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

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...

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Bibliographic Details
Published inApplied biochemistry and microbiology Vol. 55; no. 3; pp. 270 - 276
Main Authors Muranova, T. A., Zinchenko, D. V., Belova, N. A., Surin, A. K., Miroshnikov, A. I.
Format Journal Article
LanguageEnglish
Published Moscow Pleiades Publishing 01.05.2019
Springer Nature B.V
Subjects
Biochemistry
Biomedical and Life Sciences
Chymotrypsin
Deactivation
Hepatopancreas
Hydrolysates
Hydrolysis
Inactivation
Inhibitors
Life Sciences
Medical Microbiology
Microbiology
Proteins
Proteolysis
Soybeans
Trypsin
Trypsin inhibitors
soybean proteinase inhibitors
crab hepatopancreas
enzymatic hydrolysis
cod fish pyloric caeca
protosubtilin
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Summary: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.
ISSN:0003-6838
1608-3024
DOI:10.1134/S0003683819030086