Latin name: Bos spp.
Source material: Skimmed cow's milk
Milk is an opaque, white liquid produced by the mammary glands of female mammals. Mammary glands are highly specialised sweat glands. The female ability to produce milk is one of the defining characteristics of mammals. It provides the primary source of nutrition for newborns before they are able to digest other types of food. The early lactation milk is known as colostrum, and carries the mother's antibodies to the baby. In many cultures of the world – especially the Western world – humans continue to consume milk beyond infancy, using the milk of other animals (in particular, cows) as a food product. (1)
Cow's milk is a major cause of adverse reactions in infants, and hidden exposure is common. Casein (cheese) is a heat-stable allergen, while Whey proteins are altered by boiling.
Cow's milk is ingested raw, pasteurised, boiled, or processed into dairy products such as cream, butter, yoghurt, ice cream, and cheese. Industrial science has processed milk into casein, Whey protein, lactose, condensed milk, powdered milk, and many other food-additive and industrial products.
Milk, cheese and other dairy products are consumed plain or flavoured, and as ingredients in bread, pastry and numerous other dishes such as pancakes and soups.
Milk and Milk derivatives are used in a wide variety of confectionery products. Caramel flavour is best developed from sweetened condensed Milk. Caseins help enhance moisture retention in sweets. Hydrolysed Milk proteins are whipping agents for frappés and marshmallows. In baked goods, Milk improves dough strength, crust colour and resilience.
Cow’s milk protein may be found in house dust (2) and in other non-food sources such as a powder in latex gloves (3) and dermatological powders. (4)
Milk is used in making processed meat, such as ham, sausages and pâtés.
Hydrolysed Milk formulas are manufactured from whey or casein protein.
Milk contains more than 40 proteins, and all of them may act as human species antigens.
Milk of ruminant species other than Cow (e.g. buffalo, Sheep, Goat, human, and many other species) is constituted from the same or very homologous proteins, which share the same structural, functional and biological properties. However, human milk does not contain ß-lactoglobulin (beta-lactoglobulin, or BLG). (5) Human and Bovine milk differ substantially in the ratio of Whey to Casein protein (approximately 60:40 in human milk and approximately 20:80 in Bovine milk) and in the proportions of specific proteins. (6)
Milk composition changes during processing. Cow's milk contains approximately 30 to 35 g/L (3-3.5%) of Cow's milk proteins (CMPs), which can be divided into 2 main classes: Caseins (80%) and Whey proteins (20%). (7) Caseins are precipitated out by chymosin (rennin) or the acidification of the Milk to pH 4.6, forming the coagulum (curd). The Whey or Lactoserum remains soluble in the Milk serum. Lactoserum constitutes approximately 20% of the CMPs, and coagulum approximately 80% of the CMPs. Caseins and Whey proteins show very different physico-chemical and allergic properties.
Coagulum contains the Casein fraction, comprising 4 proteins: aS1-, aS2-, ß- and ?-caseins (alphaS1-, alphaS2-, beta- and kappa-caseins). Lactoserum contains mainly the globular proteins BLG and a-lactalbumin (alpha- lactalbumin, or ALA), followed by minor constituents such as Bovine serum albumin (BSA), Lactoferrin (LF), immunoglobulins (Ig) and proteosepeptone. BLG and ALA are the major constituents and are synthesised in the mammary gland. Others (such as BSA, Lactoferrin and immunoglobulins) come from the blood. Proteosepeptone is derived from Milk proteins through the action of indigenous enzymes, the most significant of which are the hydrolases, such as the lipoprotein lipase, plasmin, and alkaline phosphatase. (8) In addition to the abovementioned proteins, proteolytic fragments of Casein and fat globule membrane proteins have been reported to occur in this fraction. (9)
The main characteristics of the major Milk proteins are presented in Table 1. (10, 11)
Table 1. Main Characteristics of the Major Bovine Milk Proteins. (5)
Molecular weight (kDa)
20% Whey (approximately 5 g/L)
10% BLG (Bos d 5)
5% ALA (Bos d 4)
3% Immunoglobulins Bos d 7
1% BSA (Bos d 6)
Traces of Lactoferrin
80% Whole Casein (Bos d 8) (approximately 30 g/L)
Abbreviations: ALA, a-lactalbumin; BLG, ß-lactoglobulin; BSA, Bovine serum albumin.
