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Volumn 43, Issue 2, 2004, Pages 184-195

Rheology and microstructure of heat-induced egg yolk gels

Author keywords

Differential scanning calorimetry; Egg yolk gelation; Electron microscopy; Gel point; Small amplitude oscillatory shear

Indexed keywords

CALORIMETRY; ELECTRON MICROSCOPY; GELATION; MICROSTRUCTURE; RHEOLOGY;

EID: 2342438817     PISSN: 00354511     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00397-003-0338-3     Document Type: Article
Times cited : (89)

References (73)
  • 2
    • 2242461391 scopus 로고    scopus 로고
    • Experimental evidence for a two-step process in the aggregation of β-lactoglobulin at pH 7
    • Aymard P, Gimel JC, Nicolai T, Durand D (1996) Experimental evidence for a two-step process in the aggregation of β-lactoglobulin at pH 7. J Chim Phys 93:987-997
    • (1996) J Chim Phys , vol.93 , pp. 987-997
    • Aymard, P.1    Gimel, J.C.2    Nicolai, T.3    Durand, D.4
  • 3
    • 0033898830 scopus 로고    scopus 로고
    • Characterization and isolation of intermediates in b-lactoglobulin heat aggregation at high pH
    • Bauer R, Carrotta R, Rischell C, Ogendal L (2000) Characterization and isolation of intermediates in b-lactoglobulin heat aggregation at high pH. Biophys J 79:1030-1038
    • (2000) Biophys J , vol.79 , pp. 1030-1038
    • Bauer, R.1    Carrotta, R.2    Rischell, C.3    Ogendal, L.4
  • 4
    • 0029739584 scopus 로고    scopus 로고
    • Glass transition temperatures determined using a temperature-cycling differential scanning calorimeter
    • Bell LN, Touma DE (1996) Glass transition temperatures determined using a temperature-cycling differential scanning calorimeter. J Food Sci 61:807-810, 828
    • (1996) J Food Sci , vol.61 , Issue.807-810 , pp. 828
    • Bell, L.N.1    Touma, D.E.2
  • 5
    • 0000537572 scopus 로고    scopus 로고
    • Thermal denaturation of β-lactoglobulin a 1H-NMR study
    • Belloque J, Smith GM (1998) Thermal denaturation of β-lactoglobulin. a 1H-NMR study. J Agric Food Chem 46:1805-1813
    • (1998) J Agric Food Chem , vol.46 , pp. 1805-1813
    • Belloque, J.1    Smith, G.M.2
  • 6
    • 0030829061 scopus 로고    scopus 로고
    • In situ Investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy
    • Bourauoi M, Nakai S, Li-Chan E (1997) In situ Investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy. Food Res Int 30:65-72
    • (1997) Food Res Int , vol.30 , pp. 65-72
    • Bourauoi, M.1    Nakai, S.2    Li-Chan, E.3
  • 7
    • 0642302370 scopus 로고    scopus 로고
    • Molecular and microstructural studies of thermal denaturation and gelation of β-lactoglobulins, A and B
    • Boye JI, Ma CY, Ismail A, Harwalkar VR, Kalab M (1997) Molecular and microstructural studies of thermal denaturation and gelation of β-lactoglobulins, A and B. J Agric Food Chem 45:1608-1618
    • (1997) J Agric Food Chem , vol.45 , pp. 1608-1618
    • Boye, J.I.1    Ma, C.Y.2    Ismail, A.3    Harwalkar, V.R.4    Kalab, M.5
  • 8
    • 0000154785 scopus 로고
    • Isolation and composition of avian egg yolk granules and their constituent α- and β-lipovitellins
    • Burley RW, Cook WH (1961) Isolation and composition of avian egg yolk granules and their constituent α- and β-lipovitellins. Can J Biochem Physiol 39:1295-1307
    • (1961) Can J Biochem Physiol , vol.39 , pp. 1295-1307
    • Burley, R.W.1    Cook, W.H.2
  • 9
    • 0031570657 scopus 로고    scopus 로고
    • Study of the gelation process of polyethylene oxide-polypropylene oxide copolymer (Poloxamer 407) aqueous solutions
    • Cabana A, Aït-Kadi A, Juhász J (1997) Study of the gelation process of polyethylene oxide-polypropylene oxide copolymer (Poloxamer 407) aqueous solutions. J Colloid Interface Sci 190:307-312
