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Volumn 72, Issue , 2017, Pages 105-114

Improving solubility and emulsifying property of wheat gluten by deamidation with four different acids: Effect of replacement of folded conformation by extended structure

Author keywords

Deamidation; Emulsifying property; Protein conformation; Solubility; Wheat gluten

Indexed keywords

AMINO ACIDS; ATOMIC FORCE MICROSCOPY; CHEMICAL REACTIONS; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; EMULSIFICATION; FOURIER TRANSFORM INFRARED SPECTROSCOPY; PROTEINS; SOLUBILITY;

EID: 85019984146     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2017.04.013     Document Type: Article
Times cited : (68)

References (32)
  • 1
    • 0034001548 scopus 로고    scopus 로고
    • Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes
    • Alizadeh-Pasdar, N., Li-Chan, E.C., Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. Journal of Agricultural and Food Chemistry 48:2 (2000), 328–334.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , Issue.2 , pp. 328-334
    • Alizadeh-Pasdar, N.1    Li-Chan, E.C.2
  • 2
    • 11244340520 scopus 로고    scopus 로고
    • Thermally induced fibrillar aggregation of hen egg white lysozyme
    • Arnaudov, L.N., de Vries, R., Thermally induced fibrillar aggregation of hen egg white lysozyme. Biophysical Journal 88:1 (2005), 515–526.
    • (2005) Biophysical Journal , vol.88 , Issue.1 , pp. 515-526
    • Arnaudov, L.N.1    de Vries, R.2
  • 4
    • 0001163635 scopus 로고
    • Amide groups as interaction sites in wheat gluten proteins: Effects of amide-ester conversion
    • Beckwith, A.C., Wall, J., Dimler, R.J., Amide groups as interaction sites in wheat gluten proteins: Effects of amide-ester conversion. Archives of Biochemistry and Biophysics 103:3 (1963), 319–330.
    • (1963) Archives of Biochemistry and Biophysics , vol.103 , Issue.3 , pp. 319-330
    • Beckwith, A.C.1    Wall, J.2    Dimler, R.J.3
  • 6
    • 85022241054 scopus 로고
    • Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins
    • Church, F.C., Swaisgood, H.E., Porter, D.H., Catignani, G.L., Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. Journal of Dairy Science 66:6 (1983), 1219–1227.
    • (1983) Journal of Dairy Science , vol.66 , Issue.6 , pp. 1219-1227
    • Church, F.C.1    Swaisgood, H.E.2    Porter, D.H.3    Catignani, G.L.4
  • 8
    • 70149092311 scopus 로고    scopus 로고
    • Interfacial properties of deamidated wheat protein in relation to its ability to stabilise oil-in-water emulsions
    • Day, L., Xu, M., Lundin, L., Wooster, T.J., Interfacial properties of deamidated wheat protein in relation to its ability to stabilise oil-in-water emulsions. Food Hydrocolloids 23:8 (2009), 2158–2167.
    • (2009) Food Hydrocolloids , vol.23 , Issue.8 , pp. 2158-2167
    • Day, L.1    Xu, M.2    Lundin, L.3    Wooster, T.J.4
  • 9
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation
    • Dong, A., Prestrelski, S.J., Allison, S.D., Carpenter, J.F., Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. Journal of Pharmaceutical Sciences 84:4 (1995), 415–424.
    • (1995) Journal of Pharmaceutical Sciences , vol.84 , Issue.4 , pp. 415-424
    • Dong, A.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 11
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M., Mantsch, H.H., The use and misuse of FTIR spectroscopy in the determination of protein structure. Critical Reviews in Biochemistry and Molecular Biology 30:2 (1995), 95–120.
    • (1995) Critical Reviews in Biochemistry and Molecular Biology , vol.30 , Issue.2 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 13
    • 33846610587 scopus 로고    scopus 로고
    • Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type
    • Klompong, V., Benjakul, S., Kantachote, D., Shahidi, F., Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chemistry 102:4 (2007), 1317–1327.
    • (2007) Food Chemistry , vol.102 , Issue.4 , pp. 1317-1327
    • Klompong, V.1    Benjakul, S.2    Kantachote, D.3    Shahidi, F.4
  • 14
    • 84921876574 scopus 로고    scopus 로고
    • The effect of deamidation on the structural, functional, and rheological properties of glutelin prepared from Akebia trifoliata var. australis seed
    • Lei, L., Zhao, Q., Selomulya, C., Xiong, H., The effect of deamidation on the structural, functional, and rheological properties of glutelin prepared from Akebia trifoliata var. australis seed. Food Chemistry 178 (2015), 96–105.
    • (2015) Food Chemistry , vol.178 , pp. 96-105
    • Lei, L.1    Zhao, Q.2    Selomulya, C.3    Xiong, H.4
  • 15
    • 77952581632 scopus 로고    scopus 로고
    • Functional, nutritional and conformational changes from deamidation of wheat gluten with succinic acid and citric acid
    • Liao, L., Liu, T.X., Zhao, M.M., Cui, C., Yuan, B.E., Tang, S., et al. Functional, nutritional and conformational changes from deamidation of wheat gluten with succinic acid and citric acid. Food Chemistry 123:1 (2010), 123–130.
    • (2010) Food Chemistry , vol.123 , Issue.1 , pp. 123-130
    • Liao, L.1    Liu, T.X.2    Zhao, M.M.3    Cui, C.4    Yuan, B.E.5    Tang, S.6
  • 17
    • 0036261525 scopus 로고    scopus 로고
    • Mechanism of heat and shear mediated aggregation of wheat gluten protein upon mixing
    • Morel, M.H., Redl, A., Guilbert, S., Mechanism of heat and shear mediated aggregation of wheat gluten protein upon mixing. Biomacromolecules 3:3 (2002), 488–497.
    • (2002) Biomacromolecules , vol.3 , Issue.3 , pp. 488-497
    • Morel, M.H.1    Redl, A.2    Guilbert, S.3
  • 18
    • 77949805635 scopus 로고    scopus 로고
    • Characterization of β-lactoglobulin fibrillar assembly using atomic force microscopy, polyacrylamide gel electrophoresis, and in situ Fourier transform infrared spectroscopy
    • Oboroceanu, D., Wang, L., Brodkorb, A., Magner, E., Auty, M.A., Characterization of β-lactoglobulin fibrillar assembly using atomic force microscopy, polyacrylamide gel electrophoresis, and in situ Fourier transform infrared spectroscopy. Journal of Agricultural and Food Chemistry 58:6 (2010), 3667–3673.
    • (2010) Journal of Agricultural and Food Chemistry , vol.58 , Issue.6 , pp. 3667-3673
    • Oboroceanu, D.1    Wang, L.2    Brodkorb, A.3    Magner, E.4    Auty, M.A.5
  • 19
    • 4444234284 scopus 로고    scopus 로고
    • Food protein analysis: Qualitative effects on processing
    • Marcel Dekker, Inc. New York (Chapter 1)
    • Owusu-Apenten, R.K., Food protein analysis: Qualitative effects on processing. 2002, Marcel Dekker, Inc., New York (Chapter 1).
    • (2002)
    • Owusu-Apenten, R.K.1
  • 20
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Evaluation of a turbidimetric technique
    • Pearce, K.N., Kinsella, J.E., Emulsifying properties of proteins: Evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry 26:3 (1978), 716–723.
    • (1978) Journal of Agricultural and Food Chemistry , vol.26 , Issue.3 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 21
    • 0026576158 scopus 로고
    • Conformation of wheat gluten proteins comparison between functional and solution states as determined by infrared spectroscopy
    • Pézolet, M., Bonenfant, S., Dousseau, F., Popineau, Y., Conformation of wheat gluten proteins comparison between functional and solution states as determined by infrared spectroscopy. FEBS Letters 299:3 (1992), 247–250.
