• Journal of Dairy Science and Biotechnology
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• v.26 no.1
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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.

• Food Science of Animal Resources
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• v.20 no.2
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• pp.114-124
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• 2000

In this research the results showed that Evans blue stain causes vascular permeation at antibody injection site by the passive cutaneous anaphylaxis(PCA) screening of octpus minor so we concluded. Octopus minor causes allergy. Psedosciaena Polyactis, Raja Kenojei, Metapenaeus joyneri also showed allergenicity. Microwave and autoclaving appeared to reduced allergenicity(up to 99%) during the technological treatment processing. On the other hand, UV light didn't seem to change the protein structure of allergens affect the allergenicity. Therefore, the technological treatment processing of fish such as canning and microwave would possibly reduce the allergenicity. Among the ultrafiltration fraction of Octopus minor, Pseudosciaena Polyactis, Raja Kenojei and Metapenaeus joyneri, those fraction over 100,000 contained allergen and those under 100,000 and when screening allergenic fish went through 10,000~100,000 ultrafiltration, only the fraction of over 100,000 showed the anaphylactis activity for PCA. However whether screening fish would cause anaphylaxis in human or not is questionable. The future clinical experiment will verify this result with clinical experiment patients.

• Nutrition Research and Practice
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• v.8 no.3
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• pp.278-283
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• 2014

BACKGROUND/OBJECTIVES: Due to its beneficial health effects, use of buckwheat has shown a continuous increase, and concerns regarding the allergic property of buckwheat have also increased. This study was conducted for evaluation of the hydrolytic effects of seven commercial proteases on buckwheat allergens and its allergenicity. MATERIALS/METHODS: Extracted buckwheat protein was hydrolyzed by seven proteolytic enzymes at individual optimum temperature and pH for four hours. Analysis was then performed using SDS-PAGE, immunoblotting, and competitive inhibition ELISA (ciELISA) with rabbit antiserum to buckwheat protein, and direct ELISA with pooled serum of 21 buckwheat-sensitive patients. RESULTS: Alkaline protease, classified as serine peptidase, was most effective in reducing allergenicity of buckwheat protein. It caused decomposition of the whole buckwheat protein, as shown on SDS-PAGE, and results of immunoblotting showed that the rabbit antiserum to buckwheat protein no longer recognized it as an antigen. Allergenicity showed a decrease of more than 50% when pooled serum of patients was used in ELISA. Two proteolytic enzymes from Aspergillus sp. could not hydrolyze buckwheat allergens effectively, and the allergenicity even appeared to increase. CONCLUSIONS: Serine-type peptidases appeared to show a relatively effective reduction of buckwheat allergenicity. However, the antigenicity measured using rabbit antiserum did not correspond to the allergenicity measured using sera from human patients. Production of less allergenic buckwheat protein may be possible using enzymatic hydrolysis.

• Nutritional Sciences
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• v.9 no.4
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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.

• Preventive Nutrition and Food Science
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• v.6 no.4
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• pp.253-256
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• 2001

Irradiation of food is not only used for sanitation purposes but can be used for processing techniques to reduce or eliminate toxic or undesirable compounds on food. Irradiation wag effective to reduce the allergenicity of food by modification of the structure of proteins causing allergy reactions. Volatile N-nitrosmaine was reduced or eliminated by irradiation in the model system study and the breakdown products by irradiation did not recombine under human stomach conditions (pH 2,3, and 4,37$^{\circ}C$). The possibility of residual chlorophyll b reduction by irradiation was also found, and the model study indicated that irradiation be used to destroy chlorophyll b, resulting in protection from photooxidation in oil without acceleration of lipid oxidation during irradiation. In this paper, several on-going research projects for the application of food irradiation as a new processing technique are introduced, including reduction of food allergens, breakdown of volatile N-nitrosamine and residual chlorophyll b.

