메뉴 건너뛰기




Volumn 24, Issue 1, 2010, Pages 81-87

Rheological investigation of soy protein hydrogels induced by Maillard-type reaction

Author keywords

Cross linking; Fractal; Gel; Protein; Rheology; Stress hardening

Indexed keywords

CROSSLINKING; FRACTAL DIMENSION; GLYCOSYLATION; HYDROGELS;

EID: 70349974830     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2009.08.009     Document Type: Article
Times cited : (28)

References (40)
  • 5
    • 58149461412 scopus 로고    scopus 로고
    • Physicochemical properties and microstructure of soy protein hydrogels co-induced by Maillard type cross-linking and salt
    • Caillard R., Remondetto G.E., and Subirade M. Physicochemical properties and microstructure of soy protein hydrogels co-induced by Maillard type cross-linking and salt. Food Research International 42 (2009) 98-106
    • (2009) Food Research International , vol.42 , pp. 98-106
    • Caillard, R.1    Remondetto, G.E.2    Subirade, M.3
  • 6
    • 0037120733 scopus 로고    scopus 로고
    • Rheological study on lysozyme/tetramelthylurea viscoelastic matrices
    • Da Silva M.A., and Arêas E.P.G. Rheological study on lysozyme/tetramelthylurea viscoelastic matrices. Biophysical Chemistry 99 (2002) 129-141
    • (2002) Biophysical Chemistry , vol.99 , pp. 129-141
    • Da Silva, M.A.1    Arêas, E.P.G.2
  • 7
    • 23844482849 scopus 로고    scopus 로고
    • Solvent-induced lysozyme gels: rheology, fractal analysis, and sol-gel kinetics
    • Da Silva M.A., and Arêas E.P.G. Solvent-induced lysozyme gels: rheology, fractal analysis, and sol-gel kinetics. Journal of Colloid and Interface Science 289 (2005) 394-401
    • (2005) Journal of Colloid and Interface Science , vol.289 , pp. 394-401
    • Da Silva, M.A.1    Arêas, E.P.G.2
  • 8
    • 33750491607 scopus 로고    scopus 로고
    • Structure of heat-induced plasma protein gels studied by fractal and lacunarity analysis
    • Dàvila E., and Parés D. Structure of heat-induced plasma protein gels studied by fractal and lacunarity analysis. Food Hydrocolloids 21 (2007) 147-153
    • (2007) Food Hydrocolloids , vol.21 , pp. 147-153
    • Dàvila, E.1    Parés, D.2
  • 9
    • 0031259385 scopus 로고    scopus 로고
    • Enzymic crosslinking as a tool for food colloid rheology control and interfacial stabilization
    • Dickinson E. Enzymic crosslinking as a tool for food colloid rheology control and interfacial stabilization. Trends in Food Science and Technology 8 (1997) 334-339
    • (1997) Trends in Food Science and Technology , vol.8 , pp. 334-339
    • Dickinson, E.1
  • 10
    • 0037210719 scopus 로고    scopus 로고
    • Maillard crosslinking of food proteins II: the reaction of glutaraldehyde, formaldehyde and glyceraldehyde with wheat proteins in vitro and in situ
    • Gerrard J.A., Brown P.K., and Fayle S.E. Maillard crosslinking of food proteins II: the reaction of glutaraldehyde, formaldehyde and glyceraldehyde with wheat proteins in vitro and in situ. Food Chemistry 80 1 (2003) 35-43
    • (2003) Food Chemistry , vol.80 , Issue.1 , pp. 35-43
    • Gerrard, J.A.1    Brown, P.K.2    Fayle, S.E.3
  • 11
    • 0037210603 scopus 로고    scopus 로고
    • Maillard crosslinking of food proteins III: the reaction of glutaraldehyde, formaldehyde and glyceraldehyde upon bread and croissants
    • Gerrard J.A., Brown P.K., and Fayle S.E. Maillard crosslinking of food proteins III: the reaction of glutaraldehyde, formaldehyde and glyceraldehyde upon bread and croissants. Food Chemistry 80 1 (2003) 45-50
    • (2003) Food Chemistry , vol.80 , Issue.1 , pp. 45-50
    • Gerrard, J.A.1    Brown, P.K.2    Fayle, S.E.3
  • 12
    • 4243282343 scopus 로고    scopus 로고
    • Strain hardening of fractal colloidal gels
