메뉴 건너뛰기




Volumn 17, Issue 3, 2003, Pages 365-377

Gelation of soy glycinin; influence of pH and ionic strength on network structure in relation to protein conformation

Author keywords

Gel; Glycinin; Heat denaturation; Ionic strength; Network; pH; Soy

Indexed keywords

DENATURATION; GELATION; GELS; INFRARED IMAGING; PROTEINS; STIFFNESS;

EID: 0038286512     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0268-005X(02)00100-5     Document Type: Article
Times cited : (86)

References (40)
  • 1
    • 0026507761 scopus 로고
    • Amide modes and protein conformation
    • Bandekar, J. (1992). Amide modes and protein conformation. Biochimica et Biophysica Acta, 1120, 123-143.
    • (1992) Biochimica et Biophysica Acta , vol.1120 , pp. 123-143
    • Bandekar, J.1
  • 2
    • 0001282434 scopus 로고
    • Steric exclusion of serum proteins with respect to (para) casein micelles
    • van Boekel, M. A. J. S., & Walstra, P. (1989). Steric exclusion of serum proteins with respect to (para) casein micelles. Neth. Milk Dairy, 43, 437-446.
    • (1989) Neth. Milk Dairy , vol.43 , pp. 437-446
    • Van Boekel, M.A.J.S.1    Walstra, P.2
  • 3
    • 0030088058 scopus 로고    scopus 로고
    • Effects of physicochemical factors on the secondary structure of β-lactoglobulin
    • Boye, J. I., Ashraf, A. I., & Alli, I. (1996). Effects of physicochemical factors on the secondary structure of β-lactoglobulin. Journal of Dairy Research, 63, 97-109.
    • (1996) Journal of Dairy Research , vol.63 , pp. 97-109
    • Boye, J.I.1    Ashraf, A.I.2    Alli, I.3
  • 5
    • 84985733652 scopus 로고
    • 1H-NMR parameters of the common amino-acid measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • 1H-NMR parameters of the common amino-acid measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers, 18, 285-297.
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wütrich, K.2
  • 7
    • 0000242070 scopus 로고
    • Structure of glycinin and ovalbumin gels
    • Doi, E., & Kitabatake, N. (1989). Structure of glycinin and ovalbumin gels. Food Hydrocolloids, 3, 327-337.
    • (1989) Food Hydrocolloids , vol.3 , pp. 327-337
    • Doi, E.1    Kitabatake, N.2
  • 8
    • 0028709475 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy III. Secondary structures
    • H. J. Hilderson, & G. B. Ralston (Eds.). New York: Plenum Press
    • Goormaghtigh, E., Cabiaux, V., & Ruysschaert, J. M. (1994). Determination of soluble and membrane protein structure by Fourier Transform Infrared Spectroscopy III. Secondary structures. In H. J. Hilderson, & G. B. Ralston (Eds.), Subcellular biochemistry; physicochemical methods in the study of biomembranes (pp. 405-450). New York: Plenum Press.
    • (1994) Subcellular Biochemistry; Physicochemical Methods in the Study of Biomembranes , pp. 405-450
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 9
    • 0024564561 scopus 로고
    • Fourier transform IR spectroscopic investigation of rhodopsin structure and its comparison with bacteriorhodopsin
    • Haris, P. I., Coke, M., & Chapman, D. (1989). Fourier transform IR spectroscopic investigation of rhodopsin structure and its comparison with bacteriorhodopsin. Biochimica et Biophysica Acta, 995, 160-167.
    • (1989) Biochimica et Biophysica Acta , vol.995 , pp. 160-167
    • Haris, P.I.1    Coke, M.2    Chapman, D.3
  • 12
    • 0025092697 scopus 로고
    • The conformational changes of apocytochrome c upon binding to phospholipid vesicles and micelles of phospholipid based detergents: A circular dichroism study
    • de Jongh, H. H. J., & de Kruijff, B. (1990). The conformational changes of apocytochrome c upon binding to phospholipid vesicles and micelles of phospholipid based detergents: a circular dichroism study. Biochimica et Biophysica Acta, 1029, 105-112.
    • (1990) Biochimica et Biophysica Acta , vol.1029 , pp. 105-112
    • De Jongh, H.H.J.1    De Kruijff, B.2
  • 13
    • 0001073976 scopus 로고
    • Relationships of secondary structure, microstructure, and mechanical properties of heat induced gel of soy 11S globulin
    • Ker, Y.-C., Chen, R.-H., & Wu, C.-S. (1993). Relationships of secondary structure, microstructure, and mechanical properties of heat induced gel of soy 11S globulin. Bioscience, Biotechnology, and Biochemistry, 57, 536-541.
    • (1993) Bioscience, Biotechnology, and Biochemistry , vol.57 , pp. 536-541
