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Volumn 58, Issue 1, 2013, Pages 68-75

Emulsifying and surface properties of citric acid deamidated wheat gliadin

Author keywords

Deamidated wheat gliadin; Emulsion; Heat treatment; Surface pressure

Indexed keywords

TRITICUM AESTIVUM;

EID: 84880045974     PISSN: 07335210     EISSN: 10959963     Source Type: Journal    
DOI: 10.1016/j.jcs.2013.04.002     Document Type: Article
Times cited : (36)

References (31)
  • 1
    • 0032936698 scopus 로고    scopus 로고
    • Solubilized wheat protein isolate: functional properties and potential food applications
    • Ahmedna M., Prinyawiwatkul W., Rao R.M. Solubilized wheat protein isolate: functional properties and potential food applications. Journal of Agriculture and Food Chemistry 1999, 47:1340-1345.
    • (1999) Journal of Agriculture and Food Chemistry , vol.47 , pp. 1340-1345
    • Ahmedna, M.1    Prinyawiwatkul, W.2    Rao, R.M.3
  • 2
    • 77955049940 scopus 로고    scopus 로고
    • Temperature and pH as factors influencing droplet size distribution and linear viscoelasticity of O/W emulsions stabilized by soy and gluten proteins
    • Bengoechea C., Romero A., Aguilar J.M., Cordobés F., Guerrero A. Temperature and pH as factors influencing droplet size distribution and linear viscoelasticity of O/W emulsions stabilized by soy and gluten proteins. Food Hydrocolloids 2010, 24:783-791.
    • (2010) Food Hydrocolloids , vol.24 , pp. 783-791
    • Bengoechea, C.1    Romero, A.2    Aguilar, J.M.3    Cordobés, F.4    Guerrero, A.5
  • 4
    • 79952758423 scopus 로고    scopus 로고
    • Effects of ultrasound pretreatment on the enzymatic hydrolysis of soy protein isolates and on the emulsifying properties of hydrolysates
    • Chen L., Chen J.S., Ren J.Y., Zhao M.M. Effects of ultrasound pretreatment on the enzymatic hydrolysis of soy protein isolates and on the emulsifying properties of hydrolysates. Journal of Agriculture and Food Chemistry 2011, 59:2600-2609.
    • (2011) Journal of Agriculture and Food Chemistry , vol.59 , pp. 2600-2609
    • Chen, L.1    Chen, J.S.2    Ren, J.Y.3    Zhao, M.M.4
  • 6
    • 70149092311 scopus 로고    scopus 로고
    • Interfacial properties of deamidated wheat protein in relation to its ability to stabilize 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 stabilize oil-in-water emulsions. Food Hydrocolloids 2009, 23:2158-2167.
    • (2009) Food Hydrocolloids , vol.23 , pp. 2158-2167
    • Day, L.1    Xu, M.2    Lundin, L.3    Wooster, T.J.4
  • 7
    • 9744250918 scopus 로고    scopus 로고
    • Adsorption kinetics and rheological interfacial properties of plant proteins at the oil-water interface
    • Ducel V., Richard J., Popineau Y., Boury F. Adsorption kinetics and rheological interfacial properties of plant proteins at the oil-water interface. Biomacromolecules 2004, 5:2088-2093.
    • (2004) Biomacromolecules , vol.5 , pp. 2088-2093
    • Ducel, V.1    Richard, J.2    Popineau, Y.3    Boury, F.4
  • 8
    • 84981375054 scopus 로고
    • Rheological and interfacial behavior of some wheat protein fractions
    • Eliasson A., Lundh G. Rheological and interfacial behavior of some wheat protein fractions. Journal of Texture Studies 1989, 20:431-441.
    • (1989) Journal of Texture Studies , vol.20 , pp. 431-441
    • Eliasson, A.1    Lundh, G.2
  • 9
    • 77957823944 scopus 로고    scopus 로고
    • Emulsifying properties of sweet potato protein: effect of protein concentration and oil volume fraction
