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Volumn 39, Issue 6, 2006, Pages 704-711

Effects of transglutaminase treatment on the thermal properties of soy protein isolates

Author keywords

Cross linking; Glass transition; Soy protein isolates; Thermal property; Transglutaminase

Indexed keywords

CROSSLINKING; GLASS TRANSITION; HYDRATION; POLYMERS; PROTEINS; THERMAL EFFECTS;

EID: 33645903211     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2006.01.012     Document Type: Article
Times cited : (80)

References (34)
  • 1
    • 0000579294 scopus 로고
    • The influence of processing parameters on food protein functionality. I. Differential scanning calorimetry as an indicator of protein denaturation
    • Arntfield S.D., and Murray E.D. The influence of processing parameters on food protein functionality. I. Differential scanning calorimetry as an indicator of protein denaturation. Canadian Institute of Food Science and Technology Journal 14 (1981) 289-294
    • (1981) Canadian Institute of Food Science and Technology Journal , vol.14 , pp. 289-294
    • Arntfield, S.D.1    Murray, E.D.2
  • 2
    • 0034255689 scopus 로고    scopus 로고
    • Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein
    • Babiker E.E. Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein. Food Chemistry 70 (2000) 139-145
    • (2000) Food Chemistry , vol.70 , pp. 139-145
    • Babiker, E.E.1
  • 3
    • 0030265397 scopus 로고    scopus 로고
    • Polymerization of soy protein digests by microbial transglutaminase for improvement of the functional properties
    • Babiker E.E., Khan M.A.S., Matsudomi N., and Kato A. Polymerization of soy protein digests by microbial transglutaminase for improvement of the functional properties. Food Research International 29 (1996) 627-634
    • (1996) Food Research International , vol.29 , pp. 627-634
    • Babiker, E.E.1    Khan, M.A.S.2    Matsudomi, N.3    Kato, A.4
  • 4
    • 0035021486 scopus 로고    scopus 로고
    • Influence of transglutaminase treatment on the thermoreversible gelation of gelatin
    • Babin H., and Dickinson E. Influence of transglutaminase treatment on the thermoreversible gelation of gelatin. Food Hydrocolloids 15 (2001) 271-276
    • (2001) Food Hydrocolloids , vol.15 , pp. 271-276
    • Babin, H.1    Dickinson, E.2
  • 5
    • 0029739584 scopus 로고    scopus 로고
    • Glass transition temperatures determined using a temperature-cycling scanning calorimeter
    • 828
    • Bell L.N., and Touma D.E. Glass transition temperatures determined using a temperature-cycling scanning calorimeter. Journal of Food Science 61 (1996) 807-810 828
    • (1996) Journal of Food Science , vol.61 , pp. 807-810
    • Bell, L.N.1    Touma, D.E.2
  • 6
    • 4243167095 scopus 로고
    • A classical thermodynamic discussion of the effect of composition on glass-transition temperatures
    • Couchman P.R., and Karasz F.E. A classical thermodynamic discussion of the effect of composition on glass-transition temperatures. Macromolecules 11 (1978) 117-119
    • (1978) Macromolecules , vol.11 , pp. 117-119
    • Couchman, P.R.1    Karasz, F.E.2
  • 7
    • 0035085054 scopus 로고    scopus 로고
    • Characterization of glass transition of durum wheat semolina using modulated differential scanning calorimetry
    • Cuq B., and Lcard-Vernière. Characterization of glass transition of durum wheat semolina using modulated differential scanning calorimetry. Journal of Cereal Science 33 (2001) 213-221
    • (2001) Journal of Cereal Science , vol.33 , pp. 213-221
    • Cuq, B.1    Lcard-Vernière2
  • 8
    • 33845279681 scopus 로고
    • Refolding of thermally unfolded soy proteins during the cooling regime of the gelation process: effect on gelation
    • Damodaran S. Refolding of thermally unfolded soy proteins during the cooling regime of the gelation process: effect on gelation. Journal of Agricultural and Food Chemistry 36 (1988) 262-269
