메뉴 건너뛰기




Volumn 75, Issue , 2018, Pages 223-228

Effect of oxidative modification on structural and foaming properties of egg white protein

Author keywords

Egg white protein; Foamability; Oxidation; Structural characteristics

Indexed keywords

HYDROPHOBICITY; MOLECULAR WEIGHT DISTRIBUTION; PROTEINS; SCANNING ELECTRON MICROSCOPY; SULFUR COMPOUNDS;

EID: 85029431048     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2017.08.008     Document Type: Article
Times cited : (182)

References (31)
  • 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
    • 33745914639 scopus 로고    scopus 로고
    • Albumen protein and functional properties of gelation and foaming
    • Alleoni, A.C.C., Albumen protein and functional properties of gelation and foaming. Scientia Agricola 63:3 (2006), 291–298.
    • (2006) Scientia Agricola , vol.63 , Issue.3 , pp. 291-298
    • Alleoni, A.C.C.1
  • 3
    • 85024876909 scopus 로고    scopus 로고
    • Globular plant protein aggregates for stabilization of food foams and emulsions
    • Amagliani, L., Schmitt, C., Globular plant protein aggregates for stabilization of food foams and emulsions. Trends in Food Science & Technology 67 (2017), 248–259.
    • (2017) Trends in Food Science & Technology , vol.67 , pp. 248-259
    • Amagliani, L.1    Schmitt, C.2
  • 4
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler, D.M., Susi, H., Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25:3 (1986), 469–487.
    • (1986) Biopolymers , vol.25 , Issue.3 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 5
    • 0347991735 scopus 로고    scopus 로고
    • Modification of functional properties of egg-white proteins
    • Campbell, L., Raikos, V., Euston, S.R., Modification of functional properties of egg-white proteins. Food/Nahrung 47:6 (2003), 369–376.
    • (2003) Food/Nahrung , vol.47 , Issue.6 , pp. 369-376
    • Campbell, L.1    Raikos, V.2    Euston, S.R.3
  • 6
    • 84973480997 scopus 로고    scopus 로고
    • Correlation between bulk characteristics of aggregated β-lactoglobulin and its surface and foaming properties
    • Dombrowski, J., Johler, F., Warncke, M., Kulozik, U., Correlation between bulk characteristics of aggregated β-lactoglobulin and its surface and foaming properties. Food Hydrocolloids 61 (2016), 318–328.
    • (2016) Food Hydrocolloids , vol.61 , pp. 318-328
    • Dombrowski, J.1    Johler, F.2    Warncke, M.3    Kulozik, U.4
  • 7
    • 84879250963 scopus 로고    scopus 로고
    • Rheology of interfacial protein-polysaccharide composites
    • Fischer, P., Rheology of interfacial protein-polysaccharide composites. The European Physical Journal Special Topics 222:1 (2013), 73–81.
    • (2013) The European Physical Journal Special Topics , vol.222 , Issue.1 , pp. 73-81
    • Fischer, P.1
  • 8
    • 84976597943 scopus 로고    scopus 로고
    • Oxidation of free, peptide and protein tryptophan residues mediated by AAPH-derived free radicals: Role of alkoxyl and peroxyl radicals
    • Fuentes-Lemus, E., Dorta, E., Escobar, E., Aspee, A., Pino, E., Abasq, M., et al. Oxidation of free, peptide and protein tryptophan residues mediated by AAPH-derived free radicals: Role of alkoxyl and peroxyl radicals. Rsc Advances 6:63 (2016), 57948–57955.
    • (2016) Rsc Advances , vol.6 , Issue.63 , pp. 57948-57955
    • Fuentes-Lemus, E.1    Dorta, E.2    Escobar, E.3    Aspee, A.4    Pino, E.5    Abasq, M.6
  • 9
    • 0002184555 scopus 로고
    • The conformation of proteins at interfaces and their role in stabilizing emulsions
    • Academic Press New York
    • Graham, D., Phillips, M., The conformation of proteins at interfaces and their role in stabilizing emulsions. 1976, Academic Press, New York.
    • (1976)
    • Graham, D.1    Phillips, M.2
  • 10
    • 84978864712 scopus 로고    scopus 로고
    • Oxidation of proline decreases immunoreactivity and alters structure of barley prolamin
