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Identification of a New Soybean Kunitz Trypsin Inhibitor Mutation and Its Effect on Bowman-Birk Protease Inhibitor Content in Soybean Seed

Identification of a New Soybean Kunitz Trypsin Inhibitor Mutation and Its Effect on Bowman-Birk Protease Inhibitor Content in Soybean Seed

Jason D Gillman, Won-Seok Kim, Hari B Krishnan

J Agric Food Chem. 2015 Feb 11;63(5):1352-9.

PMID: 25608918

Abstract:

Soybean seed contains antinutritional compounds that inactivate digestive proteases, principally corresponding to two families: Kunitz trypsin inhibitors (KTi) and Bowman-Birk inhibitors (BBI). High levels of raw soybean/soybean meal in feed mixtures can cause poor weight gain and pancreatic abnormalities via inactivation of trypsin/chymotrypsin enzymes. Soybean protein meal is routinely heat-treated to inactivate inhibitors, a practice that is energy-intensive and costly and can degrade certain essential amino acids. In this work, we screened seed from 520 soybean accessions, using a combination of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblots with anti-Kunitz trypsin inhibitor antibodies. A soybean germplasm accession was identified with a mutation affecting an isoform annotated as nonfunctional (KTi1), which was determined to be synergistic with a previously identified mutation (KTi3-). We observed significant proteome rebalancing in all KTi mutant lines, resulting in dramatically increased BBI protein levels.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP37330340	Trypsin-chymotrypsin inhibitor from Glycine max (soybean)		37330-34-0	Price

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