    • Gisler T., Ball R.C., and Weitz D.A. Strain hardening of fractal colloidal gels. Physical Review Letters 82 5 (1999) 1064-1067
    • (1999) Physical Review Letters , vol.82 , Issue.5 , pp. 1064-1067
    • Gisler, T.1    Ball, R.C.2    Weitz, D.A.3
  • 17
    • 13844297080 scopus 로고    scopus 로고
    • Formation of soy protein isolate cold-set gels: protein and salt effects
    • Maltais A., Remondetto G.E., Gonzalez R., and Subirade M. Formation of soy protein isolate cold-set gels: protein and salt effects. Journal of Food Science 70 1 (2005) 67-73
    • (2005) Journal of Food Science , vol.70 , Issue.1 , pp. 67-73
    • Maltais, A.1    Remondetto, G.E.2    Gonzalez, R.3    Subirade, M.4
  • 18
    • 38849203059 scopus 로고    scopus 로고
    • Mechanisms involved in the formation and structure of soya protein cold-set gels: a molecular and supramolecular investigation
    • Maltais A., Remondetto G.E., and Subirade M. Mechanisms involved in the formation and structure of soya protein cold-set gels: a molecular and supramolecular investigation. Food Hydrocolloids 22 5 (2008) 550-559
    • (2008) Food Hydrocolloids , vol.22 , Issue.5 , pp. 550-559
    • Maltais, A.1    Remondetto, G.E.2    Subirade, M.3
  • 19
    • 0033833121 scopus 로고    scopus 로고
    • On the structure of particulate gels-the case of salt-induced cold gelation of heat denatured whey protein isolate
    • Marangoni A.G., Barbut S., McGauley S.E., Marcone M., and Narine S.S. On the structure of particulate gels-the case of salt-induced cold gelation of heat denatured whey protein isolate. Food Hydrocolloids 14 (2000) 61-74
    • (2000) Food Hydrocolloids , vol.14 , pp. 61-74
    • Marangoni, A.G.1    Barbut, S.2    McGauley, S.E.3    Marcone, M.4    Narine, S.S.5
  • 20
    • 0036255796 scopus 로고    scopus 로고
    • Categorization of rheological scaling models for particle gels applied to casein gels
    • Mellema M., van Opheusden J.H.J., and van Vliet T. Categorization of rheological scaling models for particle gels applied to casein gels. Journal of Rheology 46 (2002) 11-29
    • (2002) Journal of Rheology , vol.46 , pp. 11-29
    • Mellema, M.1    van Opheusden, J.H.J.2    van Vliet, T.3
  • 23
    • 0028518807 scopus 로고
    • Dynamic viscoelastic properties of glycinin and β-conglycinin gels from soybeans
    • Nagano T., Akasaka T., and Nishinari K. Dynamic viscoelastic properties of glycinin and β-conglycinin gels from soybeans. Biopolymers 34 (1994) 1303-1309
    • (1994) Biopolymers , vol.34 , pp. 1303-1309
    • Nagano, T.1    Akasaka, T.2    Nishinari, K.3
  • 25
    • 0028013387 scopus 로고
    • Rheological properties and conformational states of β-conglycinin gels at acidic pH
    • Nagano T., Mori H., and Nishinari K. Rheological properties and conformational states of β-conglycinin gels at acidic pH. Biopolymers 34 (1994) 293-298
    • (1994) Biopolymers , vol.34 , pp. 293-298
    • Nagano, T.1    Mori, H.2    Nishinari, K.3
  • 26
    • 1042301089 scopus 로고    scopus 로고
    • Scaling and fractal analysis of viscoelastic properties of heat-induced protein gels
    • Ould Eleya M.M., Ko S., and Gunasekaran S. Scaling and fractal analysis of viscoelastic properties of heat-induced protein gels. Food Hydrocolloids 18 (2004) 315-323
    • (2004) Food Hydrocolloids , vol.18 , pp. 315-323
    • Ould Eleya, M.M.1    Ko, S.2    Gunasekaran, S.3
  • 28
    • 0344444635 scopus 로고    scopus 로고
    • Relations between rheological properties and network structure of soy protein gels
    • Renkema J.M.S. Relations between rheological properties and network structure of soy protein gels. Food Hydrocolloids 18 1 (2004) 39-47
    • (2004) Food Hydrocolloids , vol.18 , Issue.1 , pp. 39-47
    • Renkema, J.M.S.1
  • 29
