Stability of Membrane‐Sterilized Bovine Immunoglobulins Aseptically Added to UHT Milk

Fukumoto, Lana; Skura, B.J.; Nakai, S.

doi:10.1111/j.1365-2621.1994.tb08120.x

Cited by 26 publications

(17 citation statements)

References 11 publications

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“…2) suggested a higher thermoresistance for IgA than for IgG below 69ЊC, experiments not shown demonstrated an extremely slow rate for IgG denaturation at 65ЊC. These results were consistent with those reported by Fukumoto et al (1994), who found a D 65 value for IgG more than 4 times greater than what we obtained for IgA. Li-Chan et al (1995) obtained D values lower than ours for IgG heated in different media.…”

Section: Denaturation Of Immunoglobulinssupporting

confidence: 92%

Kinetic and Thermodynamic Parameters for Heat Denaturation of Bovine Milk IgG, IgA and IgM

Mainer

Sánchez

Ena

et al. 1997

Journal of Food Science

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For heat denaturation of bovine milk immunoglobulins (IgG, IgA and IgM) in the temperature range 62 to 81ЊC, the D values were IgG Ͼ IgA Ͼ IgM at any temperature. The Z values were 6.29, 4.00 and 5.17ЊC for IgG, IgA and IgM, respectively. Heat denaturation of bovine milk immunoglobulins followed a reaction kinetics in the order of nϭ1.5. The highest value for apparent energy of activation was observed for IgA, and the lowest for IgG. Bovine milk immunoglobulins could resist the HTST pasteurization treatment at 72ЊC for 15 sec without affecting their structure.

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Section: Denaturation Of Immunoglobulinssupporting

confidence: 92%

Kinetic and Thermodynamic Parameters for Heat Denaturation of Bovine Milk IgG, IgA and IgM

Mainer

Sánchez

Ena

et al. 1997

Journal of Food Science

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“…To determine a suitable range of holding temperatures and times in this work, preliminary experiments were performed and also other authors' results (Fukumoto et al 1994;Dominguez et al 1997) were referred to. Dominguez et al showed that the antigen-binding activity of IgG could survive a heat treatment of 63 Á658C/60 min, and the temperature range of 69 Á818C was chosen.…”

Section: Discussionmentioning

confidence: 99%

“…So the quantification of IgG in dairy products was heavily dependent on the degree of denaturation of the protein. There was considerable variation in literature values, such as 1 (Fukumoto et al 1994;Chan et al 1995;Li-Chan et al 1995), 1.2 (Zhang & Guo 2001), 1.5 (Law 1995;Dominguez et al 1997;Mainer et al 1999) or 2 (Lucisano et al 1994) for the reaction orders of thermal denaturation of IgG, the denaturation of IgG was therefore believed to involve several simultaneous reactions with different temperature dependence. These differences also resulted from the different systems employed, for example, concentration of proteins or acidity can affect the conformation of IgG.…”

Section: Introductionmentioning

confidence: 95%

Comparative studies on thermoresistance of protein G-binding region and antigen determinant region of immunoglobulin G in acidic colostral whey

Jin-song

Wang

Zheng

2007

Food and Agricultural Immunology

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The kinetics of the denaturation of antigen determinant (AGD) region and protein G-binding (PGB) region of bovine immunoglobulin G (IgG) in acidic colostral whey were studied by single radial immunodiffusion (SRID) and protein G affinity chromatography (PrGAC) during the same courses of heat treatment. The kinetic and thermodynamic parameters for heat-induced denaturation of AGD and PGB regions of IgG were determined over a temperature range of 69 Á818C. The denaturation reactions of both AGD and PGB regions of IgG were best described with apparent reaction order of 1.2, the activation energy values of the denaturation reactions were 159.42 kJ/mol and 235.37 kJ/mol respectively. This work suggested that the AGD region was more heat-labile than the PGB region of IgG in acidic colostral whey, Moreover, the higher values of the constant for the AGD region meant that, once the unfolding of the region started, denaturation would occur more quickly than the PGB region on IgG molecule. All these factors contributed to the fact that generally the IgG contents in the products of bovine colostrum determined by PrGAC would be higher than those by SRID.

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“…Bovine milk is a good medium for functional products containing, for example, specific antibodies. The shelf‐life of these products can be prolonged by membrane filtration (10) or by fermentation processing. In our study with UHT milk, the pH remained stable for up to 2 months.…”

Section: Discussionmentioning

confidence: 99%

“…In addition to the previously described composition of IP and CP (20, 22), further analyses were carried out for total IgA, IgM, IGF‐1, TGF‐β1 and TGF‐β2 (10, 31). IgG was analysed with gel filtration chromatography according to Syväoja and Korhonen (37).…”

Section: Methodsmentioning

confidence: 99%

Stability and activity of specific antibodies against Streptococcus mutans and Streptococcus sobrinus in bovine milk fermented with Lactobacillus rhamnosus strain GG or treated at ultra‐high temperature

Wei

Loimaranta

Tenovuo

et al. 2002

Oral Microbiology and Immunology

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Passive local immunization against dental caries is a promising approach to its prevention, as clinical evidence of active oral or nasal immunization is still limited and controversial. By means of systemic immunization of pregnant cows with a multivalent vaccine, high titres of IgG antibodies against human cariogenic bacteria, Streptococcus mutans and Streptococcus sobrinus, were produced in bovine colostrum. The purified immune product (IP) of this preparation has a number of anticariogenic properties, such as inhibition of streptococcal adherence to saliva-coated hydroxyapatite and inhibition of glucosyltransferase enzymes. This study investigated whether IP antibodies remained active and functional when added to ultra-high temperature (UHT)-treated milk or to Lactobacillus rhamnosus GG (LGG)-fermented milk stored for an extended time. LGG was chosen because of its widely known health benefits in humans and animals. A commercial UHT toddler's milk was supplemented with IP and stored for 2 months at 5, 21 and 30 degrees C. The antistreptococcal titres in UHT milk did not decline at any temperature during storage, and UHT-IP inhibited the adherence of S. mutans for up to 2 months. This was not the case with UHT toddler's milk without IgG antibodies. Milk was fermented with live LGG cells in the presence or absence of 5% IP. The antistreptococcal titres declined to about 30% of the original titres after storage. Fresh milk alone slightly enhanced streptococcal adhesion but fresh milk with IP inhibited the adherence of S. mutans by over 50%. LGG-positive fermented milk without antibodies also inhibited (P < 0.05) the adhesion by about 40%. In both LGG-fermented and UHT immune milk, the activity of antibodies against cariogenic streptococci was maintained during the expected shelf-life of these products. From the anticariogenic point of view it may be beneficial to add bovine-specific antibodies against mutans streptococci to probiotic LGG-containing milk products.

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Stability of Membrane‐Sterilized Bovine Immunoglobulins Aseptically Added to UHT Milk

Cited by 26 publications

References 11 publications

Kinetic and Thermodynamic Parameters for Heat Denaturation of Bovine Milk IgG, IgA and IgM

Kinetic and Thermodynamic Parameters for Heat Denaturation of Bovine Milk IgG, IgA and IgM

Comparative studies on thermoresistance of protein G-binding region and antigen determinant region of immunoglobulin G in acidic colostral whey

Stability and activity of specific antibodies against Streptococcus mutans and Streptococcus sobrinus in bovine milk fermented with Lactobacillus rhamnosus strain GG or treated at ultra‐high temperature

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