메뉴 건너뛰기




Volumn 60, Issue 1, 2014, Pages 143-150

Comparison of the conformational and nutritional changes of deamidated wheat gliadin by citric acid and hydrochloric acid

Author keywords

Amino acid composition; Conformation; Deamidation; Wheat gliadin

Indexed keywords

TRITICUM AESTIVUM;

EID: 84901928859     PISSN: 07335210     EISSN: 10959963     Source Type: Journal    
DOI: 10.1016/j.jcs.2014.02.003     Document Type: Article
Times cited : (15)

References (29)
  • 1
    • 27144501099 scopus 로고    scopus 로고
    • Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by Fourier transform infrared spectroscopy and differential scanning calorimetry
    • Choi S.M., Ma C.Y. Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by Fourier transform infrared spectroscopy and differential scanning calorimetry. J.Agric. Food Chem. 2005, 53:8046-8053.
    • (2005) J.Agric. Food Chem. , vol.53 , pp. 8046-8053
    • Choi, S.M.1    Ma, C.Y.2
  • 2
    • 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 Hydrocoll. 2009, 23:2158-2167.
    • (2009) Food Hydrocoll. , vol.23 , pp. 2158-2167
    • Day, L.1    Xu, M.2    Lundin, L.3    Wooster, T.J.4
  • 4
    • 21344460693 scopus 로고    scopus 로고
    • Gelation properties of deamidated soluble wheat proteins
    • Friedli G.L., Howell N. Gelation properties of deamidated soluble wheat proteins. Food Hydrocoll. 1996, 10:255-261.
    • (1996) Food Hydrocoll. , vol.10 , pp. 255-261
    • Friedli, G.L.1    Howell, N.2
  • 5
    • 84866017508 scopus 로고    scopus 로고
    • Changes in secondary structure of gluten proteins due to emulsifiers
    • Gómez A.V., Ferrer E.G., Añón M.C., Puppo M.C. Changes in secondary structure of gluten proteins due to emulsifiers. J.Mol. Struct. 2013, 1033:51-58.
    • (2013) J.Mol. Struct. , vol.1033 , pp. 51-58
    • Gómez, A.V.1    Ferrer, E.G.2    Añón, M.C.3    Puppo, M.C.4
  • 6
    • 0032838567 scopus 로고    scopus 로고
    • Heat-induced changes in the nutritional properties of sodium caseinate
    • Guo M., Flynn A., Fox P. Heat-induced changes in the nutritional properties of sodium caseinate. Int. Dairy J. 1999, 9:243-247.
    • (1999) Int. Dairy J. , vol.9 , pp. 243-247
    • Guo, M.1    Flynn, A.2    Fox, P.3
  • 7
    • 15744372123 scopus 로고    scopus 로고
    • Nano-structure and properties of maize zein studied by atomic force microscopy
    • Guo Y.C., Liu Z.D., An H.J., Li M.Q., Hu J. Nano-structure and properties of maize zein studied by atomic force microscopy. J.Cereal Sci. 2005, 41:277-281.
    • (2005) J.Cereal Sci. , vol.41 , pp. 277-281
    • Guo, Y.C.1    Liu, Z.D.2    An, H.J.3    Li, M.Q.4    Hu, J.5
  • 8
    • 48149091243 scopus 로고    scopus 로고
    • Raman spectroscopic determination of structural changes in meat batters upon soy protein addition and heat treatment
    • Herrero A.M., Carmona P., Cofrades S., Jiménez-Colmenero F. Raman spectroscopic determination of structural changes in meat batters upon soy protein addition and heat treatment. Food Res. Int. 2008, 41:765-772.
    • (2008) Food Res. Int. , vol.41 , pp. 765-772
    • Herrero, A.M.1    Carmona, P.2    Cofrades, S.3    Jiménez-Colmenero, F.4