    • (1988) Journal of Agricultural and Food Chemistry , vol.36 , pp. 262-269
    • Damodaran, S.1
  • 9
    • 0032147916 scopus 로고    scopus 로고
    • Emulsifying properties of milk proteins cross-linked with microbial transglutaminase
    • Færgemand M., Otte J., and Qvist K.B. Emulsifying properties of milk proteins cross-linked with microbial transglutaminase. International Dairy Journal 8 (1998) 715-723
    • (1998) International Dairy Journal , vol.8 , pp. 715-723
    • Færgemand, M.1    Otte, J.2    Qvist, K.B.3
  • 10
    • 0037229340 scopus 로고    scopus 로고
    • Effect of cross-linking with transglutaminase on the heat stability and some functional characteristics of sodium caseinate
    • Flanagan J., Gunning Y., and FitzGerald R.J. Effect of cross-linking with transglutaminase on the heat stability and some functional characteristics of sodium caseinate. Food Research International 36 (2003) 267-274
    • (2003) Food Research International , vol.36 , pp. 267-274
    • Flanagan, J.1    Gunning, Y.2    FitzGerald, R.J.3
  • 12
    • 84981374673 scopus 로고
    • Physico-chemical aspects of soy proteins structure formation
    • Hermansson A.M. Physico-chemical aspects of soy proteins structure formation. Journal of Texture Study 9 (1978) 33-58
    • (1978) Journal of Texture Study , vol.9 , pp. 33-58
    • Hermansson, A.M.1
  • 13
    • 84985232976 scopus 로고
    • Study of thermal properties of oat globulin by differential scanning calorimetry
    • Harwalkar V.R., and Ma C.-Y. Study of thermal properties of oat globulin by differential scanning calorimetry. Journal of Food Science 52 (1987) 394-398
    • (1987) Journal of Food Science , vol.52 , pp. 394-398
    • Harwalkar, V.R.1    Ma, C.-Y.2
  • 14
    • 0000536914 scopus 로고
    • Determination of glycinin and β-conglycinin in soybean proteins by immunological methods
    • Iwabuchi S., and Yamauchi F. Determination of glycinin and β-conglycinin in soybean proteins by immunological methods. Journal of Agricultural and Food Chemistry 35 (1987) 200-205
    • (1987) Journal of Agricultural and Food Chemistry , vol.35 , pp. 200-205
    • Iwabuchi, S.1    Yamauchi, F.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0034648254 scopus 로고    scopus 로고
    • Study of glass transition of metallic glasses by temperature-modulated differential scanning calorimetry (MDSC)
    • Lu Z.P., Li Y., Ng S.C., and Feng Y.P. Study of glass transition of metallic glasses by temperature-modulated differential scanning calorimetry (MDSC). Thermochimica Acta 357-358 (2000) 65-69
    • (2000) Thermochimica Acta , vol.357-358 , pp. 65-69
    • Lu, Z.P.1    Li, Y.2    Ng, S.C.3    Feng, Y.P.4
  • 19
    • 0026729426 scopus 로고
    • Protein interactions with urea and guanidinium chloride. A calorimetric study
    • Makhatadze G.I., and Privalov P.L. Protein interactions with urea and guanidinium chloride. A calorimetric study. Journal of Molecular Biology 226 (1992) 491-505
    • (1992) Journal of Molecular Biology , vol.226 , pp. 491-505
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 20
    • 0035036512 scopus 로고    scopus 로고
    • Thermal properties of Phaseolus angularis (red bean) globulin
    • Meng G.-T., and Ma C.-Y. Thermal properties of Phaseolus angularis (red bean) globulin. Food Chemistry 23 (2001) 453-460
    • (2001) Food Chemistry , vol.23 , pp. 453-460
    • Meng, G.-T.1    Ma, C.-Y.2
  • 21
    • 0034643864 scopus 로고    scopus 로고
    • Thermal behavior of native and hydrophobized wheat gluten, gliadin and glutenin-rich fractions by modulated DSC
    • Micard V., and Guilbert S. Thermal behavior of native and hydrophobized wheat gluten, gliadin and glutenin-rich fractions by modulated DSC. International Journal of Biological Macromolecules 27 (2000) 229-236