    • Huang, X., Sontag-Strohm, T., Stoddard, F.L., Kato, Y., Oxidation of proline decreases immunoreactivity and alters structure of barley prolamin. Food Chemistry 214 (2017), 597–605.
    • (2017) Food Chemistry , vol.214 , pp. 597-605
    • Huang, X.1    Sontag-Strohm, T.2    Stoddard, F.L.3    Kato, Y.4
  • 12
    • 84929578956 scopus 로고    scopus 로고
    • Impact of pH on molecular structure and surface properties of lentil legumin-like protein and its application as foam stabilizer
    • Jarpa-Parra, M., Bamdad, F., Tian, Z., Zeng, H., Temelli, F., Chen, L., Impact of pH on molecular structure and surface properties of lentil legumin-like protein and its application as foam stabilizer. Colloids and Surfaces B: Biointerfaces 132 (2015), 45–53.
    • (2015) Colloids and Surfaces B: Biointerfaces , vol.132 , pp. 45-53
    • Jarpa-Parra, M.1    Bamdad, F.2    Tian, Z.3    Zeng, H.4    Temelli, F.5    Chen, L.6
  • 13
    • 0037612800 scopus 로고
    • Effect of pH and salts on the solubility of egg white protein
    • Kakalis, L.T., Regenstein, J.M., Effect of pH and salts on the solubility of egg white protein. Journal of Food Science 51:6 (1986), 1445–1447.
    • (1986) Journal of Food Science , vol.51 , Issue.6 , pp. 1445-1447
    • Kakalis, L.T.1    Regenstein, J.M.2
  • 15
    • 0032892342 scopus 로고    scopus 로고
    • Fluorescence due to interactions of oxidizing soybean oil and soy proteins
    • Liang, J.-H., Fluorescence due to interactions of oxidizing soybean oil and soy proteins. Food Chemistry 66:1 (1999), 103–108.
    • (1999) Food Chemistry , vol.66 , Issue.1 , pp. 103-108
    • Liang, J.-H.1
  • 16
    • 84862154203 scopus 로고    scopus 로고
    • Sensory characteristics and antioxidant activities of Maillard reaction products from soy protein hydrolysates with different molecular weight distribution
    • Liu, P., Huang, M., Song, S., Hayat, K., Zhang, X., Xia, S., et al. Sensory characteristics and antioxidant activities of Maillard reaction products from soy protein hydrolysates with different molecular weight distribution. Food and Bioprocess Technology 5:5 (2012), 1775–1789.
    • (2012) Food and Bioprocess Technology , vol.5 , Issue.5 , pp. 1775-1789
    • Liu, P.1    Huang, M.2    Song, S.3    Hayat, K.4    Zhang, X.5    Xia, S.6
  • 17
    • 84855674654 scopus 로고    scopus 로고
    • Effects of high hydrostatic pressure treatment on allergenicity and structural properties of soybean protein isolate for infant formula
    • Li, H., Zhu, K., Zhou, H., Peng, W., Effects of high hydrostatic pressure treatment on allergenicity and structural properties of soybean protein isolate for infant formula. Food Chemistry 132:2 (2012), 808–814.
    • (2012) Food Chemistry , vol.132 , Issue.2 , pp. 808-814
    • Li, H.1    Zhu, K.2    Zhou, H.3    Peng, W.4
  • 19
    • 84950335498 scopus 로고    scopus 로고
    • Recent approaches in physical modification of protein functionality
    • Mirmoghtadaie, L., Aliabadi, S.S., Hosseini, S.M., Recent approaches in physical modification of protein functionality. Food Chemistry 199 (2016), 619–627.
    • (2016) Food Chemistry , vol.199 , pp. 619-627
    • Mirmoghtadaie, L.1    Aliabadi, S.S.2    Hosseini, S.M.3
  • 20
    • 84939942662 scopus 로고    scopus 로고
    • Modification of foaming properties of soy protein isolate by high ultrasound intensity: Particle size effect
    • Morales, R., Martínez, K.D., Ruiz-Henestrosa, V.M.P., Pilosof, A.M., Modification of foaming properties of soy protein isolate by high ultrasound intensity: Particle size effect. Ultrasonics Sonochemistry 26 (2015), 48–55.
    • (2015) Ultrasonics Sonochemistry , vol.26 , pp. 48-55
    • Morales, R.1    Martínez, K.D.2    Ruiz-Henestrosa, V.M.P.3    Pilosof, A.M.4
  • 21
    • 33646525423 scopus 로고    scopus 로고
    • Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins
