Skip to main content
SpringerLink
Log in

Rheology and microstructure of heat-induced egg yolk gels

  • Original Contribution
  • Published:
Rheologica Acta Aims and scope Submit manuscript

Abstract

The evolution of native egg yolk undergoing a thermal-induced sol-gel transition was studied by using temperature controlled small amplitude oscillatory shear measurements. The critical gel point was determined according to Winter’s criterion: 1) from the measurements of storage and loss moduli as a function of heating time at different frequencies, and 2) from the exponents of the power law mechanical spectra obtained after cure experiments performed up to a maximum temperature (60–90 °C) followed by a sudden decrease in temperature up to 20 °C. Differential Scanning Calorimetry (DSC) was performed in order to investigate thermal transitions in egg yolk. Microstructure of gels was evaluated by Transmission and Scanning Electron Microscopy. The results obtained were discussed in terms of the processes involved in protein gelation: change in the protein system, aggregation of partially denaturated protein molecules and association of aggregates. As a result, an elastic gel network was always obtained. The influence of frequency, heating rate, solids concentration and maximum temperature of processing, was analysed. Most of the transformations found during thermal processing were found to be basically irreversible, even at the sol state and gel point. However, some reversible phenomena were detected during constant temperature processing depending on the maximum temperature performed.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3a,b
Fig. 4a,b
Fig. 5
Fig. 6a,b
Fig. 7
Fig. 8
Fig. 9
Fig. 10
Fig. 11a–f

Similar content being viewed by others

References

  • Adam M, Lairez D (1996) In: Cohen Addad JP (ed) Physical properties of polymeric gels. Wiley, New York, pp 88–139

  • 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

    CAS  Google Scholar 

  • Bauer R, Carrotta R, Rischel C, Ogendal L (2000) Characterization and isolation of intermediates in b-lactoglobulin heat aggregation at high pH. Biophys J 79:1030–1038

    CAS  PubMed  Google Scholar 

  • Bell LN, Touma DE (1996) Glass transition temperatures determined using a temperature-cycling differential scanning calorimeter. J Food Sci 61:807–810, 828

    CAS  Google Scholar 

  • Belloque J, Smith GM (1998) Thermal denaturation of β-lactoglobulin. a 1H-NMR study. J Agric Food Chem 46:1805–1813

    Article  CAS  Google Scholar 

  • 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

    Article  Google Scholar 

  • 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

    Article  CAS  Google Scholar 

  • 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

    CAS  Google Scholar 

  • 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

    Article  CAS  PubMed  Google Scholar 

  • Chambon F, Winter HH (1987) Linear viscoelasticity at the gel point of a crosslinking PDMS with imbalanced stoichiometry. J Rheol 31:683–697

    CAS  Google Scholar 

  • Chang CM, Powrie WD, Fennema O (1977) Microstructure of egg yolk. J Food Sci 42:1193–1200

    CAS  Google Scholar 

  • Clark AH (1998) In: Hill SE, Ledward DA, Mitchell JR (eds) Functional properties of food macromolecules. Aspen Publishers, Gaithersburg, pp 77–142

  • Clark AH, Lee-Tuffnell CD (1986) In: Mitchell JR, Ledward AD (eds) Functional properties of food macromolecules. Elsevier Applied Science, Barking, pp 203–272

  • 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

    Google Scholar 

  • Clark AH, Judge FJ, Richards JB, Stubbs JM, Suggett A (1981b) Electron microscopy of network structures in thermally-induced globular protein gels. Int J Peptide Protein Res 17:380–392

    CAS  Google Scholar 

  • Clark AH, Kavanagh GM, Ross-Murphy SB (2001) Globular protein gelation-theory and experiment. Food Hydrocolloid 15:383–400

    Article  CAS  Google Scholar 

  • Cocard S, Tassin JF, Nicolai T (2000) Dynamical mechanical properties of gelling colloidal disks. J Rheol 44:585–594

    Article  CAS  Google Scholar 

  • Damodaran S (1997) In: Damodaran S, Paraf A (eds) Food proteins and their applications. Marcel Dekker, New York, pp 1–24

