Heat Stability of Bovine Milk Immunoglobulins and Their Ability to Bind Lactococci as Determined by an ELISA

Ustunol, Z.; Sypien, C.

doi:10.1111/j.1365-2621.1997.tb12248.x

Cited by 12 publications

(5 citation statements)

References 16 publications

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“…Although beef or mammalian meats are not frequently cited as allergenic foods, some concern about the potential role of IgG in other bovine products such as milk could arise. It appears that the process of heating or pasteurization of the milk before consumption may reduce the immunogenicity of the milk by denaturation of the immunoglobulins ( 28). The use of SDS–PAGE or other techniques that systematically use denaturing agents when analyzing allergenic extracts may also abolish IgE reactivity to IgG.…”

Section: Discussionmentioning

confidence: 99%

Identification of bovine IgG as a major cross‐reactive vertebrate meat allergen

Ayuso

Lehrer

Lopez

et al. 2000

Allergy

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Bovine IgG appears to be a major cross-reacting meat allergen that could predict beef allergy. Further studies with oral IgG challenges should be performed to document the conclusion that in vitro reactivity correlates with clinical hypersensitivity. The role of bovine IgG in other bovine products such as milk, dander, or hair must also be studied, and the hypothesis that it is a cross-reacting allergen with other mammalian products validated.

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Section: Discussionmentioning

confidence: 99%

Identification of bovine IgG as a major cross‐reactive vertebrate meat allergen

Ayuso

Lehrer

Lopez

et al. 2000

Allergy

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“…Moreover, further increasing the pasteurization temperature gave rise to a progressively stronger inactivation of IgM, evident from the gradual disappearance of IgM from the samples at 71 °C, which was even more pronounced at 73 °C. While agglutinins in general have been shown to be inactivated in a temperature range of 62 to 81 °C (Mainer et al 1997), IgM in particular is known to be heat-labile and is totally denatured after 20 min at 85 °C (Ustonol & Sypien, 1997). However, Mainer et al (1997) showed that the overall quaternary structure of IgM was not denatured by a HTST (high temperature-short time; 72 °C, 15 s) treatment similar to that performed in the present study.…”

Section: Resultsmentioning

confidence: 99%

Thermal effects on IgM-milk fat globule-mediated agglutination

Hansen

Larsen

Wiking

2018

Journal of Dairy Research

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The process of agglutination causes firm cream layers in bovine milk, and a functioning agglutination mechanism is paramount to the quality of non-homogenized milks. The phenomenon is not well-described, but it is believed to occur due to interactions between immunoglobulins (Ig) and milk fat globules. For the first time, this paper demonstrates how the process of agglutination can be visualized using confocal laser scanning microscopy, rhodamine red and a fluoresceinisothiocynat-conjugated immunoglobulin M antibody. The method was used to illustrate the effect on agglutination of storage temperature and pasteurization temperature. Storage at 5 °C resulted in clearly visible agglutination which, however, was markedly reduced at 15 °C. Increasing storage temperature to 20 or 37 °C cancelled any detectable interaction between IgM and milk fat globules, whereby the occurrence of cold agglutination was documented. Increasing 20 s pasteurization temperatures from 69 °C to 71 °C and further to 73 °C lead to progressively higher inactivation of IgM and, hence, reduction of agglutination. Furthermore, 2-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis showed that changes in storage temperature caused a redistribution of Ig-related proteins in milk fat globule membrane isolates. Poly-immunoglobulin G receptor was present in milk fat globule preparations stored at cold (4 °C) conditions, but absent at storage at higher temperature (25 °C). The findings provide valuable knowledge to dairy producers of non-homogenized milk in deciding the right pasteurization temperature to retain the crucial agglutination mechanism.

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“…Goldsmith et al . (1983) and Ustunol and Sypien (1997) reported that heating at 62.5°C for 30 min did not affect the IgG content estimated by radial immunodiffusion assay and ELISA using antibovine IgG. The present results indicate that cow's milk IgG possesses not only strong antigen‐binding activity of the Fab region, but also biological activity of the Fc region on pasteurization at 63°C for 30 min, confirming that heat treatment at 62.5°C for 30 min is a useful practical procedure for the pasteurization of cow's milk IgG‐rich foods.…”

Section: Discussionmentioning

confidence: 99%

Antigen‐binding and protein G‐binding abilities of immunoglobulin G in hyperimmunized cow's milk treated under various conditions

Ohnuki

Otani

2005

Animal Science Journal

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Skim milk and whey prepared from milk secreted by cows that had been injected with bacteria were kept under various conditions, and the antigen‐binding and protein G‐binding abilities of immunoglobulin G (IgG) in the milk samples were investigated. More than 85% of the original antigen‐binding and protein G‐binding abilities remained when the skim milk was heated at 63°C for 60 min or kept at a pH range of 4–10 for 24 h at 37°C. Both of the high abilities were maintained on pepsin treatment above pH 4 and intestinal proteinase treatments. Little antigen‐binding and protein G‐binding abilities decreased upon storage of the powdered skim milk for 12 months at room temperature. In contrast, at least half, and more than 70% of their respective abilities, were lost upon incubation at pH 2 in the absence and presence of pepsin, respectively, for 1 h at 37°C. These results suggest that most of the biological activities of the Fab‐region and Fc‐region of bovine milk IgG can be maintained during processing or storage, and both of the inactivation degrees mainly depend on the stomach condition after oral ingestion of the IgG preparation.

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Heat Stability of Bovine Milk Immunoglobulins and Their Ability to Bind Lactococci as Determined by an ELISA

Cited by 12 publications

References 16 publications

Identification of bovine IgG as a major cross‐reactive vertebrate meat allergen

Identification of bovine IgG as a major cross‐reactive vertebrate meat allergen

Thermal effects on IgM-milk fat globule-mediated agglutination

Antigen‐binding and protein G‐binding abilities of immunoglobulin G in hyperimmunized cow's milk treated under various conditions

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