• Journal of Life Science
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• v.22 no.11
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• pp.1487-1492
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• 2012

Peach (Prunus persica) has been recognized as a food allergen for over 20 years. However, there is little information about cross-reactivity with other foods. The aim of this study was to research cross-reactivity of Korean cherry and hot pepper on patients allergic to peach and its stability by digestive enzyme treatment. Peach, Korean cherry, and hot pepper proteins were extracted and separated by Tricine-SDS-PAGE analysis. The protein extracts had a wide range of molecular weight, from 3 kDa to more than 26 kDa, and displayed different patterns of protein bands on Tricine-SDS-PAGE. Peach allergic patients' sera were used to detect the allergenic protein in three samples. Three peach allergic patients' sera reacted strongly with 9 kDa protein of peach, which was the expected lipid transfer protein (LTP) as the major allergen of peach and was detected with anti-LTP1 polyclonal antibody. However, the reactivity of the 23 kDa protein in Korean cherry and hot pepper protein was stronger than that of the 9 kDa protein. The stability of protein extracts on digestive enzyme treatment was examined using simulated gastric fluids (SGF) and simulated intestinal fluids (SIF), in which digestive enzyme stability is one of the characteristics of allergen potentially causing food allergy. Findings confirmed that allergenic proteins in peach, Korean cherry, and hot pepper were not completely digested by SGF and SIF treatments from results of SDS-PAGE analysis. These results confirmed that Korean cherry and hot pepper might cause cross-reactivity in peach allergic patients, and its allergenic proteins have stability against digestive enzymes.

• Korean Journal of Breeding Science
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• v.42 no.5
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• pp.502-506
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• 2010

Soybean seed possesses about 15 allergenic proteins recognized by IgEs from soy-sensitive human. The allergenic impact of soybean proteins limit its extensive usage in a broad range of processed foods. Soybean protein P34 or Gly m Bd 30k of the cysteine protease family is one of the major allergen of the soybean seed. P34-null soybean, PI567476, was identified among soybean (Glycine max & Glycine soja Sieb. and Zucc) of approximately 16,226 accessions from USDA soybean germplasm screened. Also, for P34 gene (Williams 82; whole genome sequence cultivar) and P34 null gene (PI567476) comparative analysis of sequences listed in the NCBI database showed the presence of a SSLP (Simple Sequence Length Polymorphism) of 4 base pair. So, a SSLP marker was designed to reveal the polymorphism of the locus. In this study, a population of 339 $F_2$ recombinant inbred lines generated by cross between Taekwang (Glycine max) and PI567476 was used to select $F_{2:3}$ plant of a P34 null gene. The result separation rate Taekwang type, heterozygous type and PI567476 type were shown in 85: 187: 67 since single gene is concerned in as the separation rate of 1:2:1 in $X^2{_{0.05}}=5.99$, df=2. In future, selected plant will identify protein level, whether P34 null protein is equal to P34 null gene.

• Asian-Australasian Journal of Animal Sciences
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• v.28 no.4
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• pp.559-567
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• 2015

Ex vivo digestion of proteins and fat in Red Chittagong Cattle milk from Bangladesh was carried out using human gastrointestinal enzymes. This was done to investigate the protein digestion in this bovine breed's milk with an especial focus on the degradation of the allergenic milk proteins; ${\alpha}_{s1}$-casein and ${\beta}$-lactoglobulin and also to record the generation of peptides. Lipolysis of the milk fat and release of fatty acids were also under consideration. After 40 min of gastric digestion, all the ${\alpha}_s$-caseins were digested completely while ${\beta}$-lactoglobulin remained intact. During 120 min of duodenal digestion ${\beta}$-lactoglobulin was reduced, however, still some intact ${\beta}$-lactoglobulin was observed. The highest number of peptides was identified from ${\beta}$-casein and almost all the peptides from ${\kappa}$-casein and ${\beta}$-lactoglobulin were identified from the gastric and duodenal samples, respectively. No lipolysis was observed in the gastric phase of digestion. After 120 min of duodenal digestion, milk fat showed 48% lipolysis. Medium (C10:0 to C16:0) and long (${\geq}C17:0$) chain fatty acids showed 6% to 19% less lipolysis than the short (C6:0 to C8:0) chain fatty acids. Among the unsaturated fatty acids $C18:1{\sum}others$ showed highest lipolysis (81%) which was more than three times of $C18:2{\sum}all$ and all other unsaturated fatty acids showed lipolysis ranging from 32% to 38%. The overall digestion of Bangladeshi Red Cattle milk was more or less similar to the digestion of Nordic bovine milk (Norwegian Red Cattle).

