J.2    Schofield, J.D.3
  • 36
    • 34447295031 scopus 로고    scopus 로고
    • Gluten: A balance of gliadin and glutenin
    • C. Wrigley, F. Békés, and W. Bushuk, eds. AACC International: St. Paul, MN
    • Wrigley, C. W., Békés, F., and Bushuk, W. 2006. Gluten: A balance of gliadin and glutenin. Pages 3-32 in: Gliadin and Glutenin: The Unique Balance of Wheat Quality. C. Wrigley, F. Békés, and W. Bushuk, eds. AACC International: St. Paul, MN.
    • (2006) Gliadin and Glutenin: The Unique Balance of Wheat Quality. , pp. 3-32
    • Wrigley, C.W.1    Békés, F.2    Bushuk, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.