    • (1997) J Colloid Interface Sci , vol.190 , pp. 307-312
    • Cabana, A.1    Aït-Kadi, A.2    Juhász, J.3
  • 10
    • 3743076841 scopus 로고
    • Linear viscoelasticity at the gel point of a crosslinking PDMS with imbalanced stoichiometry
    • Chambon F, Winter HH (1987) Linear viscoelasticity at the gel point of a crosslinking PDMS with imbalanced stoichiometry. J Rheol 31:683-697
    • (1987) J Rheol , vol.31 , pp. 683-697
    • Chambon, F.1    Winter, H.H.2
  • 12
    • 0002112253 scopus 로고    scopus 로고
    • Hill SE, Ledward DA, Mitchell JR (eds) Aspen Publishers, Gaithersburg
    • Clark AH (1998) In: Hill SE, Ledward DA, Mitchell JR (eds) Functional properties of food macromolecules. Aspen Publishers, Gaithersburg, pp 77-142
    • (1998) Functional Properties of Food Macromolecules , pp. 77-142
    • Clark, A.H.1
  • 14
    • 0019536747 scopus 로고
    • Infrared and laser-Raman spectroscopic studies of thermally-induced globular proteins
    • Clark AH, Saunderson DHP, Suggett A (1981a) Infrared and laser-Raman spectroscopic studies of thermally-induced globular proteins. Int J Peptide Protein Res 17:353-364
    • (1981) Int J Peptide Protein Res , vol.17 , pp. 353-364
    • Clark, A.H.1    Saunderson, D.H.P.2    Suggett, A.3
  • 17
    • 0033691549 scopus 로고    scopus 로고
    • Dynamical mechanical properties of gelling colloidal disks
    • Cocard S, Tassin JF, Nicolai T (2000) Dynamical mechanical properties of gelling colloidal disks. J Rheol 44:585-594
    • (2000) J Rheol , vol.44 , pp. 585-594
    • Cocard, S.1    Tassin, J.F.2    Nicolai, T.3
  • 18
    • 0002503849 scopus 로고    scopus 로고
    • Damodaran S, Paraf A (eds) Marcel Dekker, New York
    • Damodaran S (1997) In: Damodaran S, Paraf A (eds) Food proteins and their applications. Marcel Dekker, New York, pp 1-24
    • (1997) Food Proteins and Their Applications , pp. 1-24
    • Damodaran, S.1
  • 20
    • 0033066634 scopus 로고    scopus 로고
    • Thermal properties of corn gluten meal and its proteic components
    • Di Gioia L, Cuq B, Guilbert S (1999) Thermal properties of corn gluten meal and its proteic components. Int J Biological Macromol 24:341-350
    • (1999) Int J Biological Macromol , vol.24 , pp. 341-350
    • Di Gioia, L.1    Cuq, B.2    Guilbert, S.3
  • 21
    • 38749112076 scopus 로고
    • Gels and gelling of globular proteins
    • Doi E (1993) Gels and gelling of globular proteins. Trends Food Sci Technol 4:1-5
    • (1993) Trends Food Sci Technol , vol.4 , pp. 1-5
    • Doi, E.1
  • 22
    • 0016419640 scopus 로고
    • A differential scanning calorimetric study of the stability of egg white to heat denaturation
    • Donovan JW, Mapes CJ, Davis JG, Garibaldi JA (1975) A differential scanning calorimetric study of the stability of egg white to heat denaturation. J Sci Food Agric 26:73-83
    • (1975) J Sci Food Agric , vol.26 , pp. 73-83
    • Donovan, J.W.1    Mapes, C.J.2    Davis, J.G.3    Garibaldi, J.A.4
  • 24
    • 84985370806 scopus 로고
    • Dynamic rheological measurements on heat-induced myosin gels: An evaluation of the method's suitability for the filamentous gels
    • Egelandsdal B, Fretheim K, Harbirt O (1986) Dynamic rheological measurements on heat-induced myosin gels: an evaluation of the method's suitability for the filamentous gels. J Sci Food Agric 37:944-954
    • (1986) J Sci Food Agric , vol.37 , pp. 944-954
    • Egelandsdal, B.1    Fretheim, K.2    Harbirt, O.3
  • 25
    • 0001196421 scopus 로고    scopus 로고
    • Pressure/heat combinations on pork meat batters: Protein thermal behavior and product rheological properties
