Cow milk allergy is one of the common food allergies. Our previous study showed that the allergenicity of fermented milk is lower than that of unfermented skimmed milk in vitro, and the antigenicity of β-lactoglobulin and α-lactalbumin in fermented milk was decreased by 67.54% and 80.49%, respectively. To confirm its effects in vivo, allergic BALB/C mice model was used to further study the allergenicity of fermented milk. It was found that compared with the skim milk (SM) group, the intragastrically sensitization with fermented milk had no obvious allergic symptoms and the fingers were more stable: lower levels of IgE, IgG, and IgA in serum, lower levels of plasma histamine and mast cell protein-1, and immune balance of Th1/Th2 and Treg/Th17. At the same time, intragastrically sensitization with fermented milk increased the α diversity of intestinal microbiota and changed the microbiota abundance: the relative abundance of norank-f-Muribaculaceae and Staphylococcus significantly decreased, and the abundance of Lachnospiraceae NK4A136 group, Bacteroides, and Turicibacter increased. In addition, fermented milk can also increase the level of short-chain fatty acids in the intestines of mice. It turns out that fermented milk is much less allergenicity than SM. PRACTICAL APPLICATION: Fermentation provides a theoretical foundation for reducing the allergenicity of milk and dairy products, thereby facilitating the production of low-allergenic dairy products suitable for individuals with milk allergies.

α-Casein (α-CN) is considered the main allergen in bovine milk. Lactic acid bacteria (LAB) fermentation can hydrolyze milk protein and therefore reduce the antigenicity. In this paper, a LAB reducing the antigenicity of casein, identified as LactiplantibacillusPlantarum 7-2 (L. plantarum 7-2), was primarily identified by screening for protein hydrolysis ability using a method involving the determination of released free amino acid with further selection for the ideal antigenicity-reducing capability by enzyme-linked immunosorbent assay (ELISA). In order to verify the capability of L. plantarum 7-2 in inhibiting antigenicity, the standard milk proteins α-LA, β-LG, α-CN, β-CN and κ-CN were cultured with L. plantarum 7-2 for 18 h; The results of SDS-PAGE show that all the bands corresponding to the full length tested proteins became unclear or completely disappeared indicating that these proteins were hydrolyzed by L. plantarum 7-2. Correspondingly, the antigenicities of α-CN and β-LG were significantly reduced. L. plantarum 7-2 demonstrated negative hemolysis and nitrate reductase capabilities and was sensitive to the commonly used antibiotics ampicillin clindamycin tetracycline chloramphenicol, and erythromycin, demonstrating that L. plantarum 7-2 could be used in dairy product fermentation to reduce the antigenicity of milk protein.

BACKGROUND: Milk protein allergy is one of the most common food allergies in infants. We aimed to test whether fecal calprotectin can be used to monitor food allergies in infants by comparing the fecal calprotectin levels in infants with a milk protein allergy before and after an intervention treatment.
METHODS: The study was designed as a prospective case-control trial. Stool samples were collected at follow-up, and the concentration of fecal calprotectin was determined using an enzyme-linked immunosorbent assay. The infant\'s weight and length were measured.
RESULTS: The allergic group comprised 90 milk-allergic infants (41 boys, 49 girls), and the nonallergic group comprised 90 nonallergic infants (51 boys, 39 girls). Compared with the fecal calprotectin level in the nonallergic group (median: 141 μg/g), that in the allergic group (median: 410 μg/g) was significantly higher (z = - 9.335, p < 0.001). After two dietary interventions and treatments, the fecal calprotectin levels of the infants with a milk protein allergy at the first (median: 253 μg/g) and second follow-up visits (median: 160 μg/g) were significantly lower than those before the intervention (z = - 7.884, p < 0.001 and z = - 8.239, p < 0.001, respectively). The growth index values (LAZ and WAZ) of the infants with a milk protein allergy at the first and second follow-up visits were significantly higher than those before dietary intervention (p < 0.05). Fecal calprotectin was negatively and significantly correlated with the WLZ and WAZ at the second follow-up visit (Spearman\'s rho = - 0.234, p = 0.01 and Spearman\'s rho = - 0.193, p = 0.03, respectively).
CONCLUSIONS: The level of fecal calprotectin in infants with a milk protein allergy decreased after dietary intervention and seems to be a promising biological indicator for monitoring intestinal allergies.

Hepatic portal venous gas (HPVG) is a rare imaging finding in infants and usually indicative of a severe disease process such as necrotizing enterocolitis, bowel ischemia, or bowel wall rupture / infarction. The diagnosis of HPVG may have serious implications such as parenteral nutrition, antibiotics and even surgery. In this case, we present an 8-week-old male with a history of prematurity presenting with HPVG, later concluded to be caused by milk protein allergy. Milk protein allergy is a rare cause of HPVG, but it should be recognized due to its benignity and potential prevention of unnecessary testing and interventions.