    • Ker, Y.-C.1    Chen, R.-H.2    Wu, C.-S.3
  • 14
    • 0022616364 scopus 로고
    • Thermally induced protein gelation: Gelation and rheological characterization of highly concentrated ovalbumin and soybean protein gels
    • van Kleef, F. S. M. (1986). Thermally induced protein gelation: gelation and rheological characterization of highly concentrated ovalbumin and soybean protein gels. Biopolymers, 25, 31-59.
    • (1986) Biopolymers , vol.25 , pp. 31-59
    • Van Kleef, F.S.M.1
  • 17
    • 85025567869 scopus 로고
    • Fine-stranded and particulate gels of beta-lactoglobulin and whey protein at varying pH
    • Langton, M., & Hermansson, A. M. (1992). Fine-stranded and particulate gels of beta-lactoglobulin and whey protein at varying pH. Food Hydrocolloids, 5, 523-539.
    • (1992) Food Hydrocolloids , vol.5 , pp. 523-539
    • Langton, M.1    Hermansson, A.M.2
  • 19
    • 84981467177 scopus 로고
    • Rheological properties of heat-induced gel of soybean 11S globulin under high ionic strength (μ = 0.5)
    • Mori, T., Mohri, M., Artik, N., & Matsumura, Y. (1989). Rheological properties of heat-induced gel of soybean 11S globulin under high ionic strength (μ = 0.5). Journal of Texture Studies, 19, 361-371.
    • (1989) Journal of Texture Studies , vol.19 , pp. 361-371
    • Mori, T.1    Mohri, M.2    Artik, N.3    Matsumura, Y.4
  • 20
    • 84985180960 scopus 로고
    • Gelation mechanism of soybean 11S globulin: Formation of soluble aggregates as transient intermediates
    • Mori, T., Nakamura, T., & Utsumi, S. (1981). Gelation mechanism of soybean 11S globulin: formation of soluble aggregates as transient intermediates. Journal of Food Science, 47, 26-30.
    • (1981) Journal of Food Science , vol.47 , pp. 26-30
    • Mori, T.1    Nakamura, T.2    Utsumi, S.3
  • 21
    • 0001989848 scopus 로고
    • Behavior of intermolecular bond formation in the late stage of heat-induced gelation of glycinin
    • Mori, T., Nakamura, T., & Utsumi, S. (1986). Behavior of intermolecular bond formation in the late stage of heat-induced gelation of glycinin. Journal of Agricultural and Food Chemistry, 34, 33-36.
    • (1986) Journal of Agricultural and Food Chemistry , vol.34 , pp. 33-36
    • Mori, T.1    Nakamura, T.2    Utsumi, S.3
  • 22
    • 85015824436 scopus 로고
    • Study on the heat-induced conformational changes of β-conglycinin by FTIR and CD analysis
    • Nagano, T., Akasaka, T., & Nishinari, K. (1995). Study on the heat-induced conformational changes of β-conglycinin by FTIR and CD analysis. Food Hydrocolloids, 9, 83-89.
    • (1995) Food Hydrocolloids , vol.9 , pp. 83-89
    • Nagano, T.1    Akasaka, T.2    Nishinari, K.3
  • 24
    • 0001743026 scopus 로고
    • Effects of temperature on the different stages in thermal gelling of glycinin
    • Nakamura, T., Utsumi, S., & Mori, T. (1985). Effects of temperature on the different stages in thermal gelling of glycinin. Journal of Agricultural and Food Chemistry, 33, 1201-1203.
    • (1985) Journal of Agricultural and Food Chemistry , vol.33 , pp. 1201-1203
    • Nakamura, T.1    Utsumi, S.2    Mori, T.3
  • 25
    • 0001565172 scopus 로고    scopus 로고
    • Structural properties of heat-induced soy protein gels as affected by ionic strength and pH
    • Puppo, M. C., & Añón, M. C. (1998). Structural properties of heat-induced soy protein gels as affected by ionic strength and pH. Journal of Agricultural and Food Chemistry, 46, 3583-3589.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 3583-3589
    • Puppo, M.C.1    Añón, M.C.2
  • 26
    • 85025567202 scopus 로고
    • Large deformation properties of β-lactoglobulin gel structures
    • Stading, M., & Hermansson, A. M. (1991). Large deformation properties of β-lactoglobulin gel structures. Food Hydrocolloids, 5, 339-352.
    • (1991) Food Hydrocolloids , vol.5 , pp. 339-352
    • Stading, M.1    Hermansson, A.M.2
  • 27
    • 85025563484 scopus 로고
    • Microstructure and rheological behaviour of particulate beta-lactoglobulin gels
    • Stading, M., Langton, M., & Hermansson, A. M. (1993). Microstructure and rheological behaviour of particulate beta-lactoglobulin gels. Food Hydrocolloids, 7, 195-212.
    • (1993) Food Hydrocolloids , vol.7 , pp. 195-212
    • Stading, M.1    Langton, M.2    Hermansson, A.M.3
  • 28
  • 29
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • Surewicz, W. K., & Mantsch, H. H. (1988). New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochimica et Biophysica Acta, 952, 115-130.