  • 10
    • 1542708303 scopus 로고    scopus 로고
    • Adifferential scanning calorimetry study of wheat proteins
    • León A., Rosell C.M., Barber C.B. Adifferential scanning calorimetry study of wheat proteins. Eur. Food Res. Technol. 2003, 217:13-16.
    • (2003) Eur. Food Res. Technol. , vol.217 , pp. 13-16
    • León, A.1    Rosell, C.M.2    Barber, C.B.3
  • 11
    • 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 Chem. 2010, 123:123-130.
    • (2010) Food Chem. , 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
  • 13
    • 84859793711 scopus 로고    scopus 로고
    • Functional properties of acetylated glutenin and gliadin at varying pH values
    • Majzoobi M., Abedi E., Farahnaky A., Aminlari M. Functional properties of acetylated glutenin and gliadin at varying pH values. Food Chem. 2012, 133:1402-1407.
    • (2012) Food Chem. , vol.133 , pp. 1402-1407
    • Majzoobi, M.1    Abedi, E.2    Farahnaky, A.3    Aminlari, M.4
  • 14
    • 0011211606 scopus 로고
    • Polymerization of deamidated peptide fragments obtained with the mild acid hydrolysis of ovalbumin
    • Matsudomi N., Sasaki T., Tanaka A., Kobayashi K., Kato Akio. Polymerization of deamidated peptide fragments obtained with the mild acid hydrolysis of ovalbumin. J. Agric. Food Chem. 1985, 33:738-742.
    • (1985) J. Agric. Food Chem. , vol.33 , pp. 738-742
    • Matsudomi, N.1    Sasaki, T.2    Tanaka, A.3    Kobayashi, K.4    Kato, A.5
  • 17
    • 84880045974 scopus 로고    scopus 로고
    • Emulsifying and surface properties of citric acid deamidated wheat gliadin
    • Qiu C.Y., Sun W.Z., Zhao Q.Z., Cui C., Zhao M.M. Emulsifying and surface properties of citric acid deamidated wheat gliadin. J.Cereal Sci. 2013, 58:68-75.
    • (2013) J.Cereal Sci. , vol.58 , pp. 68-75
    • Qiu, C.Y.1    Sun, W.Z.2    Zhao, Q.Z.3    Cui, C.4    Zhao, M.M.5
  • 18
    • 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. J.Agric. Food Chem. 2005, 53:1757-1764.
    • (2005) J.Agric. Food Chem. , vol.53 , pp. 1757-1764
    • Secundo, F.1    Guerrieri, N.2
  • 19
    • 80055018387 scopus 로고    scopus 로고
    • Structural evaluation of myofibrillar proteins during processing of Cantonese sausage by Raman spectroscopy
    • Sun W.Z., Zhao Q.Z., Zhao M.M., Yang B., Cui C., Ren J.Y. Structural evaluation of myofibrillar proteins during processing of Cantonese sausage by Raman spectroscopy. J.Agric. Food Chem. 2011, 59:11070-11077.
    • (2011) J.Agric. Food Chem. , vol.59 , pp. 11070-11077
    • Sun, W.Z.1    Zhao, Q.Z.2    Zhao, M.M.3    Yang, B.4    Cui, C.5    Ren, J.Y.6
  • 21
    • 80051837645 scopus 로고    scopus 로고
    • Disaggregation and reaggregation of gluten proteins by sodium chloride
    • Ukai T., Matsumura Y., Urade R. Disaggregation and reaggregation of gluten proteins by sodium chloride. J.Agric. Food Chem. 2008, 56:1122-1130.
    • (2008) J.Agric. Food Chem. , vol.56 , pp. 1122-1130
    • Ukai, T.1    Matsumura, Y.2    Urade, R.3
  • 22
    • 33744521246 scopus 로고    scopus 로고
    • Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration
    • Wang J.S., Zhao M.M., Yang X.Q., Jiang Y.M. Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration. J.Cereal Sci. 2006, 44:93-100.
    • (2006) J.Cereal Sci. , vol.44 , pp. 93-100
    • Wang, J.S.1    Zhao, M.M.2    Yang, X.Q.3    Jiang, Y.M.4
  • 23
    • 79960038166 scopus 로고    scopus 로고
    • Structural rearrangement of ethanol-denatured soy proteins by high hydrostatic pressure treatment
    • Wang J.M., Yang X.Q., Yin S.W., Zhang Y., Tang C.H., Li B.S., Yuan D.B., Guo J. Structural rearrangement of ethanol-denatured soy proteins by high hydrostatic pressure treatment. J.Agric. Food Chem. 2011, 59:7324-7332.
    • (2011) J.Agric. Food Chem. , vol.59 , pp. 7324-7332
    • Wang, J.M.1    Yang, X.Q.2    Yin, S.W.3    Zhang, Y.4    Tang, C.H.5    Li, B.S.6    Yuan, D.B.7    Guo, J.8
  • 24
    • 53949124105 scopus 로고    scopus 로고
    • Raman spectroscopic study of deamidated food proteins
    • Wong H.W., Choi S.M., Phillips D.L., Ma C.Y. Raman spectroscopic study of deamidated food proteins. Food Chem. 2009, 113:363-370.
    • (2009) Food Chem. , vol.113 , pp. 363-370
    • Wong, H.W.1    Choi, S.M.2    Phillips, D.L.3    Ma, C.Y.4
  • 25
    • 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 Hydrocoll. 2012, 27:91-101.
    • (2012) Food Hydrocoll. , 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
  • 26
    • 78651068611 scopus 로고    scopus 로고
    • Conformational study of red kidney bean (Phaseolus vulgaris L.) protein isolate (KPI) by tryptophan fluorescence and differential scanning calorimetry
    • Yin S.W., Tang C.H., Yang X.Q., Wen Q.B. Conformational study of red kidney bean (Phaseolus vulgaris L.) protein isolate (KPI) by tryptophan fluorescence and differential scanning calorimetry. J.Agric. Food Chem. 2011, 59:241-248.
    • (2011) J.Agric. Food Chem. , vol.59 , pp. 241-248
    • Yin, S.W.1    Tang, C.H.2    Yang, X.Q.3    Wen, Q.B.4
  • 27
    • 1842431424 scopus 로고    scopus 로고
    • Study of succinylated food proteins by Raman spectroscopy
    • Zhao Y., Ma C.Y., Yuen S.N., Phillips D.L. Study of succinylated food proteins by Raman spectroscopy. J.Agric. Food Chem. 2004, 52:1815-1823.
    • (2004) J.Agric. Food Chem. , vol.52 , pp. 1815-1823
    • Zhao, Y.1    Ma, C.Y.2    Yuen, S.N.3    Phillips, D.L.4
  • 28
    • 79958053016 scopus 로고    scopus 로고
    • Effects of deamidation on aggregation and emulsifying properties of barley glutenin
    • Zhao J., Tian Z., Chen L. Effects of deamidation on aggregation and emulsifying properties of barley glutenin. Food Chem. 2011, 128:1029-1036.
    • (2011) Food Chem. , vol.128 , pp. 1029-1036
    • Zhao, J.1    Tian, Z.2    Chen, L.3
  • 29
    • 43649092437 scopus 로고    scopus 로고
    • Reducing, radical scavenging, and chelation properties of invitro digests of alcalase-treated zein hydrolysate
    • Zhu L., Chen J., Tang X.Y., Xiong Y.L. Reducing, radical scavenging, and chelation properties of invitro digests of alcalase-treated zein hydrolysate. J.Agric. Food Chem. 2008, 56:2714-2721.
    • (2008) J.Agric. Food Chem. , vol.56 , pp. 2714-2721
    • Zhu, L.1    Chen, J.2    Tang, X.Y.3    Xiong, Y.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.