    • Fernández-Martín F, Fernández P, Carballo J, Jiménez Colmenero F (1997) Pressure/heat combinations on pork meat batters: protein thermal behavior and product rheological properties. J Agr Food Chem 45:4440-4445
    • (1997) J Agr Food Chem , vol.45 , pp. 4440-4445
    • Fernández-Martín, F.1    Fernández, P.2    Carballo, J.3    Jiménez Colmenero, F.4
  • 28
    • 0034215958 scopus 로고    scopus 로고
    • Viscoelasticity of thermoreversible gelatin gets from mammalian and piscine collagens
    • Gilsenan PM, Ross-Murphy SB (2000) Viscoelasticity of thermoreversible gelatin gets from mammalian and piscine collagens. J Rheol 44:871-883
    • (2000) J Rheol , vol.44 , pp. 871-883
    • Gilsenan, P.M.1    Ross-Murphy, S.B.2
  • 29
    • 0028195932 scopus 로고
    • Structure and distribution of aggregates formed after heat-induced denaturation of globular-proteins
    • Gimel JC, Durand D, Nicolai T (1994) Structure and distribution of aggregates formed after heat-induced denaturation of globular-proteins. Macromolecules 257:583-589
    • (1994) Macromolecules , vol.257 , pp. 583-589
    • Gimel, J.C.1    Durand, D.2    Nicolai, T.3
  • 30
    • 85011297585 scopus 로고
    • Influence of frozen storage time on properties of salted yolk and its functionality in mayonnaise
    • Harrison LJ, Cunningham FE (1986) Influence of frozen storage time on properties of salted yolk and its functionality in mayonnaise. J Food Quality 9:167-174
    • (1986) J Food Quality , vol.9 , pp. 167-174
    • Harrison, L.J.1    Cunningham, F.E.2
  • 31
    • 0001243741 scopus 로고
    • Turbidity and hardness of a heat-induced gel of hen egg ovoalbumin
    • Hatta H, Kitabatake N. Doi E (1986) Turbidity and hardness of a heat-induced gel of hen egg ovoalbumin. Agric Biol Chem 50:2083-2089
    • (1986) Agric Biol Chem , vol.50 , pp. 2083-2089
    • Hatta, H.1    Kitabatake, N.2    Doi, E.3
  • 32
    • 84986533267 scopus 로고
    • Conditions for the formation of heat-induced gels of some globular food proteins
    • Hegg P(1982) Conditions for the formation of heat-induced gels of some globular food proteins. J Food Sci 47:1241-1244
    • (1982) J Food Sci , vol.47 , pp. 1241-1244
    • Hegg, P.1
  • 33
    • 0032981978 scopus 로고    scopus 로고
    • Rheological studies on gelling behavior of soy protein isolates
    • Hsu S (1999) Rheological studies on gelling behavior of soy protein isolates. J Food Sci 64:136-140
    • (1999) J Food Sci , vol.64 , pp. 136-140
    • Hsu, S.1
  • 34
    • 0034091868 scopus 로고    scopus 로고
    • Viscoelastic changes of rice starch suspensions during gelatinization
    • Hsu S, Lu S, Huang C (2000) Viscoelastic changes of rice starch suspensions during gelatinization. J Food Sci 65:215-220
    • (2000) J Food Sci , vol.65 , pp. 215-220
    • Hsu, S.1    Lu, S.2    Huang, C.3
  • 35
    • 0034318911 scopus 로고    scopus 로고
    • Heat-induced gelation of globular proteins. 4. Gelation kinetics of low pH β-lactoglobulin gels
    • Kavanagh GM, Clark AH, Ross-Murphy SB (2000) Heat-induced gelation of globular proteins. 4. Gelation kinetics of low pH β-lactoglobulin gels. Langmuir 16:9584-9594
    • (2000) Langmuir , vol.16 , pp. 9584-9594
    • Kavanagh, G.M.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 36
    • 84963187703 scopus 로고
    • Functional properties of proteins in foods: A survey
    • Kinsella JE (1976) Functional properties of proteins in foods: a survey. CRC Crit Rev Food Sci Nutr 7:219-280
    • (1976) CRC Crit Rev Food Sci Nutr , vol.7 , pp. 219-280
    • Kinsella, J.E.1
  • 37
    • 0020766679 scopus 로고
    • The influence of egg yolk lipoproteins on the rheology and stability of O/W emulsions and mayonnaise