• The Korean Journal of Food And Nutrition
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• v.19 no.3
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• pp.296-300
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• 2006

Immunoblotting and competitive indirect enzyme-liked immunosorbent assay(Ci-ELISA) was used for detection of ${\beta}$-lactoglobulin(BLG) in dairy products, such as milk, dried milk and fermented milk. In immunoblotting, human IgE weakly recognized proteins of fermented milk, but still responded to dried milk even though become weak. Rabbit polyclonal antibody to BLG, used as a model of antigen, and milk allergic patients' IgE was used in the ELISA. Reactivities of Abs were the highest in market milk. BLG in fermented milk was detected in a low content. This result indicates the fermented milk have the lowest BLG content and could be used as hypo-allergenic food for milk-allergic individual.

• Journal of Life Science
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• v.34 no.5
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• pp.313-319
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• 2024

Cultivars or genetic resources with a black seed coat and green cotyledons are rich in lutein, which can promote eye health, and anthocyanin, known for its numerous health benefits. However, mature seeds also contain P34, 7S α' subunit, and lectin proteins, which are allergenic and degrade quality. Here, we report the breeding of a new soybean line with a black seed coat, green cotyledon, and free of P34, 7S α' subunit, and lectin proteins. A total of 157 F₂ seeds with black seed coats and green cotyledons were selected by crossing a female parent with a brown seed coat, green cotyledon, and lacking the 7S α' subunit and lectin proteins with a male parent with a black seed coat, green cotyledon, and lacking the P34 and lectin proteins. The P34 and 7S α' subunit proteins were consistent with a ratio of 9:3:3:1, indicating that they are independent of each other. From 14 F₂ seeds that were recessive (cgy1cgy1p34p34) for both proteins, one individual F₂ plant (F₃ seeds) with the desired traits-black seed coat, green cotyledon, and lacking P34, 7S α' subunit, and lectin proteins- was finally selected. The triple null genotype (absence for P34, 7S α' subunit, and lectin proteins) was confirmed in random F₃ seeds. The selected line has a black seed coat and green cotyledons, and when sown on June 14 in the greenhouse, the maturity date was approximately October 3, the height was about 68 cm, and the 100-seed weight was about 26.5 g.

• Journal of agriculture & life science
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• v.43 no.5
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• pp.39-42
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• 2009

Soybean is an important sources of plant proteins for human and animal nutrition. The use of soybean proteins has been expanded in the food industry due to their excellent nutritional benefits. But, Soybeans contain allergenic proteins that cause allergies to sensitive individuals. ${\beta}$-conglycinin(7S globulin) and glycinin(11S globulin) are the major components of storage protein in soybean. ${\beta}$-conglycinin consists of three subunits, ${\alpha}^{\prime}$, ${\alpha}$, ${\beta}$ and exhibits poorer nutritional and food processing properties than glycinin. There is a great deal of interest in the development of soybean lines with reduced amounts of ${\beta}$-conglycinin. The objective of this study was to determine the inheritance of ${\alpha}^{\prime}$-subunit protein in 7S globulin. F2 population was developed from the cross of "Jinpumkong2ho"(${\alpha}^{\prime}$-subunit presence) and PI506876(${\alpha}^{\prime}$-subunit absence) parent. Total 98 of F2 seeds were obtained and analyzed for the segregation of ${\alpha}^{\prime}$-subunit protein by SDS-PAGE. Among 98 F2 seeds, 70 F2 seeds showed ${\alpha}^{\prime}$-subunit protein and 28 F2 seeds did not show ${\alpha}^{\prime}$-subunit protein. The segregation ratios of 3 : 1 for presence and absence of ${\alpha}^{\prime}$-subunit protein were observed(${\chi}^2=0.667$, P=0.414). These data indicate that presence and absence of ${\alpha}^{\prime}$-subunit protein is controlled by a single major gene and might be useful for strain selection of 7S protein reduced soybean.

• Journal of Life Science
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• v.22 no.4
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• pp.524-531
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• 2012

Soybean is one of the most common food materials causing food hypersensitivity reactions in Korea. In this study, we have investigated the effect of roasting and fermentation on the allergenicity of soybean. Three kinds of soybean ($Daepung$, $Daewon$, and $Taegwang$) were prepared as raw, roasted, and fermented by $Bacillus$ $subtilis$ GSK 3580, and then their proteins were extracted. The proteins were separated using SDS-PAGE, and the detection of IgE specific to soybean proteins was performed by immunoblotting using 7 sera of soybean allergy patients and non-allergic control individuals. Serum specific IgE to soybean was measured by ELISA. The SDS-PAGE of raw soybean proteins showed various-sized bands ranging from 9 to 76 kDa, which are known as major allergens. In particular, 9, 21, 34, 52, 72, and 76 kDa proteins are known as LTP, Kunits trypsin inhibitor, $Gly$ m Bd 30K, ${\beta}$-subunit, ${\alpha}$-subunit, and ${\alpha}$'-subunit of ${\beta}$-conglycinin, respectively; these are major allergens in soybean. In contrast, only peptides of less than 35 kDa were found in roasted and fermented soybeans. IgE immunoblot analysis of three roasted species of soybeans commonly detected at 38-40 kDa and 10-15 kDa. The protein bands in fermented soybean showed very weak signals or were not detected. In addition, the reactivity of most patients' sera to soybean was decreased after roasting and fermentation. With these results, it may be concluded that the allergenicity of soybeans is reduced by the roasting and fermentation processes. It is supposed that allergenic proteins in soybean were degraded by heat treatment methods and proteolytic enzymes were secreted from fermenting microorganisms.

