Contribution of structural reversibility to the heat stability of the tropomyosin shrimp allergen

Masakatsu Usui, Akihito Harada, Takayuki Ishimaru, Emiri Sakumichi, Fumihiko Saratani, Chiho Sato-Minami, Hiroyuki Azakami, Taiko Miyasaki, Ken'ichi Hanaoka

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Tropomyosins are common heat-stable crustacean allergens. However, their heat stability and their effects on antigenicity have not been clarified. We purified tropomyosin in this study from raw kuruma prawns (Marsupenaeus japonicus) without heat processing. SDS-PAGE of the purified protein showed a band at approximately 35 kDa that cross-reacted with IgE from the serum of a shrimp-allergic patient, identifying it as Pen j 1. The circular dichroism spectrum of native Pen j 1 revealed the common α-helical structure of tropomyosins which easily collapsed upon heating to 80 °C. However, there were no insoluble aggregates after heating, and the protein regained its native CD spectral pattern after cooling to 25 °C. There was no significant difference in total IgG production between mice sensitized with native and heated Pen j 1. These results suggest that heat-denatured Pen j 1 refolded upon cooling and maintained its antigenicity following the heat treatment.

Original languageEnglish
Pages (from-to)948-953
Number of pages6
JournalBioscience, Biotechnology and Biochemistry
Volume77
Issue number5
DOIs
Publication statusPublished - Jun 12 2013
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Contribution of structural reversibility to the heat stability of the tropomyosin shrimp allergen'. Together they form a unique fingerprint.

  • Cite this

    Usui, M., Harada, A., Ishimaru, T., Sakumichi, E., Saratani, F., Sato-Minami, C., Azakami, H., Miyasaki, T., & Hanaoka, K. (2013). Contribution of structural reversibility to the heat stability of the tropomyosin shrimp allergen. Bioscience, Biotechnology and Biochemistry, 77(5), 948-953. https://doi.org/10.1271/bbb.120887