    • Guo Q., Mu T. Emulsifying properties of sweet potato protein: effect of protein concentration and oil volume fraction. Food Hydrocolloids 2011, 25:98-106.
    • (2011) Food Hydrocolloids , vol.25 , pp. 98-106
    • Guo, Q.1    Mu, T.2
  • 11
  • 12
    • 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., Delcour J.A. The impact of heating and cooling on the physico-chemical properties of wheat gluten-water suspensions. Journal of Cereal Science 2005, 42:327-333.
    • (2005) Journal of Cereal Science , vol.42 , pp. 327-333
    • Lagrain, B.1    Brijs, K.2    Veraverbeke, W.S.3    Delcour, J.A.4
  • 13
    • 77950169850 scopus 로고    scopus 로고
    • Molecular basis of processing wheat gluten toward biobased materials
    • Lagrain B., Goderis B., Brijs K., Delcour J.A. Molecular basis of processing wheat gluten toward biobased materials. Biomacromolecules 2010, 11:533-541.
    • (2010) Biomacromolecules , vol.11 , pp. 533-541
    • Lagrain, B.1    Goderis, B.2    Brijs, K.3    Delcour, J.A.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., Yang F. Functional, nutritional and conformational changes from deamidation of wheat gluten with succinic acid and citric acid. Food Chemistry 2010, 123:123-130.
    • (2010) Food Chemistry , vol.123 , pp. 123-130
    • Liao, L.1    Liu, T.X.2    Zhao, M.M.3    Cui, C.4    Yuan, B.E.5    Tang, S.6    Yang, F.7
  • 16
    • 79952535945 scopus 로고    scopus 로고
    • Dynamic surface pressure and dilatational viscoelasticity of sodium caseinate/xanthan gum mixtures at the oil-water interface
    • Liu L.Y., Zhao Q.Z., Liu T.X., Zhao M.M. Dynamic surface pressure and dilatational viscoelasticity of sodium caseinate/xanthan gum mixtures at the oil-water interface. Food Hydrocolloids 2011, 25:921-927.
    • (2011) Food Hydrocolloids , vol.25 , pp. 921-927
    • Liu, L.Y.1    Zhao, Q.Z.2    Liu, T.X.3    Zhao, M.M.4
  • 18
    • 0000389663 scopus 로고
    • Combined acid deamidation and enzymatic-hydrolysis for improvement of the functional-properties of wheat gluten
    • Mimouni B., Raymond J., Merledesnoyers A.M., Azanza J.L., Ducastaing A. Combined acid deamidation and enzymatic-hydrolysis for improvement of the functional-properties of wheat gluten. Journal of Cereal Science 1994, 21:153-165.
    • (1994) Journal of Cereal Science , vol.21 , pp. 153-165
    • Mimouni, B.1    Raymond, J.2    Merledesnoyers, A.M.3    Azanza, J.L.4    Ducastaing, A.5
  • 19
    • 79851478055 scopus 로고    scopus 로고
    • Denaturation of soy proteins in solution and at the oil-water interface: a fluorescence study
    • Miriani M., Keerati-u-rai M., Corredig M., Iametti S., Bonomi F. Denaturation of soy proteins in solution and at the oil-water interface: a fluorescence study. Food Hydrocolloids 2011, 25:620-626.
    • (2011) Food Hydrocolloids , vol.25 , pp. 620-626
    • Miriani, M.1    Keerati-u-rai, M.2    Corredig, M.3    Iametti, S.4    Bonomi, F.5
  • 20
    • 4143097041 scopus 로고    scopus 로고
    • Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin
    • Pallarès I., Vendrell J., Avilés F.X., Ventura S. Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin. Journal of Molecular Biology 2004, 342:321-331.
    • (2004) Journal of Molecular Biology , vol.342 , pp. 321-331
    • Pallarès, I.1    Vendrell, J.2    Avilés, F.X.3    Ventura, S.4
  • 22
    • 55549125193 scopus 로고    scopus 로고
    • Adsorption and structural change of β-Lactoglobulin at the diacylglycerol-water interface