• Korean Journal of Food Science and Technology
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• v.41 no.3
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• pp.350-353
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• 2009

Peanut (Arachis hypogaea) often causes severe allergic reactions in sensitive people. Agglutinin is known to be one of the allergenic proteins in peanut. A polymerase chain reaction (PCR) method was developed to detect peanut ingredients in food using a primer pair corresponding to the agglutinin gene. This primer pair enabled PCR amplification of specific regions of agglutinin DNA from peanut, but not from 11 other nuts, beans, and cereals (pistachio, almond, sunflower seed, pine nut, walnut, soybean, black bean, kidney bean, azuki bean, rice, and black rice). The proposed PCR method successfully identified all of the 6 processed foods containing peanut whereas 13 other processed foods, which don't declare peanuts as an ingredient, were all negative. The detection limit of this method for purified peanut DNA was 100 pg/reaction. The sensitivity of this method was sufficient to detect peanut DNA in soybean DNA mixture which had been spiked with 0.1% peanut DNA.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.68 no.3
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• pp.114-120
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• 2023

Soybean is the one of the most important crops for providing quality vegetable protein to umans and livestock. Soybean cultivars with a brown seed coat have a wide range of antioxidant benefits because of the flavonoid components. However, they also contain lectin, 7S α′ subunit, lipoxygenase, and Kunitz trypsin inhibitor (KTI) proteins that can be allergenic and digestive inhibitors and reduce processing aptitude. Genetic removal of these four proteins is necessary in soybean breeding. Therefore, this study was conducted to select a new line with brown seed coat, green cotyledon, and tetra-null genotype (lecgy1lox1lox2lox3ti) for lectin, 7S α′ subunit, lipoxygenase, and KTI proteins in the mature seed. Five germplasms were used to create breeding population. From a total of 58 F₂ plants, F₂ plants with lele genotype were selected using a DNA marker, and F₃ seeds with a brown seed coat, green cotyledon, and the absence of 7S α′ subunit protein were selected. Three lines (S1, S2, and S3) were developed. Genetic absence of lectin, 7S α′ subunit, lipoxygenase, and KTI proteins was confirmed in F₆ seeds of the three lines, which had a brown seed coat, green cotyledons, and a white hilum. The 100 seed weights of the three lines were 26.4-30.9 g, which were lower than 36 g of the check cultivar - 'Chungja#3'. The new S2 line with 30.9 g hundred seed weight can be used as a parent to improve colored soybean cultivars without antinutritional factors such as lectin, 7S α′ subunit, lipoxygenase, and KTI proteins.

• Journal of the Korean Society of Food Science and Nutrition
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• v.38 no.1
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• pp.76-82
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• 2009

Wheat is the most widely cultivated cereal and an important source of dietary protein worldwide. Wheat allergy, defined as an adverse immunologic reaction to wheat, encompasses a broad spectrum of disorders with different pathomechanisms and clinical manifestation. The Nuruk, a traditional Korean Koji for brewing, was made with wheat flour and fermenting microbes such as bacteria, yeast and mold. The strains grown on Nuruk secrete various enzymes as amylase and protease. By the activation of such enzymes, starch and proteins in Nuruk are hydrolyzed to sugar and amino acid. Therefore, it is supposed to reduce allergic proteins in wheat. To study quality properties and degradation degree of allergenicity in Nuruk by fermentation, we investigated the changes of general ingredients and allergenicity in Nuruk during fermentation. Moisture contents was decreased from 24.2% to 13.6% during fermentation. Crude lipid and protein contents were gradually increased during fermentation. After 15 days of fermentation, reducing sugar and total sugar contents were reached its maximum level, and they were 27.45% and 39.00%, respectively. Acid and neutral protease activity were significantly increased during fermentation, but alkaline protease activity was not detected. ${\alpha}$-amylase activity was gradually increased and showed maximum level about 2,833.00 U/g after 15 days of fermentation. Glucoamylase activity was the highest level about 497.9 U/g after 10 days of fermentation. The increase of these proteolytic and saccharogenic enzyme activities will provide efficient condition for production of rice wine. Also, protein fractions were isolated from Nuruk, and degradation of these proteins during fermentation were confirmed by SDS-PAGE. IgE immunoblotting using patient's sera with wheat allergy was performed to confirm allergenic protein in Nuruk. These results as fermentation of Nuruk will provide a useful tool for developing safer wheat products to prevent wheat allergy.