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Soybean Trypsin Inhibitors: Selective Inactivation at Hydrolysis of Soybean Proteins by Some Enzymatic Complexes

Abstract

Inactivation of the Kunitz and Bowman-Birk soybean trypsin inhibitors at hydrolysis of soybean proteins by enzymatic complexes was studied. These complexes are derived from king crab hepatopancreas, cod fish pyloric caeca, and a commercial enzymatic complex of protosubtilin. Analysis of the soybean protein hydrolysates showed that these enzymatic complexes completely digested the Kunitz trypsin inhibitor (60–70% of the total trypsin inhibitors) and had almost no effect on the Bowman-Birk trypsin and chymotrypsin inhibitor. All of the enzymatic complexes contain different sets of enzymes with different proteolytic specificity. This allow to make the conclusion that Bowman-Birk inhibitor is highly resistant to proteolysis and is not inactivated at enzymatic hydrolysis.

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Correspondence to D. V. Zinchenko.

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Translated by A. Boutanaev

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Muranova, T.A., Zinchenko, D.V., Belova, N.A. et al. Soybean Trypsin Inhibitors: Selective Inactivation at Hydrolysis of Soybean Proteins by Some Enzymatic Complexes. Appl Biochem Microbiol 55, 270–276 (2019). https://doi.org/10.1134/S0003683819030086

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Keywords:

  • soybean proteinase inhibitors
  • enzymatic hydrolysis
  • protosubtilin
  • crab hepatopancreas
  • cod fish pyloric caeca