    • Morzel, M., Gatellier, P., Sayd, T., Renerre, M., Laville, E., Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins. Meat Science 73:3 (2006), 536–543.
    • (2006) Meat Science , vol.73 , Issue.3 , pp. 536-543
    • Morzel, M.1    Gatellier, P.2    Sayd, T.3    Renerre, M.4    Laville, E.5
  • 23
    • 85006892686 scopus 로고    scopus 로고
    • Effect of hydrogen peroxide on improving the heat stability of whey protein isolate solutions
    • Sutariya, S., Patel, H., Effect of hydrogen peroxide on improving the heat stability of whey protein isolate solutions. Food Chemistry 223 (2017), 114–120.
    • (2017) Food Chemistry , vol.223 , pp. 114-120
    • Sutariya, S.1    Patel, H.2
  • 25
    • 84893487854 scopus 로고    scopus 로고
    • Effect of frozen storage on physico-chemistry of wheat gluten proteins: Studies on gluten-, glutenin-and gliadin-rich fractions
    • Wang, P., Chen, H., Mohanad, B., Xu, L., Ning, Y., Xu, J., et al. Effect of frozen storage on physico-chemistry of wheat gluten proteins: Studies on gluten-, glutenin-and gliadin-rich fractions. Food Hydrocolloids 39 (2014), 187–194.
    • (2014) Food Hydrocolloids , vol.39 , pp. 187-194
    • Wang, P.1    Chen, H.2    Mohanad, B.3    Xu, L.4    Ning, Y.5    Xu, J.6
  • 26
    • 84975230514 scopus 로고    scopus 로고
    • Effect of oxidization and chitosan on the surface activity of soy protein isolate
    • Wang, W., Li, J., Yan, L., Huang, G., Dong, Z., Effect of oxidization and chitosan on the surface activity of soy protein isolate. Carbohydrate Polymers 151 (2016), 700–706.
    • (2016) Carbohydrate Polymers , vol.151 , pp. 700-706
    • Wang, W.1    Li, J.2    Yan, L.3    Huang, G.4    Dong, Z.5
  • 27
    • 84901910835 scopus 로고    scopus 로고
    • Effect of frozen storage on the foaming properties of wheat gliadin
    • Wang, P., Tao, H., Wu, F., Yang, N., Chen, F., Jin, Z., et al. Effect of frozen storage on the foaming properties of wheat gliadin. Food Chemistry 164 (2014), 44–49.
    • (2014) Food Chemistry , vol.164 , pp. 44-49
    • Wang, P.1    Tao, H.2    Wu, F.3    Yang, N.4    Chen, F.5    Jin, Z.6
  • 28
    • 70349985769 scopus 로고    scopus 로고
    • Structural modification of soy protein by 13-hydroperoxyoctadecadienoic acid
    • Wu, W., Hou, L., Zhang, C., Kong, X., Hua, Y., Structural modification of soy protein by 13-hydroperoxyoctadecadienoic acid. European Food Research and Technology 229:5 (2009), 771–778.
    • (2009) European Food Research and Technology , vol.229 , Issue.5 , pp. 771-778
    • Wu, W.1    Hou, L.2    Zhang, C.3    Kong, X.4    Hua, Y.5
  • 29
    • 84897657554 scopus 로고    scopus 로고
    • Effects of oxidative modification on thermal aggregation and gel properties of soy protein by malondialdehyde
    • Wu, W., Hua, Y., Lin, Q., Effects of oxidative modification on thermal aggregation and gel properties of soy protein by malondialdehyde. Journal of Food Science and Technology 51:3 (2014), 485–493.
    • (2014) Journal of Food Science and Technology , vol.51 , Issue.3 , pp. 485-493
    • Wu, W.1    Hua, Y.2    Lin, Q.3
  • 30
    • 64449084784 scopus 로고    scopus 로고
    • Oxidative modification of soy protein by peroxyl radicals
    • Wu, W., Zhang, C., Kong, X., Hua, Y., Oxidative modification of soy protein by peroxyl radicals. Food Chemistry 116:1 (2009), 295–301.
    • (2009) Food Chemistry , vol.116 , Issue.1 , pp. 295-301
    • Wu, W.1    Zhang, C.2    Kong, X.3    Hua, Y.4
  • 31
    • 84884277420 scopus 로고    scopus 로고
    • Protein oxidation: Basic principles and implications for meat quality
    • Zhang, W., Xiao, S., Ahn, D.U., Protein oxidation: Basic principles and implications for meat quality. Critical Reviews in Food Science and Nutrition 53:11 (2013), 1191–1201.
    • (2013) Critical Reviews in Food Science and Nutrition , vol.53 , Issue.11 , pp. 1191-1201
    • Zhang, W.1    Xiao, S.2    Ahn, D.U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.