A study on gelation of soybean globulin solutions

Bikbov, T. M.; Grinberg, V. Ya.; Schmandke, H.; Chaika, T. S.; Vaintraub, I. A.; Tolstoguzov, V. B.

doi:10.1007/bf01397891

Cited by 33 publications

(24 citation statements)

References 20 publications

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“…The nature of cross-links in protein gels has been discussed by several authors (Bikbov et al 1979(Bikbov et al , 1981Clark and Lee-Tuffnel, 1986;Clark et al, 1983;Morris, 1985Morris, , 1986Nishinari, 1978;Oakenfull, 1987). The consensus view is that with the exception of disulfide bonds in some protein gels, the molecules are held together by a combination of weak intermolecular forces, i.e., hydrogen bonds, electrostatic forces, Van der Waals forces and hydrophobic interactions.…”

Section: Introductionmentioning

confidence: 96%

Effects of Temperature on Viscoelastic Properties and Activation Energies of Whey Protein Gels

Katsuta

Kinsella

1990

Journal of Food Science

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The creep behavior of gels prepared with lo-15% whey protein was measured at 15-75°C. Gels prepared with 12-15% protein were thermorheologically simple, although their action was not totally consistent with Williams-Landel-Ferry (WLF) criteria. Gels made with less than 11% protein were more sensitive to temperature than those containing more than 11% protein and their thermal viscoclastic action was not consistent with polymer theory. The apparent activation energy (AHa) of the gels decreased with increasing tempcraturcs and noncovalent forces were important in maintaining gel structures.

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Section: Introductionmentioning

confidence: 96%

Effects of Temperature on Viscoelastic Properties and Activation Energies of Whey Protein Gels

Katsuta

Kinsella

1990

Journal of Food Science

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“…The results of a systematic study on phenomenology of formation and viscoelastic properties of soybean globulin (SBG) fraction gels were described by Bibkov et al [1]. The study showed the SBG gel network to be composed of aggregates of protein molecules.…”

Section: Introductionmentioning

confidence: 94%

Thermotropic gelation of ovalbumin 1. Viscoelastic properties of gels as a function of heating conditions and protein concentration at various pH values

Grinberg

Bibkov

Grinberg

et al. 1988

Colloid & Polymer Sci

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A study has been undertaken of stress relaxation in ovalbumin thermotropic gels with a concentration of 8-20 %, depending on time and temperature of heating (respectively, 20-60 min, 70~176 at pH 2.5-10.0. In all instances, the dependence of the initial gel elasticity modulus on heating has a single maximum. Gelation conditions corresponding to this maximum are considered optimal. Optimal gelation time is 30 rain, regardless of pH. On the other hand, the optimal heating temperature depends on pH. To the fight and left of the isoelectric point of protein (2.5 < pH < 4.0 and 5.5 < pH < 10.0) the optimal temperature is 80 ~ However, in the vicinity of the isoelectric point (4.0 < pH <_ 5.5) the optimal temperature rises considerably. Gels produced to the right and left of the isoelectric point belong to the homologous group A, while gels produced in the point vicinity belong to another homologous group B. Light scattering data proves group A gels to be more homogeneous optically. These gels may be supposed a single-phase system, while group B gels are two-phase-systems. For each group, the dependence of the relaxation modulus (G) of gels on heating conditions, pH and protein concentration (X 1, X2, X3, X4), as well as on time of relaxation (t) may be generally described as G(X1, X2, X3, X4, t) = Ge(X1, X2, X3, X4) f(t), where Ge is the equilibrium value of the elasticity modulus, and f(t) the relaxation function. Thus, a change in the parameters only affects the value of the equilibrium elasticity modulus, and exerts no effect on the relaxation time spectrum. For this reason, all the relaxation curves obtained may be transformed into two normalized relaxation functions: X1, X2, X3, X4, t)/G(X1, X2, X3, X4, 1) Each of these normalized functions corresponds to one of the homologous groups. Rheological similarity of gels in each homologous group evidently points to their structural similarity. Invariance of the gel relaxationproperties with regard to protein concentration, leads to a concentration dependence of the equilibrium modulus at various pH values. These dependences are curvilinear on a double logarithmic scale. The slope of the curve exceeds 2 in the entire concentration interval studied. In other words, the dependences obtained cannot be described by the usual "law of squares". On the other hand, they adequately match Hermans' theoretical relation for a network formed by random association of identical polyfunctional particles without cyclization. This simple model evidently gives a true picture of the major regularities of thermotropic gelation for ovalbumin. An agreement between this theory and experiment was achieved for a protein concentration of C* = 6.0 +_ 1.0 % at the gel point regardless of pH. Invariance of gelpoint position with regards to pH demands further confirmation.Key words: Ovalbumin, thermotropic_gels, stress relaxation, reduced variables method, viscoeleasticity, _heating, protein concentration, rheological similarity, structure of_gels. List of SymbolsTh, th = heating tempe...

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“…The work by Circle et al [1] has marked the beginning of investigations into thermotropic gelation of soybean globulin fraction (SBGF) [2][3][4][5][6][7][8] as well as its main components 7S and 11S globulins [9][10][11]. At present, the conditions of formation, structure, viscoelastic properties and conditions of solubility of SBGF thermotropic gels are well known [6,8].…”

Section: Introductionmentioning

confidence: 99%

“…At present, the conditions of formation, structure, viscoelastic properties and conditions of solubility of SBGF thermotropic gels are well known [6,8]. Experimental data served as a basis for proposing a structural model of gel, defining some of its parameters and putting forward assumptions in respect to the character of interaction leading to gelation [8]. However many problems associated with a gelation mechanism remain to be solved.…”

Section: Introductionmentioning

confidence: 99%

“…Experimental data served as a basis for proposing a structural model of gel, defining some of its parameters and putting forward assumptions in respect to the character of interaction leading to gelation [8]. According to certain data [9,10,12], the leading part in this process belongs to 11S globulin. Specifically, there is no unified opinion on the role of the basic SBGF components in the gelation process.…”

Section: Introductionmentioning

confidence: 99%

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