It was classically accepted that the major allergen in Cow’s milk allergy is BLG, but subsequent research has proved that sensitivity to the various Cow’s milk proteins is distributed widely. (7, 12, 13)
BLG is the most abundant protein in Whey, accounting for 50% of total protein in the Lactoserum fraction. It has no homologous counterpart in human milk. For a review of BLG, see Beta-lactoglobulin f77.
ALA is a monomeric globular calcium-binding protein representing about 25% of Lactoserum (Whey) proteins. It is a regulatory component of the enzymatic system of galactosyl transferase responsible for the synthesis of lactose in mammary secretory cells.
For a review of ALA, see Alpha-lactalbumin f76.
Bovine serum albumin (BSA)
BSA accounts for around 5% of the total Whey proteins. BSA is physically and immunologically very similar to human blood serum albumin. Its main role is the transport, metabolism and distribution of ligands, and protection from free radicals. (11)
For a review of BSA, see Bovine serum albumin e204.
LF is a protein of mammary origin and is a Milk-specific iron-binding glycoprotein of the Transferrin family. It can be found in the Milk of most species, at levels lower than 1%. LF is present in much higher concentrations in human breast milk (and particularly in colostrum) than in Bovine milk. Although it is present in very low concentrations in Cow's milk, it has been shown to be an important allergen.
For a review of LF, see Lactoferrin f334.
The Immunoglobulin (Ig) fraction, which includes IgG and IgE, accounts for about 1% of total Milk protein and 6% of Whey protein. The basic structures of Ig in Bos species are very similar to those in humans, possessing a basic ‘Y- shaped’ unit composed of 4 polypeptide chains linked through intra- and intermolecular disulfide bonds. (8) Three IgG classes in Cattle have been recognised as IgG1, IgG2, IgG3. (14) Data on the potential allergenicity of Bovine immunoglobulins is very limited. However, some studies propose IgG as another Milk allergen due to the observation that IgE from CMA patients specifically binds Bovine IgG. (15) Bovine IgG has been reported to be a major Beef allergen. (16)
The proteose-peptone fraction represents about 1.1% of the total Milk protein. It is a heat-stable and acid-soluble protein fraction of Milk with important functional properties. This Milk component is derived mainly from the proteolysis of Beta-casein, and the enzymatic activity of plasmin over time can increase its concentration in Milk. (8)
The coagulum consists of the whole Casein fraction (i.e. the solid fraction of proteins obtained after coagulation of Milk). It is subdivided into a number of families, of which the most important are the aS1-, aS2-, ß-, ?- and ?-caseins (AlphaS1-, AlphaS2-, Beta-, Kappa- and Gamma-caseins). (8) Each individual Casein represents a well-defined chemical compound, but they cross-link to form ordered aggregates or nanoclusters (i.e. micelles) that assemble into larger structures, forming Casein micelles characterised by a central hydrophobic part and a peripheral hydrophilic layer in suspension in Lactoserum (Whey). (17, 18) Their proportion in the micelles is relatively constant at approximately 37%, 13%, 37% and 13%, respectively.
For a review of Casein, see Casein f78.
The following allergens have been characterised to date:
- Bos d Lactoferrin. (11, 26, 46, 47, 62)
- Bos d Lactoperoxidase. (63, 64, 65)
Other Cow allergens not found in Cow’s milk but only in Cow dander or meat (Beef) include:
- Bos d 2, lipoclalin.
- Bos d 3, calcium binding protein.
- Bos d OBP, Odorant Binding Protein.
