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http://dx.doi.org/10.5352/JLS.2012.22.11.1487

Cross-Reactivity and Digestive Enzyme Stability of Peach, Korean Cherry, and Hot Pepper  

Kim, Eun-Jung (Division of Applied Life Science (BK21 program), Institute of Agriculture and Life Science, Gyeongsang National University)
Ko, Yu-Jin (Division of Applied Life Science (BK21 program), Institute of Agriculture and Life Science, Gyeongsang National University)
Lee, Gyeong-Ran (Division of Applied Life Science (BK21 program), Institute of Agriculture and Life Science, Gyeongsang National University)
Seol, Hui-Gyeong (Department of Environmental Toxicology & Chemistry, Korea Institute of Toxicology)
Kang, Chang-Min (Department of Environmental Toxicology & Chemistry, Korea Institute of Toxicology)
Ryu, Chung-Ho (Division of Applied Life Science (BK21 program), Institute of Agriculture and Life Science, Gyeongsang National University)
Publication Information
Journal of Life Science / v.22, no.11, 2012 , pp. 1487-1492 More about this Journal
Abstract
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.
Keywords
Peach; Korean cherry; hot pepper; cross-reactivity;
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