  • de Gennes PG (1979) Scaling concepts in polymer physics. Cornell University Press, Ithaca

  • 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

    Article  Google Scholar 

  • Doi E (1993) Gels and gelling of globular proteins. Trends Food Sci Technol 4:1–5

    CAS  Google Scholar 

  • 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

    CAS  PubMed  Google Scholar 

  • Doublier JL, Launay B, Cuvelier G (1992) In: Rao MA, Steffe JF (eds) Viscoelastic properties of foods. Elsevier Applied Science, London, pp 371–434

  • 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

    CAS  Google Scholar 

  • 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

    Article  Google Scholar 

  • Ferry JD (1948) Protein gels. Adv Protein Chem 4:1–78

    CAS  Google Scholar 

  • Fox, PF, Mulvihill DM (1990) In: Harris P (ed) Casein in food gels. Elsevier Applied Science, London, pp 121–173

  • Gilsenan PM, Ross-Murphy SB (2000) Viscoelasticity of thermoreversible gelatin gels from mammalian and piscine collagens. J Rheol 44:871–883

    Article  CAS  Google Scholar 

  • Gimel JC, Durand D, Nicolai T (1994) Structure and distribution of aggregates formed after heat-induced denaturation of globular-proteins. Macromolecules 257:583–589

    Google Scholar 

  • 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

    Google Scholar 

  • 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

    CAS  Google Scholar 

  • Hegg P(1982) Conditions for the formation of heat-induced gels of some globular food proteins. J Food Sci 47:1241–1244

    CAS  Google Scholar 

  • Hsu S (1999) Rheological studies on gelling behavior of soy protein isolates. J Food Sci 64:136–140

    CAS  Google Scholar 

  • Hsu S, Lu S, Huang C (2000) Viscoelastic changes of rice starch suspensions during gelatinization. J Food Sci 65:215–220

    CAS  Google Scholar 

  • 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

    Article  CAS  Google Scholar 

  • Kinsella JE (1976) Functional properties of proteins in foods: a survey. CRC Crit Rev Food Sci Nutr 7:219–280

    CAS  Google Scholar 

  • 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

    CAS  Google Scholar 

  • Lairez D, Adam M, Raspaud E, Emery JR, Durand D (1992) Do local motions influence rheological properties near the gelation threshold? Progr Colloid Polym Sci 90:37–42

    CAS  Google Scholar 

  • Langton M, Hermansson AM (1992) Fine-stranded and particulate gels of β-lactoglobulin and whey-protein at varying pH. Food Hydrocolloid 5:523–539

    CAS  Google Scholar 

  • 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

    Article  Google Scholar 

  • Le Bon C, Nicolai T, Durand D (1999b) Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation. Macromolecules 32:6120–6127

    Article  Google Scholar 

  • 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

    Article  CAS  PubMed  Google Scholar 

  • 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

    Google Scholar 

  • 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

    CAS  Google Scholar 

  • 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

    CAS  Google Scholar 

  • Ndi EE, Swanson BG, Barbosa-Canovas GV, Luedecke LO (1996) Rheology and microstructure of β-lactoglobulin/sodium polypectate gels, J Agric Food Chem 44:86–92

    Google Scholar 

  • 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

    Article  CAS  PubMed  Google Scholar 

  • 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

    Article  Google Scholar 

  • 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

  • Oakenfull D, Pearce J, Burley RW (1997) In: Damodaran S, Paraf A (eds) Food proteins and their applications. Marcel Dekker, New York, pp 111–142

  • Pilosof AMR (2000) In: Pilosof AMR, Bartholomai GB (eds) Caracterización funcional y estructural de proteínas. Eudeba, Buenos Aires, pp 75–95

  • Puppo MC, Añon MC (1998) Structural properties of heat-induced soy protein gels as affected by ionic strength and pH. J Agric Food Chem 46:3583–3589

    Article  CAS  Google Scholar 

  • Puppo MC, Añon MC (1999) Soybean protein dispersions at acid pH. Thermal and rheological properties. J Food Sci 64:50–56