    • (2000) International Journal of Biological Macromolecules , vol.27 , pp. 229-236
    • Micard, V.1    Guilbert, S.2
  • 22
    • 0033770706 scopus 로고    scopus 로고
    • Thermal properties of raw and processed wheat gluten in relation with protein aggregation
    • Micard V., Morel M.-H., Bonicel J., and Guilbert S. Thermal properties of raw and processed wheat gluten in relation with protein aggregation. Polymer 42 (2001) 477-485
    • (2001) Polymer , vol.42 , pp. 477-485
    • Micard, V.1    Morel, M.-H.2    Bonicel, J.3    Guilbert, S.4
  • 23
    • 0033851272 scopus 로고    scopus 로고
    • Effect of transglutaminase treatment on the glass transition of soy protein
    • Mizuno A., Mitsuiki M., and Motoki M. Effect of transglutaminase treatment on the glass transition of soy protein. Journal of Agricultural and Food Chemistry 48 (2000) 3286-3291
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 3286-3291
    • Mizuno, A.1    Mitsuiki, M.2    Motoki, M.3
  • 24
    • 0031239863 scopus 로고    scopus 로고
    • Glass transition of soy globulins using differential scanning calorimetry and mechanical spectrometry
    • Morales A., and Kokini J. Glass transition of soy globulins using differential scanning calorimetry and mechanical spectrometry. Biotechnology Progress 13 (1997) 624-629
    • (1997) Biotechnology Progress , vol.13 , pp. 624-629
    • Morales, A.1    Kokini, J.2
  • 25
    • 84954942298 scopus 로고
    • Functional properties of food proteins polymerized by transglutaminase
    • Motoki M., Nio N., and Takinami K. Functional properties of food proteins polymerized by transglutaminase. Agricultural and Food Chemistry 48 (1984) 1257-1261
    • (1984) Agricultural and Food Chemistry , vol.48 , pp. 1257-1261
    • Motoki, M.1    Nio, N.2    Takinami, K.3
  • 28
    • 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
    • 0037165563 scopus 로고    scopus 로고
    • Functional properties of oat globulin modified by a calcium-independent microbial transglutaminase
    • Siu N.-C., Ma C.-Y., Mock W.-Y., and Mine Y. Functional properties of oat globulin modified by a calcium-independent microbial transglutaminase. Journal of Agricultural and Food Chemistry 50 (2002) 2666-2672
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , pp. 2666-2672
    • Siu, N.-C.1    Ma, C.-Y.2    Mock, W.-Y.3    Mine, Y.4
  • 31
    • 24144467835 scopus 로고    scopus 로고
    • Physicochemical and structural properties of sodium caseinate biopolymers induced by microbial transglutaminase
    • Tang C.H., Yang X.Q., Chen Z., Wu H., and Peng Z.Y. Physicochemical and structural properties of sodium caseinate biopolymers induced by microbial transglutaminase. Journal of Food Biochemistry 29 (2005) 402-421
    • (2005) Journal of Food Biochemistry , vol.29 , pp. 402-421
    • Tang, C.H.1    Yang, X.Q.2    Chen, Z.3    Wu, H.4    Peng, Z.Y.5
  • 32
    • 33645137009 scopus 로고    scopus 로고
    • Coagulation and gelation of native soy protein isolates induced by microbial transglutaminase
    • Tang C.H., Wu H., Yu H.P., Lin L., Chen Z., and Yang X.Q. Coagulation and gelation of native soy protein isolates induced by microbial transglutaminase. Journal of Food Biochemistry 30 (2006) 35-55
    • (2006) Journal of Food Biochemistry , vol.30 , pp. 35-55
    • Tang, C.H.1    Wu, H.2    Yu, H.P.3    Lin, L.4    Chen, Z.5    Yang, X.Q.6
  • 34
    • 0037058957 scopus 로고    scopus 로고
    • Relationships between the temperature dependence of solvent denaturation and the denaturant dependence of protein stability curves
    • Zweifel M.E., and Barrick D. Relationships between the temperature dependence of solvent denaturation and the denaturant dependence of protein stability curves. Biophysical Chemistry 101/102 (2002) 221-237
    • (2002) Biophysical Chemistry , vol.101-102 , pp. 221-237
    • Zweifel, M.E.1    Barrick, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.