    • 0035186748 scopus 로고    scopus 로고
    • Gel formation by β-conglycinin and glycinin and their mixtures
    • Renkema J.M.S., Knabben J.H.M., and van Vliet T. Gel formation by β-conglycinin and glycinin and their mixtures. Food Hydrocolloids 15 (2001) 407-414
    • (2001) Food Hydrocolloids , vol.15 , pp. 407-414
    • Renkema, J.M.S.1    Knabben, J.H.M.2    van Vliet, T.3
  • 30
    • 1542358897 scopus 로고    scopus 로고
    • Concentration dependence of dynamic moduli of heat-induced soy protein hydrogels
    • Renkema J.M.S., and van Vliet T. Concentration dependence of dynamic moduli of heat-induced soy protein hydrogels. Food Hydrocolloids 18 3 (2004) 483-487
    • (2004) Food Hydrocolloids , vol.18 , Issue.3 , pp. 483-487
    • Renkema, J.M.S.1    van Vliet, T.2
  • 31
    • 0001024684 scopus 로고
    • Scaling behavior of elastic properties of colloidal gels
    • Shih W.-H., Shih W.Y., Kim S.-I., Liu J., and Aksay I.A. Scaling behavior of elastic properties of colloidal gels. Physical Review A 42 8 (1990) 4772-4779
    • (1990) Physical Review A , vol.42 , Issue.8 , pp. 4772-4779
    • Shih, W.-H.1    Shih, W.Y.2    Kim, S.-I.3    Liu, J.4    Aksay, I.A.5
  • 33
    • 33645903211 scopus 로고    scopus 로고
    • Effects of transglutaminase treatment on the thermal properties of soy protein isolates
    • Tang C.-H., Chen Z., Li L., and Yang X.-Q. Effects of transglutaminase treatment on the thermal properties of soy protein isolates. Food Research International 39 6 (2006) 704-711
    • (2006) Food Research International , vol.39 , Issue.6 , pp. 704-711
    • Tang, C.-H.1    Chen, Z.2    Li, L.3    Yang, X.-Q.4
  • 34
    • 26844437327 scopus 로고    scopus 로고
    • Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase
    • Tang C.-H., Wu H., Chen Z., and Yang X.-Q. Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase. Food Research International 39 1 (2006) 87-97
    • (2006) Food Research International , vol.39 , Issue.1 , pp. 87-97
    • Tang, C.-H.1    Wu, H.2    Chen, Z.3    Yang, X.-Q.4
  • 35
    • 33645137009 scopus 로고    scopus 로고
    • Coagulation and gelation of soy protein isolates induced by microbial transglutaminase
    • Tang C.-H., Wu H., Yu H.-P., Li L., Chen Z., and Yang X.-Q. Coagulation and gelation of soy protein isolates induced by microbial transglutaminase. Journal of Food Biochemistry 30 1 (2006) 35-55
    • (2006) Journal of Food Biochemistry , vol.30 , Issue.1 , pp. 35-55
    • Tang, C.-H.1    Wu, H.2    Yu, H.-P.3    Li, L.4    Chen, Z.5    Yang, X.-Q.6
  • 38
    • 0035249267 scopus 로고    scopus 로고
    • A model relating structure of colloidal gels to their elastic properties
    • Wu H., and Morbidelli M. A model relating structure of colloidal gels to their elastic properties. Langmuir 17 (2001) 1030-1036
    • (2001) Langmuir , vol.17 , pp. 1030-1036
    • Wu, H.1    Morbidelli, M.2
  • 39
    • 4444224511 scopus 로고    scopus 로고
    • Cooling effects on a model rennet casein gel system: part I. Rheological characterization
    • Zhong Q., Daubert R.C., and Velev O.D. Cooling effects on a model rennet casein gel system: part I. Rheological characterization. Langmuir 20 (2004) 7399-7405
    • (2004) Langmuir , vol.20 , pp. 7399-7405
    • Zhong, Q.1    Daubert, R.C.2    Velev, O.D.3
  • 40
    • 4444266641 scopus 로고    scopus 로고
    • Cooling effects on a model rennet casein gel system. Part II. Permeability and microscopy
    • Zhong Q., Daubert C.R., and Velev O.D. Cooling effects on a model rennet casein gel system. Part II. Permeability and microscopy. Langmuir 20 (2004) 7406-7411
    • (2004) Langmuir , vol.20 , pp. 7406-7411
    • Zhong, Q.1    Daubert, C.R.2    Velev, O.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.