An improved method for the purification of eggplant trypsin inhibitor.

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  • 伊吹 文男
    Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto Prefectural University
  • 山田 正明
    Research Laboratories, The Green Cross Corp.
  • 田代 操
    Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto Prefectural University Department of Food Science, Faculty of Living Science, Kyoto Prefectural University
  • 金森 正雄
    Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto Prefectural University

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  • Improved Method for the Purification of

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The trypsin inhibitor in eggplant, Solanum melongena L., was isolated and purified by the improved method with the techniques of dialysis using acetylated cellulose tube and ion-exchange chromato-graphy on DEAE-Sephadex. The final preparation was found to be homogeneous by disc and SDS-polyacrylamide gel electrophoreses. This inhibitor had the molecular weight of about 6, 200, the pI value of 4.7, and furthermore characteristic amino acid composition lacking in trypto-phan, histidine, valine and methionine. The trypsin inhibition data indicated that the purified inhibitor combined with bovine trypsin [EC 3.4.21.4] in the molar ratio of 1:1. These properties of this inhibitor were in agreement with those of the dialyzable eggplant trypsin inhibitor pre-viously purified, indicating that the dialyzable and non-dialyzable inhi-bitors in eggplant are identical.

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