• Journal of Dairy Science and Biotechnology
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• 제26권1호
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• pp.27-36
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• 2008

This review was written to introduce updated data on the structure and function of the major milk proteins identified as allergens, the characterization of their epitopes in each allergenic milk proteins, and the reduction of milk protein allergenicity. Most mammalian milk protein, even protein present at low concentration, are potential allergens. Epitopes identified in milk proteins are both conformational(structured epitope) and sequential epitopes(linear epitope), throughout the protein molecules. Epitopes on casein and whey proteins are reported to be sequential epitope and conformational epitopes, respectively. Conformational epitopes on whey protein are changed into sequential epitope by heat denaturation during heat treatment. Several methods have been proposed to reduce allergenicity of milk proteins. Most ideal and acceptable method to make hypoallergenic milk or formula, so far, is the hydrolysis of allergenic milk proteins by enzymes that has substrate specificity, such as pepsin, trypsin, or chymotrypsin. Commercial formulas based on milk protein hydrolysate are available for therapeutic purpose, hypoantigenic formula for infants from families with a history of milk allergy and hypoallergenic formula for infants with existing allergic symptoms.

• Current Research on Agriculture and Life Sciences
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• 제31권2호
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• pp.108-112
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• 2013

Nuts are one of the most common sources of allergies in individuals of all ages. In order for a particular protein to render an allergic reaction, it must resist proteolytic digestion by intestinal enzymes. In this study, three well-known allergenic nuts, almonds, cashew nuts, and peanuts, were used as samples, and enzyme digestion with Bacillus protease and porcine pepsin was tested. A proteomic approach using two-dimensional gel electrophoresis and an MS/MS analysis was applied to visualize and identify the proteins that were resistant to enzyme digestion. Among the 150 protein spots tested, 42 proteins were assigned functions. Due to the lack of genomic databases, 41% of the identified proteins were grouped as hypothetical. However, 12% of them were well-known allergens, including AraH. The remainder were grouped as storage, enzymes, and binding proteins.

• Journal of Plant Biotechnology
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• 제42권2호
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• pp.123-128
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• 2015

Pregermination treatment of cocoa beans either with the testa, group PCB (+T), or without the testa, group PCB (-T), was studied here to determine whether this treatment (incubation up to 120 h at $25^{\circ}C$) has any effect on the levels of allergenic proteins or on chemical composition. Our proximate analysis included carbohydrates, proteins, and lipids. We used western blotting to measure changes in the amounts of allergenic proteins in the cocoa beans during the pregermination treatment. The protein and carbohydrate content of both groups (with or without the testa) decreased slightly during this treatment, whereas lipid content increased. Group PCB (-T) showed more rapid metabolic processes than did group PCB (+T) during the pregermination treatment. Western blot analysis showed that the cocoa beans contained an allergenic protein of ~28 kDa. Removal of the testa strongly reduced the amount of this allergenic protein after 72 h of the pregermination treatment. Generally, the pregermination treatment increased antioxidant activity in both groups. Significant differences in the antioxidant activity were observed between groups PCB (-T) and PCB (+T). Particularly, group PCB (-T) showed high antioxidant activity at 72 h of the pregermination treatment. Thus, the combination of cocoa beans without the testa and pregermination treatment (72 h) seems to be the optimal method for production of hypoallergenic cocoa beans rich in antioxidants for patients with allergic disorders.

• Animal cells and systems
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• 제8권Supplyment
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• pp.73-73
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• 2004

• Nutrition Research and Practice
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• 제7권1호
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• pp.3-8
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• 2013

Buckwheat is known as a health food but is one of the major food allergens triggering potentially fatal anaphylaxis in Asia, especially in Japan and Korea. This study was conducted to investigate the characteristic of enzymatic resistance of buckwheat protein and allergenic potential. Enzymatic resistance of buckwheat protein was performed with in vitro digestibility test in simulated gastric fluid (SGF), pH 1.2, using pepsin and simulated intestinal fluid (SIF) using chymotrypsin. Reactivity of buckwheat proteins to human IgE was performed using six allergic patients sensitized to buckwheat. Buckwheat's IgE levels were measured using the Phadia UniCAP-system. Buckwheat protein, 16 kDa, still remained after 30 min treatment of pepsin on SDS-PAGE. Even though 16 kDa almost disappeared after 60 min treatment, two out of the six buckwheat patients' sera showed reactivity to hydrolysate after 60 min treatment, indicating that allergenicity still remained. In simulated intestinal fluid (SIF) using chymotrypsin, buckwheat protein, 24 kDa, showed resistance to hydrolysis with chymotrypsin on SDS-PAGE, and still had allergenicity based on the result of ELISA. Our results suggest that buckwheat proteins have strong resistance to enzyme degradation. This may be attributed in part to the allergenic potential of buckwheat. Further study should be continued regarding buckwheat allergy.

