Elimination of the Allergenicity of Food Protein by High Pressure

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  • NOGAMI Naoyuki
    Graduate School of Science and Technology, Niigata University
  • MATSUNO Masatomo
    Department of Pediatrics, Yoshida Hospital
  • HARA Takashi
    Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University
  • JOH Toshio
    Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University
  • NISHIUMI Tadayuki
    Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University
  • SUZUKI Atsushi
    Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University

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Other Title
  • 高圧極限環境を利用した食品加工における新展開　　高圧処理による食品タンパク質のアレルゲン性低減化
  • 高圧処理による食品タンパク質のアレルゲン性低減化
  • コウアツ ショリ ニ ヨル ショクヒン タンパクシツ ノ アレルゲンセイ テイゲンカ

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Abstract

This paper describes general methods to eliminate or decrease the allergenicity of food protein, and also describes high pressure-induced elimination of the allergenicity of food protein, especially meat protein.The effect of high pressure treatment on the elimination of bovine serum albumin (BSA, the major beef allergen) allergenicity was evaluated on the basis of histamine release from human basophilic KU812F cells sensitized with sera from allergic patients, and the structural changes of BSA responsible for reducing allergenicity was estimated. BSA pressurized at pressures ranging from 300 to 600 MPa reduced histamine release from the cells sensitized with A5 serum with significance. The reducing effect of high-pressure treatment gradually increased with the increase of pressure applied to BSA. The pressure-induced structural changes of BSA were estimated by fluorescence spectra, circular dichroism (CD) spectra (the content of secondary structure), the amount of surface sulfhydryl (SH) group, and the surface aromatic hydrophobicity. The blue shift and decrease of the fluorescence of BSA gradually progressed with the increase of pressure applied. But no significant effect of pressure on CD spectra was observed. Pressure-treated BSA showed the maximum increase in the amount of SH group by pressure treatment at 100 MPa, and the aromatic hydrophobicity gradually decreased with the increase of high pressure applied. These results indicated that high pressure treatment induced the tertiary structural changes of BSA, but no effect on the secondary structure. We concluded that the pressure-induced elimination of BSA allergenicity seemed to be related to the tertiary structural change of BSA.

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