    • Kiosseoglou VD, Sherman P (1983) The influence of egg yolk lipoproteins on the rheology and stability of O/W emulsions and mayonnaise. Colloid Polym Sci 261:502-507
    • (1983) Colloid Polym Sci , vol.261 , pp. 502-507
    • Kiosseoglou, V.D.1    Sherman, P.2
  • 39
    • 85025567869 scopus 로고
    • Fine-stranded and particulate gels of β-lactoglobulin and whey-protein at varying pH
    • Langton M, Hermansson AM (1992) Fine-stranded and particulate gels of β-lactoglobulin and whey-protein at varying pH. Food Hydrocolloid 5:523-539
    • (1992) Food Hydrocolloid , vol.5 , pp. 523-539
    • Langton, M.1    Hermansson, A.M.2
  • 40
    • 0001029710 scopus 로고    scopus 로고
    • Growth and structure of aggregates of heat-denatured β-lactoglobulin
    • Le Bon C, Nicolai T, Durand D (1999a) Growth and structure of aggregates of heat-denatured β-lactoglobulin. Int J Food Sci Technol 34:451-465
    • (1999) Int J Food Sci Technol , vol.34 , pp. 451-465
    • Le Bon, C.1    Nicolai, T.2    Durand, D.3
  • 41
    • 0342374989 scopus 로고    scopus 로고
    • Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation
    • Le Bon C, Nicolai T, Durand D (1999b) Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation. Macromolecules 32:6120-6127
    • (1999) Macromolecules , vol.32 , pp. 6120-6127
    • Le Bon, C.1    Nicolai, T.2    Durand, D.3
  • 42
    • 0000508270 scopus 로고
    • Fractionation and characterization of the low-density lipoproteins of hen's egg yolk
    • Martin WG, Augustyniak J, Cook W H (1964) Fractionation and characterization of the low-density lipoproteins of hen's egg yolk. Biochim Biophys Acta 84:714-720
    • (1964) Biochim Biophys Acta , vol.84 , pp. 714-720
    • Martin, W.G.1    Augustyniak, J.2    Cook, W.H.3
  • 43
    • 0001656218 scopus 로고
    • Paper electrophoresis characterization of proteins and lipoproteins of hen's yolk
    • McCully KA, Mok CC, Common RH (1962) Paper electrophoresis characterization of proteins and lipoproteins of hen's yolk, Can J Biochem Physiol 40:937-952
    • (1962) Can J Biochem Physiol , vol.40 , pp. 937-952
    • McCully, K.A.1    Mok, C.C.2    Common, R.H.3
  • 44
    • 0000511699 scopus 로고
    • Concentration dependence of the critical viscoelastic properties of gelatin at the gel point
    • Michon C, Cuvelier G, Launay B (1993) Concentration dependence of the critical viscoelastic properties of gelatin at the gel point. Rheol Acta 32:94-103
    • (1993) Rheol Acta , vol.32 , pp. 94-103
    • Michon, C.1    Cuvelier, G.2    Launay, B.3
  • 45
    • 0036474057 scopus 로고    scopus 로고
    • Rheological characterization of egg yolk processed by spray-drying and lipid-cholesterol extraction with CO2
    • Miranda J, Cordobés F, Partal P, Guerrero A (2002) Rheological characterization of egg yolk processed by spray-drying and lipid-cholesterol extraction with CO2. J Am Oil Chem Soc 79:183-190
    • (2002) J Am Oil Chem Soc , vol.79 , pp. 183-190
    • Miranda, J.1    Cordobés, F.2    Partal, P.3    Guerrero, A.4
  • 47
    • 0035881706 scopus 로고    scopus 로고
    • Light scattering study of turbid heat-set globular protein gels using cross-correlation dynamic light scattering
    • Nicolai T, Urban C, Schurtenberger P (2001) Light scattering study of turbid heat-set globular protein gels using cross-correlation dynamic light scattering. J Colloid Interface Sci 240:419-424
    • (2001) J Colloid Interface Sci , vol.240 , pp. 419-424
    • Nicolai, T.1    Urban, C.2    Schurtenberger, P.3
  • 48
    • 0000780882 scopus 로고    scopus 로고
    • Rheological and DSC study of sol-gel transition in aqueous dispersions of industrially important polymers and colloids