    • Sakuno M.M., Matsumoto S., Kawai S., Taihei K., Matsumura Y. Adsorption and structural change of β-Lactoglobulin at the diacylglycerol-water interface. Langmuir 2008, 24:11483-11488.
    • (2008) Langmuir , vol.24 , pp. 11483-11488
    • Sakuno, M.M.1    Matsumoto, S.2    Kawai, S.3    Taihei, K.4    Matsumura, Y.5
  • 23
    • 84859152164 scopus 로고    scopus 로고
    • Microfluidization as a potential technique to modify surface properties of soy protein isolate
    • Shen L., Tang C.H. Microfluidization as a potential technique to modify surface properties of soy protein isolate. Food Research International 2012, 48:108-118.
    • (2012) Food Research International , vol.48 , pp. 108-118
    • Shen, L.1    Tang, C.H.2
  • 24
    • 0034975223 scopus 로고    scopus 로고
    • Emulsifying and surface properties of wheat gluten under acidic condition
    • Takeda K., Matsumura Y., Shimizu M. Emulsifying and surface properties of wheat gluten under acidic condition. Journal of Food Science 2001, 66:393-399.
    • (2001) Journal of Food Science , vol.66 , pp. 393-399
    • Takeda, K.1    Matsumura, Y.2    Shimizu, M.3
  • 26
    • 68949214303 scopus 로고    scopus 로고
    • Characteristics of enzymatic hydrolysis of thermal-treated wheat gluten
    • Wang J.S., Wei Z.Y., Li L., Bian K., Zhao M.M. Characteristics of enzymatic hydrolysis of thermal-treated wheat gluten. Journal of Ceareal Science 2009, 50:205-209.
    • (2009) Journal of Ceareal Science , vol.50 , pp. 205-209
    • Wang, J.S.1    Wei, Z.Y.2    Li, L.3    Bian, K.4    Zhao, M.M.5
  • 27
    • 59549096539 scopus 로고    scopus 로고
    • The effect of maillard conjugation of deamidated wheat proteins with low molecular weight carbohydrates on the secondary structure of the protein
    • Wong B.T., Day L., McNaughton D., Augustin M.A. The effect of maillard conjugation of deamidated wheat proteins with low molecular weight carbohydrates on the secondary structure of the protein. Food Biophysics 2009, 4:1-12.
    • (2009) Food Biophysics , vol.4 , pp. 1-12
    • Wong, B.T.1    Day, L.2    McNaughton, D.3    Augustin, M.A.4
  • 28
    • 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.A., Wooster T.J., Day L. Conformational changes to deamidated wheat gliadins and β-casein upon adsorption to oil-water emulsion interfaces. Food Hydrocolloids 2012, 27:91-101.
    • (2012) Food Hydrocolloids , vol.27 , pp. 91-101
    • Wong, B.T.1    Zhai, J.2    Hoffmann, S.V.3    Aguilar, M.I.4    Augustin, M.A.5    Wooster, T.J.6    Day, L.7
  • 30
    • 77950630279 scopus 로고    scopus 로고
    • Surface protein composition and concentration of whey protein isolate-stabilized oil-in-water emulsions: effect of heat treatment
    • Ye A. Surface protein composition and concentration of whey protein isolate-stabilized oil-in-water emulsions: effect of heat treatment. Colloids and Surface B: Biointerfaces 2010, 78:24-29.
    • (2010) Colloids and Surface B: Biointerfaces , vol.78 , pp. 24-29
    • Ye, A.1
  • 31
    • 33748437518 scopus 로고    scopus 로고
    • Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten
    • Yong Y.H., Yamaguchi S., Matsumura Y. Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten. Journal of Agriculture and Food Chemistry 2006, 54:6034-6040.
    • (2006) Journal of Agriculture and Food Chemistry , vol.54 , pp. 6034-6040
    • Yong, Y.H.1    Yamaguchi, S.2    Matsumura, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.