    • (1992) FEBS Letters , vol.299 , Issue.3 , pp. 247-250
    • Pézolet, M.1    Bonenfant, S.2    Dousseau, F.3    Popineau, Y.4
  • 22
    • 84901928859 scopus 로고    scopus 로고
    • Comparison of the conformational and nutritional changes of deamidated wheat gliadin by citric acid and hydrochloric acid
    • Qiu, C., Sun, W., Su, G., Cui, C., Zhao, M., Comparison of the conformational and nutritional changes of deamidated wheat gliadin by citric acid and hydrochloric acid. Journal of Cereal Science 60:1 (2014), 143–150.
    • (2014) Journal of Cereal Science , vol.60 , Issue.1 , pp. 143-150
    • Qiu, C.1    Sun, W.2    Su, G.3    Cui, C.4    Zhao, M.5
  • 23
    • 35648986641 scopus 로고    scopus 로고
    • Factors affecting the stability of O/W emulsion in BSA solution: Stabilization by electrically neutral protein at high ionic strength
    • Rangsansarid, J., Fukada, K., Factors affecting the stability of O/W emulsion in BSA solution: Stabilization by electrically neutral protein at high ionic strength. Journal of Colloid and Interface Science 316:2 (2007), 779–786.
    • (2007) Journal of Colloid and Interface Science , vol.316 , Issue.2 , pp. 779-786
    • Rangsansarid, J.1    Fukada, K.2
  • 25
    • 14644425920 scopus 로고    scopus 로고
    • ATR-FT/IR study on the interactions between gliadins and dextrin and their effects on protein secondary structure
    • Secundo, F., Guerrieri, N., ATR-FT/IR study on the interactions between gliadins and dextrin and their effects on protein secondary structure. Journal of Agricultural and Food Chemistry 53:5 (2005), 1757–1764.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.5 , pp. 1757-1764
    • Secundo, F.1    Guerrieri, N.2
  • 27
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N., Woody, R.W., Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Analytical Biochemistry 287:2 (2000), 252–260.
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 28
    • 0025613794 scopus 로고
    • Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands
    • Venyaminov, S.Y., Kalnin, N.N., Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands. Biopolymers 30:13–14 (1990), 1243–1257.
    • (1990) Biopolymers , vol.30 , Issue.13-14 , pp. 1243-1257
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 29
    • 21444448203 scopus 로고    scopus 로고
    • Comparison of the official EC method for the determination of total volatile bases in fish with routine methods
    • Vyncke, W., Comparison of the official EC method for the determination of total volatile bases in fish with routine methods. Archiv für Lebensmittelhygiene 47 (1996), 110–112.
    • (1996) Archiv für Lebensmittelhygiene , vol.47 , pp. 110-112
    • Vyncke, W.1
  • 30
    • 80054986127 scopus 로고    scopus 로고
    • Conformational changes to deamidated wheat gliadins and β-casein upon adsorption to oil–water emulsion interfaces
    • Wong, B.T., Zhai, J., Hoffmann, S.V., Aguilar, M.I., Augustin, M., Wooster, T.J., et al. Conformational changes to deamidated wheat gliadins and β-casein upon adsorption to oil–water emulsion interfaces. Food Hydrocolloids 27:1 (2012), 91–101.
    • (2012) Food Hydrocolloids , vol.27 , Issue.1 , pp. 91-101
    • Wong, B.T.1    Zhai, J.2    Hoffmann, S.V.3    Aguilar, M.I.4    Augustin, M.5    Wooster, T.J.6
  • 31
    • 0026320363 scopus 로고
    • Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins
    • Wright, H.T., Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Critical Reviews in Biochemistry and Molecular Biology 26:1 (1991), 1–52.
    • (1991) Critical Reviews in Biochemistry and Molecular Biology , vol.26 , Issue.1 , pp. 1-52
    • Wright, H.T.1


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