.Kemin Foods, L.c.

Other

Kemin Consumer Care, L.c.

Fayad Z Sheabar

Robert Stomp

Rod Ausich

Clarence A Ryan

Jerry Newman

Rodney L Ausich

Hal G Fallert

George Mather

Andrew Shao

Brent Davieson

Brent Davidson

Zoriada DeFeitas

A nutritional intervention composition for reducing post-prandial blood glucose levels in humans, including between about 0.1 mg and about 500 mg of a proteinase inhibitor that is administered prior to the meal. The composition is effective for treating or ameliorating the effects of hyperglycemia and Type II diabetes. The composition also is effective in combating obesity. The proteinase inhibitor is preferably isolated from plant material, such as potatoes, soy, and beans. Potato proteinase inhibitor II and soybean Bowman-Birk inhibitor are included in the group of effective proteinase inhibitors.

Composition and method for reducing post-prandial blood glucose

The present invention provides a method for adjusting the yield and purity of a proteinase inhibitor extract from plant tissue, preferably potato tubers. The extraction and isolation of the proteinase inhibitor from potatoes begins with the addition of an organic acid, preferably formic acid, and a salt, preferably sodium chloride, to raw potatoes. The mixture is subjected to process steps to extract soluble proteins. The extract is subjected to heat treatment at an adjusted temperature and adjusted duration whereby purity of the proteinase inhibitor is enhanced by heating at a relatively high temperature for a relatively short duration and whereby yield of the proteinase inhibitor is enhanced by heating at a relatively low temperature for a relatively long duration. If the removal of soluble protein impurities that are not denatured during the heat treatment step is desired, ultrafiltration is used. By adjusting the cycles of filtration, purity of the proteinase inhibitor can be adjustably selected.

Method for controlling the yield and purity of proteinase inhibitor II during extraction

The present invention provides a method for the extraction of a proteinase inhibitor from plant tissue. The extraction of the proteinase inhibitor begins with the addition of an alcohol-free, aqueous solution of an organic acid and a salt to plant tissue. The extraction solution and plant tissue are comminuted to reduce the average particle size of the plant tissue to improve extraction efficiencies. A weight ratio of between about 1:1 and about 1:10 extraction solution to plant tissue is used. In extracting proteinase inhibitor II from potato tubers, the extraction solution utilizes formic acid and sodium chloride, and the average particle size is reduced to between about 100 and 1500 microns. The process has been demonstrated to be cost-effective and provide high yields of the target proteinase inhibitor on commercial scales.

Method of enhancing the extraction of proteinase inhibitors

A method for removing protein impurities from extracts of protease inhibitor-containing plant material. Plant materials containing protease inhibitors, such a potato tubers that contain protease inhibitor II, are extracted using an alcohol-free solvent. The proteins present in the extract include impurities other than the protease inhibitor, specifically Kunitz, Bowman-Birk and carboxypeptidase inhibitors. The extract is subjected to heat treatment to denature and precipitate the unstable protein impurities followed by centrifugation to remove the precipitate. Ultrafiltration in the presence of a buffer removes the Bowman-Birk and carboxypeptidase inhibitors. The resulting purified protease inhibitor has applicability in the control of obesity and diabetes.

Method for the elimination of Kunitz and Bowman-Birk trypsin inhibitors and carboxypeptidase inhibitor from potato proteins

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West Des Moines, IA, United States of America

Fayad Z Sheabar