Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins

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

doi:10.1021/ma00080a037

Cited by 152 publications

(136 citation statements)

References 6 publications

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“…19 ) They reported that the value of the fractal dimension Dr was 2.01 ±0.02 which was similar to that predicted by the RLCCA model. However, in their study, the value of the polydispersity exponent 't was about I, which disagreed with that predicted by the RLCCA model, 1.5.…”

Section: Discussionsupporting

confidence: 66%

Fractal Analysis of Aggregates Formed by Heating Dilute BSA Solutions Using Light Scattering Methods

Hagiwara

Kumagai

Nakamura

1996

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionsupporting

confidence: 66%

Fractal Analysis of Aggregates Formed by Heating Dilute BSA Solutions Using Light Scattering Methods

Hagiwara

Kumagai

Nakamura

1996

Bioscience, Biotechnology, and Biochemistry

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“…This polymodal distribution of unheated WPI dispersions agrees with published literature. In particular, non-aggregated whey proteins, such as lg and lac monomers and dimers, remain below 7 nm (Gimel, Durand, & Nicolai, 1994;Nicorescu et al, 2008;Roefs & De Kruif, 1994); this corresponds to peak 1 distribution observed in unheated WPI. Peak 2 and 3 correspond to native whey aggregates, which are commonly observed in industrial hydrated WPI (Gr' acia-Julia ' et al, 2008;Nicorescu et al, 2008).…”

Section: Whey Protein Aggregationmentioning

confidence: 81%

Influence of moderate electric fields on gelation of whey protein isolate

et al. 2015

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Proteins are one of the food constituents most affected by heating, and some of the changes involve their unfolding, denaturation and gelation. Ohmic heating has often been claimed to improve the quality of foodstuffs due to its uniform heating and (putative) presence of a moderate electric field (MEF). However, this is still subject to discussion, so it is important to determine the effect of ohmic heating and of its MEF upon food constituents. Hence, the aim of this work was to evaluate the effects of MEF on denaturation, aggregation and viscoelastic properties of whey protein isolate (WPI), and compare them with those obtained via conventional heating under identical treatment conditions (up to 30 min at 85 o C). Results have shown that MEF interferes with whey protein unfolding and aggregation pathways at relatively high temperatures. MEF treatments have resulted in WPI solutions possessing more 8 and 10% of native Lactoglobulin and Lactalbumin, respectively, after 30 s of heating at 85 o C, when compared with a conventional heating method. Protein aggregates from MEF-treated WPI solutions presented a maximum increase in size of 78 nm, whereas conventional heating produced an increase of 86 nm. Unlike in conventional heating, aggregation of whey proteins during MEF was not sufficiently strong to form a true elastic gel network, since decreases in both storage and loss modulus were observed following MEF treatment. Our results suggest that MEF may provide a novel method for production of a whey protein matrix with distinctive gel-forming properties.2

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“…Typical fractal dimensions for protein aggregates are in the range 2.0-2.7. 38,39 We chose d ¼ 2.5, close to the value of 2.56 reported previously for antibodies, 18 but choosing other values in the interval did not qualitatively change the results. The radius of gyration in Eq.…”

Section: Thermal Denaturationmentioning

confidence: 95%

Aggregation of a multidomain protein: A coagulation mechanism governs aggregation of a model IgG1 antibody under weak thermal stress

et al. 2010

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Using an IgG1 antibody as a model system, we have studied the mechanisms by which multidomain proteins aggregate at physiological pH when incubated at temperatures just below their lowest thermal transition. In this temperature interval, only minor changes to the protein conformation are observed. Light scattering consistently showed two coupled phases: an initial fast phase followed by several hours of exponential growth of the scattered intensity. This is the exact opposite of the lagtime behavior typically observed in protein fibrillation. Dynamic light scattering showed the rapid formation of an aggregate species with a hydrodynamic radius of about 25 nm, which then increased in size throughout the experiment. Theoretical analysis of our light scattering data showed that the aggregate number density goes through a maximum in time providing compelling evidence for a coagulation mechanism in which aggregates fuse together. Both the analysis as well as size-exclusion chromatography of incubated samples showed the actual increase in aggregate mass to be linear and reach saturation long before all molecules had been converted to aggregates. The CH2 domain is the only domain partly unfolded in the temperature interval studied, suggesting a pivotal role of this least stable domain in the aggregation process. Our results show that for multidomain proteins at temperatures below their thermal denaturation, transient unfolding of a single domain can prime the molecule for aggregation, and that the formation of large aggregates is driven by coagulation.

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Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins

Cited by 152 publications

References 6 publications

Fractal Analysis of Aggregates Formed by Heating Dilute BSA Solutions Using Light Scattering Methods

Fractal Analysis of Aggregates Formed by Heating Dilute BSA Solutions Using Light Scattering Methods

Influence of moderate electric fields on gelation of whey protein isolate

Aggregation of a multidomain protein: A coagulation mechanism governs aggregation of a model IgG1 antibody under weak thermal stress

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