Improving Digestibility of Soy Flour by Reducing Disulfide Bonds with Thioredoxin

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Improving digestibility of soy flour by reducing disulfide bonds with thioredoxin.

The Kunitz trypsin inhibitor (KTI) and the Bowman-Birk inhibitor (BBI) of trypsin and chymotrypsin contain disulfide bonds. Glycinin, the major storage protein in soybeans also contains disulfide bonds. Treatment of soy white flour with a NADP-thioredoxin system (NTS) effectively reduced disulfide bonds in soy flour and increased protein digestibility by trypsin and pancreatin as measured by th...

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The interaction of thioredoxin with Txnip. Evidence for formation of a mixed disulfide by disulfide exchange.

The thioredoxin system plays an important role in maintaining a reducing environment in the cell. Recently, several thioredoxin binding partners have been identified and proposed to mediate aspects of redox signaling, but the significance of these interactions is unclear in part due to incomplete understanding of the mechanism for thioredoxin binding. Thioredoxin-interacting protein (Txnip) is ...

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Disulfide bonds are generated by quinone reduction.

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ژورنال

عنوان ژورنال: Journal of Agricultural and Food Chemistry

سال: 2008

ISSN: 0021-8561,1520-5118

DOI: 10.1021/jf801136n