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- Title
Chemical inactivation of soybean protease inhibitors.
- Authors
Sessa, David; Nelsen, Terry
- Abstract
This study aimed to optimize chemical treatments to destroy Kunitz (KTI) and Bowman- Birk (BBI) type protease inhibitors in model systems, and to destroy total trypsin inhibitor activity in soy flour. Time, temperature, and reagent concentration were studied and 40 to more than 85% inactivation of KTI and BBI were observed by treatment with 0.6 mM NaSO,10 mM ascorbic acid + 0.8 mM CuSO or 20 mM HO + 0.8 mM CuSO at 65- 90°C for 0.5- 1 hr. Upon treatment with NaSO, KTI and BBI amino acid composition had no significant change. In contrast, AH + CU treatment of both KTI and BBI markedly increased aspartic acid + asparagine and glutamic acid + glutamine contents, and significantly decreased histidine, tyrosine, and methionine. With soy flour, only NaSO effectively inactivated both protease inhibitors. Steeping soybean flour in 50 mM NaSO at 65°C for 1 hr inactivated about 98% BBI and 95% KTI. The information conveyed is basic to developing chemical methodology needed to inactivate both KTI and BBI protease inhibitors in soy protein products.
- Publication
Journal of the American Oil Chemists' Society (JAOCS), 1991, Vol 68, Issue 7, p463
- ISSN
0003-021X
- Publication type
Article
- DOI
10.1007/BF02663814