Journal of Life Science (생명과학회지)

Korean Society of Life Science (한국생명과학회)
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Cross-Reactivity and Digestive Enzyme Stability of Peach, Korean Cherry, and Hot Pepper

복숭아, 앵두, 고추의 교차반응성 및 소화효소안정성

  • 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)
  • 김은정 (경상대학교 응용생명과학부(BK 21 프로그램).농업생명과학연구원) ;
  • 고유진 (경상대학교 응용생명과학부(BK 21 프로그램).농업생명과학연구원) ;
  • 이경란 (경상대학교 응용생명과학부(BK 21 프로그램).농업생명과학연구원) ;
  • 설희경 (안전성평가연구소.경남환경독성본부) ;
  • 강창민 (안전성평가연구소.경남환경독성본부) ;
  • 류충호 (경상대학교 응용생명과학부(BK 21 프로그램).농업생명과학연구원)
  • Received : 2012.08.11
  • Accepted : 2012.11.22
  • Published : 2012.11.30
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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.

복숭아는 오래 전부터 알레르기를 일으키는 식품으로 알려져 있으나 특정 식품과의 교차반응에 대한 연구는 부족한 실정이다. 본 연구에서는 한국에서 재배되고 있는 복숭아, 앵두, 고추의 단백질을 추출하여 복숭아 알레르기를 가진 환자가 앵두와 고추에 대해 교차반응성을 일으키는지 확인하고 이 단백질들의 소화효소처리에 따른 안정성을 조사하였다. 복숭아, 앵두 및 고추 단백질 추출물은 Tricine-SDS-PAGE상에서 3 kDa부터 26 kDa 이상까지 넓은 범위의 단백질 분포를 보였으나 각기 다른 패턴을 가지는 것을 확인하였다. 복숭아 단백질의 항원성을 확인하기 위해 복숭아 민감성 환자의 혈청과의 IgE반응성을 확인한 결과, 환자 혈청은 모두 복숭아의 주요 항원성 단백질 lipid transfer protein로 예상되는 9 kDa 부근에서 강한 IgE결합력을 보였으며 또한 9 kDa 단백질이 anti-LTP1 polyclonal antibody에 의해 검출되는 것을 확인하였다. 앵두와 고추 단백질 추출물은 23 kDa 부근에서의 IgE결합력이 9 kDa과의 반응성보다 크게 나타났다. 복숭아, 앵두 및 고추의 소화효소에 대한 안정성을 SDS-PAGE 상에서 확인한 결과, 복숭아, 앵두 및 고추의 항원성 단백질은 인공 위액 및 장액에 의해 완전히 분해되지 않아 알레르기를 유발할 잠재성이 있는 것을 확인할 수 있었다. 본 연구 결과를 바탕으로, 복숭아, 앵두 및 고추 단백질 추출물이 소화효소처리에 안정성을 가지는 특성을 가지며 복숭아 알레르기 증상을 가지는 사람에게 앵두 및 고추는 교차반응성을 일으킬 가능성이 크다는 것을 확인할 수 있었다.

Keywords

References

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