    CAS  Google Scholar 

  • 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

    CAS  PubMed  Google Scholar 

  • Richardson, PH Norton IT (1998) Gelation behavior of concentrated locust bean gum solutions. Macromol 31:1575–1583

    Article  CAS  Google Scholar 

  • Richardson RK, Ross-Murphy SB (1981) Mechanical properties of globular protein gels. I. Incipient gelation behaviour. Int J Biol Macromol 3:315–322

    Article  CAS  Google Scholar 

  • Ross-Murphy SB (1991) Incipient behaviour of gelatin gels. Rheol Acta 30:401–411

    CAS  Google Scholar 

  • Sánchez C, Burgos J (1997) Gelation of sunflower globulin hydrolysates: rheological and calorimetric studies. J Agric Food Chem 45:2407–2412

    Article  Google Scholar 

  • Scanlan JC, Winter HH (1991) Composition dependence of the viscoelasticity of end-linked poly(dimethylsiloxane) at the gel point. Macromolecules 24:47–54

    CAS  Google Scholar 

  • Shay JS, Raghavan SR, Khan SA (2001) Thermoreversible gelation in aqueous dispersions of colloidal particles bearing grafted PEO chains. J Rheol 45:913–927

    Article  CAS  Google Scholar 

  • Shenstone FS (1968) In: Carter TC (ed) Egg quality: a study of the hen’s egg. Oliver and Boyd, Edinburgh, pp 26–66

  • Standing M, Langton M, Hermansson AM (1992) Inhomogeneous fine-stranded β-lactoglubulin gels. Food Hydrocolloid 6:455–470

    Google Scholar 

  • Standing M, Langton M, Hermansson AM (1995) Small and large deformation studies of protein gels. J Rheol 39:1445–1450

    Article  Google Scholar 

  • Stauffer D, Coniglio A, Adam M (1982) Gelation and critical phenomena. Adv Polym Sci 44:103–158

    CAS  Google Scholar 

  • 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

    Google Scholar 

  • Te Nijenhuis K, Winter HH (1989) Mechanical properties at the gel point of a crystallizing poly(vinylchloride) solution. Macromolecules 22:411–414

    Google Scholar 

  • 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

    Article  Google Scholar 

  • Vardhanabhuti B, Foegeding EA, McGuffey MK, Daubert CR, Swaisgood HE (2001) Gelation properties of dispersions containing polymerized and native whey protein isolate. Food Hydrocolloid 15:165–175

    Article  CAS  Google Scholar 

  • 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

    Article  CAS  Google Scholar 

  • 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

    CAS  Google Scholar 

  • Winter HH, Chambon F (1986) Analysis of the linear viscoelasticity of a crosslinking polymer at the gel point. J Rheol 30:367–382

    Article  Google Scholar 

  • Woodward SA (1990) In: Harris P (ed) Food gels. Elsevier Science Publishers, Barking, pp 175–199

  • Wright DJ (1986) In: Hudson BJF (ed) Developments in food proteins, vol 4. Applied Science Publishers, London, pp 61–90

Download references

Acknowledgments

This work is part of a research project sponsored by the CICYT, Spain (research project ALI 99-0502). The authors gratefully acknowledge its financial support.

Author information

Authors and Affiliations

  1. Departamento de Ingeniería Química, Facultad de Química, Universidad de Sevilla, 41012, Sevilla, Spain

    Felipe Cordobés & Antonio Guerrero

  2. Departamento de Ingeniería Química, Escuela Politécnica Superior La Rábida, 21819 Palos de la Frontera, Huelva, Spain

    Pedro Partal

Authors
  1. Felipe Cordobés
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Pedro Partal
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Antonio Guerrero
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Antonio Guerrero.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Cordobés, F., Partal, P. & Guerrero, A. Rheology and microstructure of heat-induced egg yolk gels. Rheol Acta 43, 184–195 (2004). https://doi.org/10.1007/s00397-003-0338-3

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00397-003-0338-3

Keywords

Search

Navigation