Inhibition of Trypsin by Oxidized Methyl Linolenate

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  • Hatate Hideo
    Laboratory or Fisheries Technology, Faculty of Agriculture, Kyushu University
  • Toyomizu Masamichi
    Laboratory or Fisheries Technology, Faculty of Agriculture, Kyushu University

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Other Title
  • 酸化リノレン酸メチルによるtrypsin阻害
  • サンカ リノレンサン メチル ニ ヨル trypsin ソガイ

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Abstract

The authors found that autoxidized methyl linolenate (oxd MLn) inhibited trypsin, so the relation between the autoxidation of MLn and the inhibition of trypsin by oxd MLn was studied. The results obtained are summarized as follows. 1. The inhibition by oxd MLn was observed only in the absence of Ca^2+ and the rate of inhibition increased under the condition that trypsin activity lowered owing to the autolysis of trypsin. 2. The inhibitory action of oxd MLn depended on the reaction with trypsin but not on the substrates used in the determination of trypsin activity. 3. Peroxide value, conjugated diene content and TBA value of oxd MLn were the highest in one day, when oxidized at 40℃. The inhibition by oxd MLn was not so serious at the early stage of oxidation and increased gradually with the progress of oxidation. The fact indicated that the inhibition was not due to methyl linolenate hydroperoxides but to the secondary products of oxd MLn. 4. The polymer inhibited trypsin definitely among the fractions obtained from oxd MLn by chromatography on Bio-Beads S-X3. 5. The inhibitory action of polymer on trypsin was found to be the noncompetitive type by employing the Lineweaver-Burk method of plotting.

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