• Proceedings of the Korean Society of Food Hygiene and Safety Conference
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• 2003.05a
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• pp.20-35
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• 2003

• Journal of the Korean Society of Food Science and Nutrition
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• v.41 no.8
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• pp.1066-1071
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• 2012

In this study we investigated the change in antigenicity and allergenicity of Meju, a traditional Korean soybean product, by fermentation via 3 different microorganisms. The steamed soybeans were fermented with Lactococcus lactis subsp. lactis and/or Aspergillus oryzae and/or Bacillus subtilis. Proteins in soybean were degraded after fermentation. Antigenicity or allergenicity were analysed by immunoblotting and ELISA using soybean protein-specific polyclonal antibodies or soybean allergic patient sera. The best degradation was achieved by three step fermentation using nisin-producing Lactococcus lactis subsp. lactis IFO12007, A. oryzae and B. subtilis. Allergenicity and antigenicity were also starkly reduced after three step fermentation. The three-step fermentation method developed in our lab suggests an excellent alternative to reduce the allergenicity of soybeans.

• Genomics & Informatics
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• v.21 no.2
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• pp.25.1-25.12
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• 2023

Adaptation of infections and hosts has resulted in several metabolic mechanisms adopted by intracellular pathogens to combat the defense responses and the lack of fuel during infection. Human tuberculosis caused by Mycobacterium tuberculosis (MTB) is the world's first cause of mortality tied to a single disease. This study aims to characterize and anticipate potential antigen characteristics for promising vaccine candidates for the hypothetical protein of MTB through computational strategies. The protein is associated with the catalyzation of dithiol oxidation and/or disulfide reduction because of the protein's anticipated disulfide oxidoreductase properties. This investigation analyzed the protein's physicochemical characteristics, protein-protein interactions, subcellular locations, anticipated active sites, secondary and tertiary structures, allergenicity, antigenicity, and toxicity properties. The protein has significant active amino acid residues with no allergenicity, elevated antigenicity, and no toxicity.

• Food Science of Animal Resources
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• v.29 no.2
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• pp.238-244
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• 2009

Food allergy is a serious nutritional problem in both children and adults. Therefore, food allergenicity reduction methods are greatly needed. The allergenicity is altered by various manufacturing processes, and the digestibility of food proteins can be affected by food processing. This study was conducted to investigate the effect of in-vitro digestibility on the allergenicity of autoclaved market pork sausages using pepsin (30min) and trypsin (5, 30, 60, 90, and 120min). The binding ability of the porcine serum albumin (PSA) from sausages A and B significantly decreased by about 30 and 23%, respectively, after autoclave treatment (121; 5, 10, and 30 min). After the pepsin and trypsin treatments, the binding ability of products A and B at 30 min decreased. These competitive indirect enzyme-linked immunosorbent assay (ci-ELISA) results corresponded well with the sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting results. The results demonstrated that the allergenicity of pork sausages considerably decreased after autoclave treatment, and were also maintained or decreased after enzyme treatment. Accordingly, autoclave treatment represents a promising processing technology for the reduction of the allergenicity of diverse food products.

• Asian-Australasian Journal of Animal Sciences
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• v.22 no.2
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• pp.289-295
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• 2009

To develop a safer yogurt for immuno-compromised or allergy patients and to extend shelf-life, a plain yogurt was irradiated with doses of 0, 1, 3, 5, and 10 kGy using a gamma ray and the chemical and microbiological quality and allergenicity change were investigated. There was no difference in the content of protein, total solid, and amino acids of the plain yogurt by irradiation treatment and different storage temperatures (4, 20, and $35^{\circ}C$). The lactic acid bacterial counts of irradiated plain yogurt had approximately 3-decimal reduction at 3 kGy, and no viable cell at 10 kGy regardless of storage time and temperature. The binding ability of rabbit antiserum to milk proteins in irradiated plain yogurt showed that 10 kGy of irradiation produced significantly higher binding ability than other treatments. Sensory evaluation indicated that only appearance of the plain yogurt irradiated at 3 kGy or higher had a lower value than the non-irradiated control when stored at $20^{\circ}C$. Results suggest that irradiation of plain yogurt does not significantly affect the chemical and sensory quality of plain yogurt, but can extend the shelf-life, possibly reduce allergenicity, and provide a safer product.