• Food Science and Biotechnology
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• 제15권4호
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• pp.523-528
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• 2006

The digestibility of heat- or high-pres sure-treated beef extracts was evaluated with an in vitro simulated gastric digestion model and each sample also underwent immune assay to detect its antigenicity with the sera of beef allergic patients. Heat treatment of the beef extracts considerably decreased their digestibility, whereas high-pressure treatment at 200 MPa improved their digestibility compared with the control, but the difference was not significant. The digestibility of the high pressure-treated beef extract was generally higher than that of the heat-treated samples. Depending on the degree of digestion, the degree of antigenicity of the main beef allergens decreased. On the basis of these results, we hypothesized that the allergenicity of beef could be eliminated if the allergenic proteins are sufficiently digested in the digestive organ, leading to the suggestion that the digestibility of allergenic proteins must be improved in food processing. In conclusion, high-pressure processing is a more acceptable food processing technique for beef considering its digestibility.

• Journal of Dairy Science and Biotechnology
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• 제30권1호
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• pp.17-22
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• 2012

Since the prevalence of allergies is increasing, food allergy is a major concern for consumers, as well as for the food industry. The foods that account for over 90% of all moderate to severe allergic reactions to food are milk, eggs, peanuts, soybeans, fish, shellfish, wheat, and tree nuts. Of these food allergens, milk is one of the major animal food allergens in infants and young children. Milk is the first food that an infant is exposed to; therefore, the sensitization rate of milk in sensitive individuals is understandably higher. The mechanisms involved in allergic reactions caused by this hypersensitivity are similar to those of other immune-mediated allergic reactions. The reactions occur in the gastrointestinal tract, skin, and respiratory tract, with headaches and psychological disorders occurring in some instances. The major allergenic proteins in milk are casein, ${\beta}$-lactoglobulin, and ${\alpha}$-lactalbumin, while some of the minor allergenic proteins are lactoferrin, bovine serum albumin, and immunoglobulin. Reliable allergen detection and quantification are essential for compliance with food allergen-labeling regulations, which protect the consumer and facilitate international trade.

• Nutritional Sciences
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• 제9권4호
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• pp.317-322
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• 2006

Soybeans are well-known as allergenic foods. Koreans consume large amounts of soybean foods, such as kochujang, which have gone through the fermentation process. To lower the allergenicity of these foods, we prepared hypo allergenic kochujang with aloe extract (AK). A sensory evaluation was conducted along with a clinical evaluation that used a double-blind, placebo-controlled food challenge (DBPCFC) test These tests were designed to evaluate the acceptability of the fermented foods. In comparison to normal kochujang (NK), AK elicited a higher sensory test score, and the rate of positive reactions in atopic dermatitis patients during the DBPCFC test was reduced. Methods of protein extraction, protein quantitation with sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), and protein identification using two-dimensional (2D) gel electrophoresis were performed for both NK and AK to compare the functional factors. We found a reduction in the levels of high molecular proteins even though the bands of the proteins had not entirely disappeared, indicating that the boiling and fermentation process changed the soybean protein patterns. The rate of the reduction of high molecular proteins was more effective in the AK. In conclusion, AK can be recognized as a food with hypoallergenic effect.

• Asian Journal of Atmospheric Environment
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• 제6권1호
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• pp.33-40
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• 2012

In this study, we characterized the physical form of allergenic Cry j 1 in the urban atmosphere. Through an immunofluorescence antibody method, we showed that allergenic Cry j 1 exists as fine particles (${\leq}1.1{\mu}m$). To determine Cry j 1 concentrations and its particle size distribution, we used the ELISA method to confirm that most Cry j 1 exists as fine particles in the urban atmosphere and is found at high concentrations on fine day next to rainy day. Furthermore, we evaluated Cry j 1 denaturation by using the Biacore J system based on the surface plasmon resonence (SPR) principle and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). We showed that the dissociation constant ($K_D$) of Cry j 1 that has been exposed to urban polluted air is lower ($1.76{\times}10^{-14}$ M) than that of Cry j 1 ($1.32{\times}10^{-9}-3.37{\times}10^{-9}$ M) of original pollen grains that has not been exposed to air pollutants. Cry j 1 turns into low molecular weight proteins by reacting with various acidic solutions. In sum, we showed that allergenic Cry j 1 exists as fine particles that can deposit in the lower respiratory tract. This finding clarifies the relationship between Japanese cedar pollinosis and air pollutants.

• Food Science and Biotechnology
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• 제17권2호
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• pp.357-361
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• 2008

One of the major allergenic proteins in common buckwheat (Fagopyrum elculentum) was found to be a BW10KD. In this work, allergenic BW10KD genomic DNAs from the native common buckwheat 'Pyeongchang' and Tartarian buckwheat 'Clfa47' were cloned by polymerase chain reaction (PCR), and their nucleotide sequences were determined. In addition, a novel PCR assay targeting the allergenic BW10KD gene was developed to detect and differentiate both buckwheat species in food. The nucleotide sequences of the BW10KD genomic DNA from 'Pyeongchang' and 'Clfa47' were 94% identical. Base differences in the nucleotide sequences of the BW10KD genes are probably useful as a molecular marker for species-specific identification. The 'Pyeongchang'-specific primer set 154PF/400PR and the 'Clfa47'-specific primer set 154DF/253DR generated 247 and 100 bp fragments in singleplex PCR, respectively. A duplex PCR assay with 2 species-specific primer sets simultaneously differentiated the 'Pyeongchang' and 'Clfa47' in a single reaction. The PCR assay also successfully allowed for the rapid detection of buckwheat ingredients in foods.