    • (1988) Biochimica et Biophysica Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 31
    • 0017019007 scopus 로고
    • Major proteins of soybean seeds. A straightforward fractionation and their characterization
    • Thanh, V. H., & Shibasaki, K. (1976). Major proteins of soybean seeds. A straightforward fractionation and their characterization. Journal of Agricultural and Food Chemistry, 24, 1117-1121.
    • (1976) Journal of Agricultural and Food Chemistry , vol.24 , pp. 1117-1121
    • Thanh, V.H.1    Shibasaki, K.2
  • 33
    • 0019888343 scopus 로고
    • Purification and characterisation of mRNA from soybean seeds
    • Tumer, N. E., Thanh, V. H., & Nielsen, N. C. (1981). Purification and characterisation of mRNA from soybean seeds. Journal of Biological Chemistry, 256, 8756-8760.
    • (1981) Journal of Biological Chemistry , vol.256 , pp. 8756-8760
    • Tumer, N.E.1    Thanh, V.H.2    Nielsen, N.C.3
  • 34
    • 0006278588 scopus 로고
    • Effects of deletion of disulfide bonds by protein engineering on the conformation and functional properties of soybean proglycinin
    • Utsumi, S., Gidamis, A. B., Kanamori, J., Kang, I. J., & Kito, M. (1993). Effects of deletion of disulfide bonds by protein engineering on the conformation and functional properties of soybean proglycinin. Journal of Agricultural and Food Chemistry, 41, 687-691.
    • (1993) Journal of Agricultural and Food Chemistry , vol.41 , pp. 687-691
    • Utsumi, S.1    Gidamis, A.B.2    Kanamori, J.3    Kang, I.J.4    Kito, M.5
  • 35
    • 84987318401 scopus 로고
    • Forces involved in soy protein gelation: Effects of various reagents on the formation, hardness and solubility of heat-induced gels made from 7S, 11S, and soy isolate
    • Utsumi, S., & Kinsella, J. E. (1985a). Forces involved in soy protein gelation: effects of various reagents on the formation, hardness and solubility of heat-induced gels made from 7S, 11S, and soy isolate. Journal of Food Science, 50, 1278-1282.
    • (1985) Journal of Food Science , vol.50 , pp. 1278-1282
    • Utsumi, S.1    Kinsella, J.E.2
  • 36
    • 0000810637 scopus 로고
    • Structure-function relationships in food proteins: Subunit interactions in heat-induced gelation of 7S 11S, and soy isolate proteins
    • Utsumi, S., & Kinsella, J. E. (1985b). Structure-function relationships in food proteins: subunit interactions in heat-induced gelation of 7S 11S, and soy isolate proteins. Journal of Agricultural and Food Chemistry, 33, 297-303.
    • (1985) Journal of Agricultural and Food Chemistry , vol.33 , pp. 297-303
    • Utsumi, S.1    Kinsella, J.E.2
  • 37
    • 0001784413 scopus 로고    scopus 로고
    • Structure and rheology of gels formed by aggregated protein particles
    • K. Nishinari (Ed.). Amsterdam: Elsevier
    • van Vliet, T. (2000). Structure and rheology of gels formed by aggregated protein particles. In K. Nishinari (Ed.), Hydrocolloids-part 1 (pp. 367-377). Amsterdam: Elsevier.
    • (2000) Hydrocolloids-Part 1 , pp. 367-377
    • Van Vliet, T.1
  • 38
    • 0007674510 scopus 로고    scopus 로고
    • Structure of whey protein gels, studied by permeability, scanning electron microscopy and rheology
    • Verheul, M., & Roefs, S. (1998). Structure of whey protein gels, studied by permeability, scanning electron microscopy and rheology. Food Hydrocolloids, 12, 17-24.
    • (1998) Food Hydrocolloids , vol.12 , pp. 17-24
    • Verheul, M.1    Roefs, S.2
  • 39
    • 0027527209 scopus 로고
    • Characterization of the contribution of aromatic side chains
    • Vuilleumier, S., Sancho, J., Loewenthal, R., & Fersht, A. R. (1993). Characterization of the contribution of aromatic side chains. Biochemistry, 32, 10303-10313.
    • (1993) Biochemistry , vol.32 , pp. 10303-10313
    • Vuilleumier, S.1    Sancho, J.2    Loewenthal, R.3    Fersht, A.R.4
  • 40
    • 0000293117 scopus 로고
    • Covalent polymerization of acidic subunits on heat-induced gelation of soybean glycinin
    • Yamagishi, T., Takahashi, N., & Yamauchi, F. (1987). Covalent polymerization of acidic subunits on heat-induced gelation of soybean glycinin. Cereal Chemistry, 64, 207-212.
    • (1987) Cereal Chemistry , vol.64 , pp. 207-212
    • Yamagishi, T.1    Takahashi, N.2    Yamauchi, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.