Analysis of denaturation of bovine IgG by heat and high pressure using an optical biosensor

Indyk, Harvey E.; Williams, Jacob W.

doi:10.1016/j.idairyj.2007.10.004

Cited by 54 publications

(40 citation statements)

References 37 publications

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“…IgG denaturation becomes significantly irreversible at temperatures higher than 65°C (Mainer et al 1999;Indyk et al 2008). IgG almost completely loses its antigen-binding activity after heat treatment for several minutes at 90°C (Augener and Grey 1970;van der Linden et al 1999;Ladenson et al 2006;Akazawa-Ogawa et al 2014).…”

Section: Heat-induced Denaturation Of Iggmentioning

confidence: 99%

Heat denaturation of the antibody, a multi-domain protein

2017

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The antibody is one of the most well-studied multi-domain proteins because of its abundance and physiological importance. In this article, we describe the effect of the complex, multi-domain structure of the antibody on its denaturation by heat. Natural antibodies are composed of 6 to 70 immunoglobulin fold domains, and are irreversibly denatured at high temperatures. Although the separated single immunoglobulin fold domain can be refolded after heat denaturation, denaturation of pairs of such domains is irreversible. Each antibody subclass exhibits a distinct heat tolerance, and IgE is especially known to be heat-labile. IgE starts unfolding at a lower temperature compared to other antibodies, because of the low stability of its CH3 domain. Each immunoglobulin domain starts unfolding at different temperatures. For instance, the CH3 domain of IgG unfolds at a higher temperature than its CH2 domain. Thus, the antibody has a mixture of folded and unfolded structures at a certain temperature. Co-existence of these folded and unfolded domains in a single polypeptide chain may increase the tendency to aggregate which causes the inactivation of the antibody.

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Section: Heat-induced Denaturation Of Iggmentioning

confidence: 99%

Heat denaturation of the antibody, a multi-domain protein

2017

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“…For n ≠ 1, the general rate equation can be solved to get: [207], 1.5 [208,209], 2.0 [210,211] or 2.5 [212]. The order of the reaction is typically determined by fitting the experimental data using different reaction orders, and assigning the order with highest R 2 value.…”

Section: Comparison Of Es-dma With Secmentioning

confidence: 99%

Electrospray–differential mobility analysis of bionanoparticles

Guha

Tarlov

et al. 2012

Trends in Biotechnology

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The growth of the multibillion dollar bionanoparticle industry has spurred the development of new physical characterization methods. One such method, electrospraydifferential mobility analysis (ES-DMA) constitutes an electrospray for aerosolization of bionanoparticles (such as viruses, gold-nanoparticles, proteins, nanoparticle-protein complexes) and an ion mobility method that operates at atmospheric conditions, and separates bionanoparticles spatially. This dissertation identifies some relevant "problem" areas for ES-DMA by reviewing selected applications.Some such problems are: proteins while passing through ES capillaries are found to interact with it and thus produce time dependent size distributions. Further, it is thought that adsorbed proteins may subsequently desorb and influence size distributions with the ES-DMA which may concomitantly affect quantification of aggregates. These artifacts are studied systematically and it is demonstrated that ES-DMA can quantify adsorption-desorption of complex protein mixtures at high shear rates. Further, it is shown that desorbing proteins do not have a significant effect on size distributions. Another artifact of the ES takes place during the aersolization process. Two units (called monomers) of a bionanoparticle may get encapsulated in the same ES droplet and upon drying of the droplet create artificial dimers thus affecting quantification with ES-DMA. Assuming Poisson distribution, this thesis provides a systematic approach that can be undertaken to eliminate this artifact. A third artifact arises from the low sensitivity of the DMA to size increase. When a ligand (for e.g. protein) adsorbs to a bionanoparticle it creates an increase in the size of the later, which can be used to quantify the amount of ligand adsorbed per bionanoparticle. As ligands can change conformations upon adsorption, using ES-DMA for such applications may be flawed. This issue has been identified and a solution has been provided by integrating a mass analyzer after the ES-DMA.After correcting for these artifacts, this dissertation delves into characterization of different types of bionanoparticles and demonstrates that ES-DMA has several advantages over other traditional techniques such as transmission electron microscopy, size exclusion chromatography, analytical ultracentrifugation, dynamic light scattering and plaque assay and thus has immense potential to become a process analytical technique in biomanufacturing environments. ELECTROSPRAY-DIFFERENTIAL MOBILITY ANALYSIS OF BIONANOPARTICLES

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“…The decrease in IgG content, TWP assayed by ELISA technique and turbidity decrease (after centrifugation) may be due to aggregation and denaturation/unfolding of IgG molecules effected by heat treatment and pH increase (close to pI) that influences in loss of antigenicity [16,61]. The conformation change in the IgG molecule occurred during heat exposure reduces antigen-binding activity of this protein Calmettes et al [62], whereas, antigen-binding site of IgG is more sensitive to heat compared to other part of the molecule [21,22].…”

Section: Effect Of Heat On Liquid Whey Igg Content At Various Phmentioning

confidence: 99%

“…The same observation was noted even when whole colostrum was pasteurized (60°C/30 min), that no reduction on the concentration of the Immunoglobulins. Immunoglobulins in whole colostrum and colostrum whey were more resistant to heat processing temperatures compared to colostrum concentrate without fat, casein, salts and lactose, means that such components may protect the Immunoglobulins during heat processing treatment and filtration [16].…”

Section: Effect Of Heat On Liquid Whey Igg Content At Various Phmentioning

confidence: 99%

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The Influence of Heat Treatment in Liquid Whey at Various pH on Immunoglobulin G and Lactoferrin from Yak and Cows’ Colostrum/Milk

Xiaoyun¹,

Lin²

2015

J Food Process Technol

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Yak milk is gaining popularity yearly, as a source of nutritious, immune, less likely to cause allergies than cows' milk and a means of generating income, though ranked behind bovine milk in China. The main objective of the research was to compare the Immunoglobulin G (IgG) and Lactoferrin (LF) concentrations of liquid whey from Yak and dairy Cows' colostrum or milk. Thereafter, the thermal stability of liquid whey was evaluated by measuring the concentration change in IgG and LF using an ELISA technique, as influenced by temperature and pH after centrifugation.IgG and LF concentrations in liquid whey from colostrums both in yak and cow were significantly higher (p<0.05) compared to milk. IgG did not differ significantly (p>0.05) between yak and cow's milk, as well as between yak and cow's colostrum. Also, LF content was not significant different between yak and cow milk. However, LF concentration was significantly higher in cows' colostrum than in yak. With reference to IgG content, yak breed observed to produce high quality colostrum for all samples tested compared to cows.The extent of IgG and LF denaturation confirmed to increase with increased protein concentration, temperature and pH change near to pI. Colostral IgG and LF were more denatured compared to milk in both yak and dairy cows. There was significant (p<0.05) influence of pH changes resulted in either partial or complete denaturation or increased tendency to aggregate, which was removed during centrifugation. Liquid whey less affected at lower pH and at mild heat temperatures.

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Analysis of denaturation of bovine IgG by heat and high pressure using an optical biosensor

Cited by 54 publications

References 37 publications

Heat denaturation of the antibody, a multi-domain protein

Heat denaturation of the antibody, a multi-domain protein

Electrospray–differential mobility analysis of bionanoparticles

The Influence of Heat Treatment in Liquid Whey at Various pH on Immunoglobulin G and Lactoferrin from Yak and Cows’ Colostrum/Milk

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