FOOD SCIENCE ›› 2017, Vol. 38 ›› Issue (11): 33-39.doi: 10.7506/spkx1002-6630-201711006

• Basic Research • Previous Articles     Next Articles

Relationship between Conformational Changes Caused by Ultra-high Pressure and Allergenicity of Shrimp Tropomyosin

HU Zhihe, WANG Xingxuan, ZHANG Qingqing, WU Zijian, XUE Lu, JIA Ying   

  1. Tianjin Key Laboratory of Food Biotechnology, School of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China
  • Online:2017-06-15 Published:2017-06-19

Abstract: The objective of this work was to research the relationship between the conformational changes and allergenicity of tropomyosin (TM) from the white shrimp Litopenaeus vannamei after ultra-high pressure. TM was treated under different conditions of pressure (0.1–800.0 MPa), holding time (10–40 min) and temperature (10–37 ℃) and then tested for changes in it secondary and tertiary structures and allergenicity by circular dichroism spectrum (CD), fluorospectrophotometry and indirect enzyme linked immunosorbent assay (ELISA), respetively. Results showed that both the allergenicity and tertiary structure rather than the secondary structure of TM were changed under different high pressure conditions. There was a significant correlation between the changes in the allergenicity and tertiary structure of TM under different high pressure conditions. In the pressure range tested, the number of surface-exposed hydrophobic amino acids was the lowest at 20 ℃, 40 min, 300 MPa while achieving minimal allergenicity (OD492 nm was 0.210 ± 0.005), and the largest number of exposed hydrophobic amino acids and the maximal allergenicity (OD492 nm was 0.328 ± 0.004) were observed at 700 MPa. Therefore, the allergenicity of TM was related to its tertiary structure but not its secondary structure.

Key words: Litopenaeus vannamei, tropomyosin, ultra-high prssure treatment, protein conformation, allergenicity

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