Experimental evidence for a two-step process in the aggregation of β-lactoglobulin at pH 7

Aymard, P; Gimel, Jean-Christophe; Nicolai, Taco; Durand, Dominique

doi:10.1051/jcp/1996930987

Cited by 80 publications

(95 citation statements)

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“…Based on the hypothesis regarding the gelation mechanism of yolk, gelation induced by freeze-thawing is a result of the formation of lipoprotein aggregates. The β-LG aggregate network structure determined by Aymard, Gimel, Nicolai, and Durand (1996) has a similar appearance to the proposed lipoprotein aggregate network shown in Figure 3.6.…”

Section: Matrix Mobilitymentioning

confidence: 58%

“…Though the structure of β-LG and yolk LDL are different, the aggregation is similar so the effect on T2 is comparable between the two food components. With high concentrations of β-LG as well as application of heat and prolonged heating, β-LG form aggregates possessing a fractal pattern, and these fractal aggregates form a gel (Aymard, Gimel, Nicolai, & Durand, 1996;Indrawati, Stroshine, & Narsimhan, 2007). Based on the hypothesis regarding the gelation mechanism of yolk, gelation induced by freeze-thawing is a result of the formation of lipoprotein aggregates.…”

Section: Matrix Mobilitymentioning

confidence: 99%

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Determination of the Gelation Mechanism of Freeze–Thawed Hen Egg Yolk

Acevedo

Horner

et al. 2015

J. Agric. Food Chem.

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A study of yolks stored up to 168 d at −20 °C was conducted to determine the gelation behavior and mechanism of freeze–thawed yolk. Methods used were rheology, native and sodium dodecyl sulfate polyacrylamide gel electrophoresis (native- and SDS-PAGE), differential scanning calorimetry (DSC), transmission electron microscopy (TEM), particle size analysis, and proton nuclear magnetic resonance (1H NMR) spectroscopy for matrix mobility. Results indicate that both constituents of plasma and granules contributed to gelation of yolk under freezing. PAGE analyses suggest that granular proteins participated in aggregation during freeze–thaw. Increasing gel strength and particle size and decreasing water and lipid–water mobility indicate that lipoproteins or apolipoproteins aggregated. At storage times ≥84 d, increased protein and lipid mobility, the detection of smaller particles, and secondarily increased gel strength suggest the liberation of protein or lipoprotein components from previously formed aggregates and further aggregation of these constituents. Disruption of the gelled yolk matrix observed with TEM supported that ice crystal formation was required for gelation to occur. A two-stage dynamic gelation model is thus proposed.

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Section: Matrix Mobilitymentioning

confidence: 58%

Section: Matrix Mobilitymentioning

confidence: 99%

Determination of the Gelation Mechanism of Freeze–Thawed Hen Egg Yolk

Acevedo

Horner

et al. 2015

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

“…34 The analogous model, namely, the model of nucleation-depend- 40 observed the appearance of the primary aggregates with R h 5 85 nm that serve as precursors to large precipitates in the course of aggregation of bovine Zn-insulin upon shaking at 378C. According to Nicolai and coworkers, [41][42][43][44][45] thermal aggregation of b-lactoglobulin at pH 7 in the presence of 0.1M NaCl proceeds through the stage of the formation of the primary aggregates containing about 100 denatured monomers. In the works by Kurganov and coworkers, 5,23,24,46 these primary aggregates were called the start aggregates to stress the circumstance that the further growth of the primary aggregates occur by their sticking but not by the attachment of the individual molecules of denatured protein.…”

Section: Discussionmentioning

confidence: 99%

Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle: Mechanism of protective action of α‐crystallin

et al. 2007

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The kinetics of thermal aggregation of glycogen phosphorylase b (Phb) from rabbit skeletal muscle have been studied by dynamic light scattering (0.08M Hepes, pH 6.8, containing 0.1M NaCl; 48 degrees C). The hydrodynamic radius of the start aggregates determined from the initial linear parts of the dependences of the hydrodynamic radius (R(h)) on time was found to be 16.7 +/- 1.0 nm. At rather high values of time, the R(h) value for the protein aggregates becomes proportional to t(1/1.8) = t(0.56) suggesting that the aggregation process proceeds in the regime of diffusion-limited cluster-cluster aggregation. In the presence of alpha-crystallin, a protein possessing the chaperone-like activity, the process of protein aggregation switches to the regime of reaction-limited cluster-cluster aggregation as indicated by the exponential dependence of the R(h) value on time. It was shown that the addition of alpha-crystallin raises the rate of thermal inactivation of Phb. These data in combination with the results of the study of interaction of Phb with alpha-crystallin by analytical ultracentrifugation suggest that alpha-crystallin interacts with the intermediates of unfolding of the Phb molecule.

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“…For heat-induced denaturation the important concentrations are the critical association concentration (CAC) below which aggregation does not occur, gelation concentration (C g ) above which gel formation occurs and salt concentration (C s ). C s can dramatically change the structure of a gel, causing densification of aggregates due to increased branching, resulting in a decrease in CAC and decreased flexibility [25,31]. The gels used here have concentration C = 90 g/L which is well above the expected CAC and C g for pH = 5.2 and 7.0 [25,28], while C s = 0.3 M NaCl falls into a high ionic strength regime.…”

Section: Introductionmentioning

confidence: 91%

Erratum to: Hydrodynamic dispersion in $ \beta$ -lactoglobulin gels measured by PGSE NMR

et al. 2011

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Abstract. The displacement scale dependent molecular dynamics of solvent water molecules flowing through β-lactoglobulin gels are measured by pulse gradient spin echo (PGSE) nuclear magnetic resonance (NMR). Gels formed under different pH conditions generate structures which are characterized by magnetic resonance imaging (MRI) and PGSE NMR measured dynamics as homogeneous and heterogeneous. The data presented clearly demonstrate the applicability of the theoretical framework for modeling hydrodynamic dispersion to the analysis of protein gels.

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Experimental evidence for a two-step process in the aggregation of β-lactoglobulin at pH 7

Cited by 80 publications

References 0 publications

Determination of the Gelation Mechanism of Freeze–Thawed Hen Egg Yolk

Determination of the Gelation Mechanism of Freeze–Thawed Hen Egg Yolk

Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle: Mechanism of protective action of α‐crystallin

Erratum to: Hydrodynamic dispersion in $ \beta$ -lactoglobulin gels measured by PGSE NMR

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