The main characteristics that should be emphasised are the multiplicity and diversity of proteins that are involved in Cow's milk allergy (CMA). Polysensitisation to several proteins occurs most often, and all Milk proteins appear to be potential allergens. (5) A great variability is observed in the affinity, specificity and magnitude of IgE responses in patients’ sera. (66) Most Milk-allergic patients are sensitised to several proteins, including BLG (Bos d 5), Casein (Bos d 8), ALA (Bos d 4), BSA (Bos d 6), Lactoferrin, and Immunoglobulins (Bos d 7). (66, 67, 68, 69, 70, 71, 72, 73, 74) Great variability is observed in IgE response. (5)
Casein and BLG, as well as ALA, are major allergens. However, proteins present in very low quantities (such as BSA, immunoglobulins, and especially Lactoferrin) also appear to be important, since 35% to 50% of patients are sensitised to those proteins – and sometimes to those proteins only. (71) In the last few years, sensitivity to Casein has increased in terms of both frequency and intensity of IgE response. (5) Sensitisations to Casein, BLG and ALA are closely linked. In contrast, sensitivity to BSA appears to be completely independent, with 50% of patients being allergic to BSA regardless of their sensitivity to other Milk allergens. (5)
The role of various Cow's milk proteins (CMPs) in the pathogenesis of CMA is still controversial. Sera from 20 Milk-allergic subjects have been used for Cow's milk major allergen identification. The prevalence of CMP allergens has been measured as the following: 55% Alpha(s1)-casein, 90% Alpha(s2)-casein, 15% Beta-casein, 50% Kappa-casein, 45% Beta-lactoglobulin, 45% BSA, 95% IgG-heavy chain, 50% Lactoferrin, and 0% Alpha-lactalbumin. (75)
See the review for each component: Casein f78, Beta-lactoglobulin f77, Alpha-lactalbumin f76, Bovine serum albumin e204 and Lactoferrin f334.
Possible Effects of Processing on Allergenicity
Heat and digestion contribute to the structure and other properties of CMPs, as well as to the IgE-binding epitopes. Casein is thermostable, whereas BLG is thermolabile. However, BLG may be protected through interaction with Casein. Furthermore, the food matrix may play an important role in the allergenicity of Milk. Formation of aggregates may increase the allergenicity of the heated product. Boiling of Milk for a few minutes (2, 5, or 10 minutes) results either in no difference or in a reduction of approximately 50% to 66% of the positive reactions, compared with those for raw Milk; similar observations have been reported with raw versus pasteurised or homogenised and pasteurised Milk. (5, 69, 76, 77, 78) Casein has been shown to resist digestion, particularly Kappa- and Alpha(s2)-casein. Resistant areas corresponded to fragments that were hydrophobic at pH 3.0 (gastric conditions) and/or carrying post-translational modification. Milk processing led to differences in peptide patterns; and heat treatment of milk tended to increase the number of peptides found in digested samples, highlighting the probable impact of milk processing on the allergenic potential of caseins. (79)
Hydrolysis of Milk proteins is thought to considerably reduce their allergenicity. However, several studies have shown that specific IgE from patients with Milk allergy recognised enzymatic digestion products of Whey proteins (e.g. BLG and ALA) and Casein, and that the recognition of peptides may be even better than in the case of the intact molecule. (56, 80, 81, 82, 83) For example, the incidence of reported adverse effects in infants fed partially-hydrolysed Milk formulae is reported to be approximately 45%, and in those fed extensively-hydrolysed Milk formulae (either Casein or Whey), the incidence ranges from approximately 65% to 15%, respectively. (84, 85, 86) Partially-hydrolysed formulae may cause allergic reactions due to the presence of residual native protein, or of large fragments. Reactions to extensively-hydrolysed formulae have been shown to result from short peptidic fragments that still contain the relevant IgE-binding epitopes, which are exposed during the proteolysis. (5)
Characterisation of Epitopes on CMPs
Although the 3-dimensional structures of Cow’s milk allergens play an important role in Cow’s milk protein allergenicity, the presence of sequential epitopes on peptides of various sizes, from as short as approximately 12 to 14 amino acid residues (i.e. approximately 1.5 kDa), has been demonstrated to be significantly allergenic. The most allergenic and prevalent peptides are BLG fragments, and these have been reported to be recognised by more than 90% of the patients. (5) Numerous IgE- and IgG-binding epitopes of BLG and ALA exist, and these result in a variability of the antibody responses to various regions of the molecules. Interestingly, the authors correlate the presence of IgE to multiple linear epitopes with persistent (versus transient) Milk allergy, and suggest that this could be a good marker for identifying the patients who would have a lifelong Milk allergy.