The authors describe a fluorometric aptamer based assay for detecting β-lactoglobulin by using carbon dots (C-dots) as a signal indicator. The aptamer was immoblized on magnetite (Fe3O4) nanoparticles (MNPs), and the C-dots served as a label for the complementary oligonucleotide (cDNA). The assay is based on the hybridization that takes place between aptamer and cDNA. In the presence of β-lactoglobulin (β-LG), the aptamer preferentially binds to β-LG, and this leads to a partial release of the C-dots-cDNA into the solution. After magnetic separation, the supernatant of the solution contains the released C-dots-cDNA which are quantified by fluorometry, best under excitation/emission wavelengths of 354/447 nm. Under the optimal conditions, the fluorescence intensity is proportional to the logarithm of the β-LG concentration in the 0.25 to 50 ng mL-1 range, with a 37 pg mL-1 detection limit. The method was successfully applied to the determination of β-LG in hypoallergenic formulations, and the results demonstrated that this assay is a promising tool in food quality control. Conceivably, it also provides the opportunity for detection of other analytes. Graphical abstract Schematic of a novel aptamer based fluorometric β-lactoglobulin assay based on the use of magnetite (Fe3O4) nanoparticles (MNPs) and carbon dots (C-dots). C-dots were used as a signal indicator and Fe3O4 MNPs acted as a magnetic separator. This assay exhibits high sensitivity and selectivity with a detection limit as low as 37 pg mL-1.

The legendary therapeutics properties of donkey milk have recently been supported by many clinical trials who have clearly demonstrated that, even if with adequate lipid integration, it may represent a valid natural substitute of cow milk for feeding allergic children. During the last decade many investigations by MS-based methods have been performed in order to obtain a better knowledge of donkey milk proteins. The knowledge about the primary structure of donkey milk proteins now may provide the basis for a more accurate comprehension of its potential benefits for human nutrition. In this aspect, experimental data today available clearly demonstrate that donkey milk proteins (especially casein components) are more closely related with the human homologues rather than cow counterparts. Moreover, the low allergenic properties of donkey milk with respect to cow one seem to be related to the low total protein content, the low ratio of caseins to whey fraction, and finally to the presence in almost all bovine IgE-binding linear epitopes of multiple amino acid differences with respect to the corresponding regions of donkey milk counterparts.

A two-step enzymatic approach to reduce immuno-reactivity of whey protein isolate and casein has been studied. The method involves partial hydrolysis of proteins with proteases, followed by repolymerization with microbial transglutaminase. Whey protein isolate partially hydrolyzed with chymotrypsin, trypsin, or thermolysin retained about 80%, 30%, and 20% of the original immuno-reactivity, respectively. Upon repolymerization the immuno-reactivity decreased to 45%, 35%, and 5%, respectively. The immuno-reactivity of hydrolyzed and repolymerized casein was negligible compared to native casein. The repolymerized products were partially resistant to in vitro digestion. Peptides released during digestion of repolymerized thermolysin-whey protein hydrolysate had less than 5% immuno-reactivity, whereas those of whey protein control exhibited a sinusoidal immuno-reactivity ranging from 5 to 20%. Peptides released during digestion of repolymerized thermolysin-casein hydrolysates had no immuno-reactivity. These results indicated that it is possible to produce hypoallergenic milk protein products using the two-step enzymatic modification method involving thermolysin and transglutaminase.

OBJECTIVE: To examine the prevalence, clinical features and influence on illness severity of cow\'s milk protein intolerance in young people with chronic fatigue syndrome.
METHODS: In a two-year prospective study of 55 adolescents and young adults with chronic fatigue syndrome, we defined intolerance to milk protein if subjects reported (i) no evidence of immediate or anaphylactic reactions to milk, (ii) at least 2 of the following 3 chronic symptoms: gastroesophageal reflux, early satiety and epigastric/abdominal pain, (iii) improvement in upper gastrointestinal symptoms on a milk protein elimination diet and (iv) at least 2 recurrences of upper gastrointestinal symptoms >two hours following open re-exposure to milk protein. Subjects completed three quality of life surveys at baseline and at six months.
RESULTS: The mean (SD) age of the 55 participants was 16.5 (2.1) years. Seventeen (31%; 95% CI, 19-43%) met study criteria for cow\'s milk protein intolerance. Compared to milk-tolerant subjects, milk-sensitive participants had significantly worse health-related quality of life at baseline but not at six months (after institution of the milk-free diet).
CONCLUSIONS: Cow\'s milk protein intolerance is a common problem in young people with chronic fatigue syndrome and is a treatable contributor to their symptoms.

Milk is an essential source of nutritionally excellent quality protein in human, particularly in vegan diet. Before consumption, milk is invariably processed depending upon final product requirement. This processing may alter the nutritive value of protein in a significant manner. The processing operations like thermal treatment, chemical treatment, biochemical processing, physical treatments, nonconventional treatments, etc. may exert positive or negative influence on nutritional quality of milk proteins. On one side, processing enhances the nutritive and therapeutic values of protein while on other side intermediate or end products generated during protein reactions may cause toxicity and/or antigenicity upon consumption at elevated level. The review discusses the changes occurring in nutritive quality of milk proteins under the influence of various processing operations.