    • Nishinari K (1997) Rheological and DSC study of sol-gel transition in aqueous dispersions of industrially important polymers and colloids. Colloid Polym Sci 275:1093-1107
    • (1997) Colloid Polym Sci , vol.275 , pp. 1093-1107
    • Nishinari, K.1
  • 49
    • 0002217546 scopus 로고
    • Egg quality - Current problems and recent advances
    • Well RG, Belyavin CG (eds) Series 20. Butterworths, London
    • Noble RC (1987) In: Well RG, Belyavin CG (eds) Egg quality-current problems and recent advances. Poultry Science Symposium Series 20. Butterworths, London, pp 159-191
    • (1987) Poultry Science Symposium , pp. 159-191
    • Noble, R.C.1
  • 52
    • 0001565172 scopus 로고    scopus 로고
    • Structural properties of heat-induced soy protein gels as affected by ionic strength and pH
    • Puppo MC, Anon MC (1998) Structural properties of heat-induced soy protein gels as affected by ionic strength and pH. J Agric Food Chem 46:3583-3589
    • (1998) J Agric Food Chem , vol.46 , pp. 3583-3589
    • Puppo, M.C.1    Anon, M.C.2
  • 53
    • 0345320385 scopus 로고    scopus 로고
    • Soybean protein dispersions at acid pH. Thermal and rheological properties
    • Puppo MC, Anon MC (1999) Soybean protein dispersions at acid pH. Thermal and rheological properties. J Food Sci 64:50-56
    • (1999) J Food Sci , vol.64 , pp. 50-56
    • Puppo, M.C.1    Anon, M.C.2
  • 54
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of β-lactglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis
    • Qi XL, Holt C, McNulty D, Clarke DT, Brownlow S, Jones GR (1997) Effect of temperature on the secondary structure of β-lactglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochem J 324:341-346
    • (1997) Biochem J , vol.324 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    McNulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 55
    • 0032022340 scopus 로고    scopus 로고
    • Gelation behavior of concentrated locust bean gum solutions
    • Richardson, PH Norton IT (1998) Gelation behavior of concentrated locust bean gum solutions. Macromol 31:1575-1583
    • (1998) Macromol , vol.31 , pp. 1575-1583
    • Richardson, P.H.1    Norton, I.T.2
  • 56
    • 0001001105 scopus 로고
    • Mechanical properties of globular protein gels. I. Incipient gelation behaviour
    • Richardson RK, Ross-Murphy SB (1981) Mechanical properties of globular protein gels. I. Incipient gelation behaviour. Int J Biol Macromol 3:315-322
    • (1981) Int J Biol Macromol , vol.3 , pp. 315-322
    • Richardson, R.K.1    Ross-Murphy, S.B.2
  • 57
    • 0000710517 scopus 로고
    • Incipient behaviour of gelatin gels
    • Ross-Murphy SB (1991) Incipient behaviour of gelatin gels. Rheol Acta 30:401-411
    • (1991) Rheol Acta , vol.30 , pp. 401-411
    • Ross-Murphy, S.B.1
  • 58
    • 0642332201 scopus 로고    scopus 로고
    • Gelation of sunflower globulin hydrolysates: Rheological and calorimetric studies
    • Sánchez C, Burgos J (1997) Gelation of sunflower globulin hydrolysates: rheological and calorimetric studies. J Agric Food Chem 45:2407-2412
    • (1997) J Agric Food Chem , vol.45 , pp. 2407-2412
    • Sánchez, C.1    Burgos, J.2
  • 59
    • 0026418469 scopus 로고
    • Composition dependence of the viscoelasticity of end-linked poly(dimethylsiloxane) at the gel point
    • Scanlan JC, Winter HH (1991) Composition dependence of the viscoelasticity of end-linked poly(dimethylsiloxane) at the gel point. Macromolecules 24:47-54
    • (1991) Macromolecules , vol.24 , pp. 47-54
    • Scanlan, J.C.1    Winter, H.H.2
  • 60
    • 0035399088 scopus 로고    scopus 로고