Polysensitisation also appeared to be due to cross-sensitisation mechanisms. Interestingly, Bovine Beta-casein induces a high IgE response, despite the fact that it is also abundant in human Milk and that human and Bovine Beta-caseins share a high sequence homology. (5)
Conserved regions shared by both Bovine and human beta-caseins (and particularly those comprising clusters of phosphorylated seryl residues) are responsible for IgE cross-reactivity. Some of the major epitopes already characterised on AlphaS-caseins are continuous epitopes that have also been located in hydrophobic regions of the molecule, where they are not accessible to antibodies unless the Casein is denatured or degraded; as, for instance, during digestion. (87) Also, differences are found in the anti-Casein IgE capacity to bind different epitopes of AlphaS2-casein across 2 groups of patients with persistent or transient CMA. (87)
The presence of shared allergens in Milk, meat, and dander from Cow has been demonstrated. Sensitivity to Cow's milk does not usually entail sensitivity to Beef or inhaled Cow dander. However, the presence of common allergens in Milk, meat and dander has been demonstrated. (88, 89)
There is cross-reactivity between Cow's milk and Milk from related animals. (90)
The same or closely homologous proteins and their variants are present in Milk of other ruminant species. However, the polymorphism of Milk proteins is genetically determined, and of great importance in specifying the origin of Milk and in animal breeding. For example, Variant C of BLG is found only in the Jersey breed of Cow.
The gross composition of Cow’s, Sheep’s and Goat’s milk may appear to be very similar, but slight differences in fat, solid (non-fat) and protein fractions result in changes in biological and physico-chemical properties. Sheep’s milk contains almost twice as many solids as Cow’s milk and has a higher Casein and fat content. The higher proportion of medium- or short-chain saturated fatty acids is believed to lead to greater lactose absorption, which might benefit the mildly lactose intolerant. (8)
Goat’s milk proteins have many significant differences in their amino acid composition, compared to the Milk proteins of other mammalian species. The relative proportions of the various Milk proteins also differ in Goat’s and Cow’s milk. For example, Goat’s milk may contain only trace amounts of the allergenic Casein protein alphaS1-Casein, whereas beta-Casein represents the most abundant protein in Goat’s milk. (8)
Of particular importance is the fact that the same Caseins are present, with high sequence homologies, varying from 80% to more than 90%. As a consequence, a high IgE cross-reactivity among Sheep's, Goat’s, and Cow's milk Casein occurs in most patients with CMA. (91, 92, 93, 94) However, the IgE response may also be specific, with allergic reactions to Goat's and Sheep's milk without associated CMA, (95, 96) and with manifestations that occur after ingestion of Sheep's and Goat's cheese but not Cow's milk or other dairy products. (97)
Cross-reacting allergens other than proteins from Milk of other species may also exist. Mare's or Donkey's milk may be tolerated by some individuals. (98, 99) However, there is not universal consensus on this, with some authors suggesting that processing of Donkey’s milk may attenuate the allergenicity of the product and that close homology exists between certain Cow’s and Donkey’s milk allergens, in particular heat-labile allergens. (100) Reindeer milk also contains beta-lactoglobulin; however, partial cross-reactivity of human anti-cow’s milk IgE with reindeer beta-lactoglobulin suggests that it lacks important bovine epitopes, and those that are recognised are only weakly bound. (101)
Adverse reactions have been reported in Milk-allergic patients fed Soy-based formulae as Cow's milk substitutes. (102) This may be as a result of the Cow’s milk-allergic individual commonly also being allergic to Soy protein, or as a result of cross-reactivity with a specific cross-reactive protein present in Soy: a 30-kDa glycinin-like protein from Soybean that cross-reacts with Cow's milk Casein has been isolated and partially sequenced. (103)
Cow's milk is a major cause of adverse reactions in infants. Cow’s milk-induced asthma is often observed in infants with food hypersensitivity. In fact, asthma has been noted in 7-29% of those sensitive to Milk. (104) Milk is often described as a cause of rhinoconjunctivitis in young children, and a role for food allergy in serous otitis media has also been proposed. (104) Cow's milk allergy in infants has a much better prognosis than in older children or adults. (105) Onset of IgE-mediated allergy in a patient aged 29 has been described. (106)
Cases have been reported of allergic reactions to non-dairy or pareve (no Milk or meat) products containing Milk proteins, either through contamination during processing or through the addition of sodium caseinate. (107, 108)
In a study in Japan using the Pharmacia CAP System, the clinical sensitivity for Milk was 95% and the specificity was 93%. (109) It has been found that Cow's milk-allergic children developed IgE antibodies to Milk before the onset of clinical allergy, indicating that in vitro measures can be good predictive tools. (110) High levels of specific IgE antibodies against Milk proteins were reported in 6-month-old infants with Cow’s milk allergy. The levels were further elevated in children with persistent problems at 12 months, but fell in children on Milk-free diets. (72) Milk protein-specific IgE antibody levels correlate with development of tolerance to Milk. (111) IgE antibodies to Milk proteins were rarely found in a normal Japanese population. IgG antibody levels to the same proteins were influenced by age and feeding habits, peaking at between 5 and 12 months of age, and decreasing to undetectable in normal adults. (112)
The symptoms in infants are usually gastrointestinal (GI) and dermatological, with dermatitis often appearing early. A study described 2 different groups of infants: those who react immediately with GI symptoms and urticaria and who are often atopic, with positive skin-prick tests and Milk-specific IgE antibodies; and the late responders, who may have a non-IgE-mediated allergy. (113) In children retaining Milk allergy, cutaneous symptoms decrease while respiratory and GI symptoms increase with age (4-14 years). (111, 114) Infants with early sensitisation to Cow's milk proteins have an increased risk for later development of other food allergies and for sensitisation to inhalant allergens. (115, 116) A retrospective study of adults with Milk and cheese allergy showed that the majority of the patients were women with symptoms involving the respiratory tract or the skin. Many of them suffered their first symptoms in relation to pregnancy, and most of them remained monosensitised to Milk proteins, primarily Casein. (117) Inhaled Milk proteins may cause occupational asthma in workers handling powdered proteins, (118, 119) as well as in people milking animals. (120) Gastrointestinal symptoms in adults after Milk consumption are often caused by lactase deficiency resulting in lactose intolerance, but may also be immune reactions to the Milk proteins, with or without involvement of IgE antibodies. (121)
Reports of prevalence range from 0.5 to 7.5% in infants. (105) Some patients retain the allergy their entire lives. (120) May et al. found that children hypersensitive to another food were likely to have a greater antibody production to Milk than those children who were not hypersensitive. (122)
Prevention and elimination
There are many studies supporting avoidance of Cow's milk and prolonged breastfeeding as preventive measures. In a report on a prevention program in Denmark, breastfeeding or a hypoallergenic formula and avoidance of other foods during the first 6 months of life had a protective effect. (123) The authors reviewed 10 prospective studies, almost all of which showed a reduction of atopic dermatitis and wheeze when preventive measures were taken. (123) In a follow-up study of the effects of maternal antigen avoidance after 4 years, the authors found that avoidance of Cow’s milk, fish and Hen’s egg during the first 3 months of lactation decreased both the current prevalence and the cumulative incidence of atopic dermatitis at age 4 in atopic children. (124) High IgG antibody levels against ß-lactoglobulin in atopic dermatitis were found to be predictive of a positive response to a Milk exclusion diet. (125, 126)
There are many proteins in Milk; six are of major interest. These include: Bovine serum albumin, gamma globulin, a-lactalbumin, ß-lactoglobulin, Lactoferrin and Casein. Reactions to separate proteins are uncommon. (127) Ordinary industrial treatment of Milk does not remove proteins and only partially reduces allergenicity. Undegraded allergens are often present in hydrolysed Milk formulas and may cause symptoms in already-sensitised subjects. (128, 129, 130) Intact Cow's milk proteins may pass from the gut into the circulation. High concentrations of a-lactalbumin were measured in sera of children with Cow's milk allergy, (131) and Bovine IgG was found in breast milk from mothers on diets including Cow’s milk. (132)
It is evident that very low amounts of Cow’s milk protein may elicit an adverse response. Severe reactions have also been reported after ingestion of Casein used, for example, as a texturing agent in meat products at concentrations ranging from 1.1% to 0.04%. (133) In reports of breast-fed infants experiencing severe reactions, the concentrations of contaminating CMPs were as low as 0.5 to 50 ng/mL, and reportedly reactions often occurred at approximately 5 ng/mL. (134, 135, 136, 137) BLG from ingested Cow's milk has been demonstrated to be absorbed through the mother’s gut mucosa and was detected in human milk. BLG was also said to be responsible for colic in breast-fed infants. (138, 139, 140) Similarly, frozen desserts containing unexpected trace amounts of Whey proteins (9 microg/mL), probably as a result of cross-contamination at the factory, resulted in anaphylaxis in a 3-year-old boy. (141) Food-quality lactose containing trace amounts of CMPs may be present in baby food expected to be free of CMPs, and may cause failure to thrive, digestive troubles, and coughing. (142) Anaphylaxis to lactose-containing medications contaminated by Milk protein has also been reported. (143)
Other reactions include lactase deficiency (or lactose intolerance) and other immune reactions without IgE antibody involvement.
Compiled by Dr Harris Steinman, email@example.com
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