    • Thermoreversible gelation in aqueous dispersions of colloidal particles bearing grafted PEO chains
    • Shay JS, Raghavan SR, Khan SA (2001) Thermoreversible gelation in aqueous dispersions of colloidal particles bearing grafted PEO chains. J Rheol 45:913-927
    • (2001) J Rheol , vol.45 , pp. 913-927
    • Shay, J.S.1    Raghavan, S.R.2    Khan, S.A.3
  • 63
    • 0000845195 scopus 로고
    • Small and large deformation studies of protein gels
    • Standing M, Langton M, Hermansson AM (1995) Small and large deformation studies of protein gels. J Rheol 39:1445-1450
    • (1995) J Rheol , vol.39 , pp. 1445-1450
    • Standing, M.1    Langton, M.2    Hermansson, A.M.3
  • 65
    • 0019563671 scopus 로고
    • Investigation into the aging process in gels of gelatin/water systems by the measurements of their dynamic moduli. I. Phenomenology
    • Te Nijenhuis K (1981) Investigation into the aging process in gels of gelatin/water systems by the measurements of their dynamic moduli. I. Phenomenology. Colloid Polym Sci 259:522-535
    • (1981) Colloid Polym Sci , vol.259 , pp. 522-535
    • Te Nijenhuis, K.1
  • 66
    • 0024302907 scopus 로고
    • Mechanical properties at the gel point of a crystallizing poly(vinylchloride) solution
    • Te Nijenhuis K, Winter HH (1989) Mechanical properties at the gel point of a crystallizing poly(vinylchloride) solution. Macromolecules 22:411-414
    • (1989) Macromolecules , vol.22 , pp. 411-414
    • Te Nijenhuis, K.1    Winter, H.H.2
  • 67
    • 0031212243 scopus 로고    scopus 로고
    • Heat-induced gelation of globular proteins. 1. Model for the effects of time and temperature on the gelation time of BSA gels
    • Tobitany A, Ross-Murphy SB (1997) Heat-induced gelation of globular proteins. 1. Model for the effects of time and temperature on the gelation time of BSA gels. Macromolecules 30:4845-4854
    • (1997) Macromolecules , vol.30 , pp. 4845-4854
    • Tobitany, A.1    Ross-Murphy, S.B.2
  • 69
    • 0000289106 scopus 로고    scopus 로고
    • Structure of particulate whey protein gels: Effect of NaCl concentration, pH, heating temperature, and protein composition
    • Verheul M, Roefs SPFM (1998) Structure of particulate whey protein gels: effect of NaCl concentration, pH, heating temperature, and protein composition. J Agric Food Chem 46:4909-4916
    • (1998) J Agric Food Chem , vol.46 , pp. 4909-4916
    • Verheul, M.1    Roefs, S.P.F.M.2
  • 70
    • 84989743963 scopus 로고
    • Can the gel point of a cross-linking polymer be detected by the G′-G" crossover?
    • Winter HH (1987) Can the gel point of a cross-linking polymer be detected by the G′-G" crossover? Polym Eng Sci 27:1698-1702
    • (1987) Polym Eng Sci , vol.27 , pp. 1698-1702
    • Winter, H.H.1
  • 71
    • 0022694827 scopus 로고
    • Analysis of the linear viscoelasticity of a crosslinking polymer at the gel point
    • Winter HH, Chambon F (1986) Analysis of the linear viscoelasticity of a crosslinking polymer at the gel point. J Rheol 30:367-382
    • (1986) J Rheol , vol.30 , pp. 367-382
    • Winter, H.H.1    Chambon, F.2
  • 72
    • 0001071307 scopus 로고
    • Harris P (ed) Elsevier Science Publishers, Barking
    • Woodward SA (1990) In: Harris P (ed) Food gels. Elsevier Science Publishers, Barking, pp 175-199
    • (1990) Food Gels , pp. 175-199
    • Woodward, S.A.1
  • 73
    • 0039163193 scopus 로고
    • Hudson BJF (ed) Applied Science Publishers, London
    • Wright DJ (1986) In: Hudson BJF (ed) Developments in food proteins, vol 4. Applied Science Publishers, London, pp 61-90
    • (1986) Developments in Food Proteins , vol.4 , pp. 61-90
    • Wright, D.J.1


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