Abstract: Provided herein are pongamia oil compositions suitable for animal consumption, in particular human consumption, as well as methods of producing such compositions. The compositions are edible and non-bitter tasting, and have certain attributes that make such compositions suitable for use as and/or in various food and beverage products. Provided herein are also methods of analyzing pongamia oil.

Abstract: Provided herein are Pongamia oil compositions suitable for animal consumption, in particular human consumption, as well as methods of producing such compositions. The compositions are edible and non-bitter tasting, and have certain attributes that make such compositions suitable for use as and/or in various food and beverage products. Provided herein are also methods of analyzing Pongamia oil.

Abstract: Provided herein are protein-enriched pongamia compositions, including pongamia protein concentrates and isolates, suitable for animal consumption, in particular human consumption. Provided herein are also various food and beverage products that can be fortified with such protein-enriched pongamia compositions. Provided herein are also methods of producing the protein-enriched pongamia compositions, as well as methods of producing such protein-enriched pongamia compositions from pongamia beans or various forms of pongamia meal.

Abstract: Provided herein are compositions obtained from processing pongamia oilseeds. The resulting pongamia compositions may be in the form of meal, and have an optimized nutritional composition achieved by subjecting pongamia oilseeds to certain processing steps. The resulting pongamia compositions may also have reduced levels of karanjin, pongamol and tannins. Such pongamia compositions may be suitable as food or food ingredients to humans and other animals.

Abstract: A food label includes a food product portion providing indicia of a nutritional composition of a food product, with aspects of the indicia being coded to match aspects of a program recommendation portion of the food label.

Abstract: Modified proteins are disclosed that maintain enzymatic and insecticidal activity while displaying reduced or eliminated allergenicity. Epitopes which bind to anti-patatin antibodies were identified, and removed via site directed mutagenesis. Tyrosines were observed to generally contribute to the allergenic properties of patatin proteins. Removal of glycosylation sites was observed to reduce or eliminate antibody binding. Permuteins are also disclosed which have a rearranged amino acid sequence while retaining enzymatic activity. Deallergenized proteins and permuteins can be used as insecticidal materials, as nutritional supplements, and as immunotherapeutic agents.

Abstract: Modified proteins are disclosed that maintain enzymatic and insecticidal activity while displaying reduced or eliminated allergenicity. Epitopes which bind to anti-patatin antibodies were identified, and removed via site directed mutagenesis. Tyrosines were observed to generally contribute to the allergenic properties of patatin proteins. Removal of glycosylation sites was observed to reduce or eliminate antibody binding. Permuteins are also disclosed which have a rearranged amino acid sequence while retaining enzymatic activity. Deallergenized proteins and permuteins can be used as insecticidal materials, as nutritional supplements, and as immunotherapeutic agents.

Abstract: The present invention is in the fields of lipid metabolism and dietary supplementation and provides methods and compositions to improve heart health of a mammal by orally administering stearidonic acid and related compounds to the mammal. The improved heart health is evidenced by the enrichment of cardiac tissue with eicosapentaenoic acid (20:5, ?3) and docosapentaenoic acid (22:5, ?3) following the administration. Also provided are methods for promoting a stearidonic acid containing product by advertising its heart health benefits.

Abstract: Modified proteins are disclosed that maintain enzymatic and insecticidal activity while displaying reduced or eliminated allergenicity. Epitopes which bind to anti-patatin antibodies were identified, and removed via site directed mutagenesis. Tyrosines were observed to generally contribute to the allergenic properties of patatin proteins. Removal of glycosylation sites was observed to reduce or eliminate antibody binding. Permuteins are also disclosed which have a rearranged amino acid sequence while retaining enzymatic activity. Deallergenized proteins and permuteins can be used as insecticidal materials, as nutritional supplements, and as immunotherapeutic agents.

Abstract: Modified proteins are disclosed that maintain enzymatic and insecticidal activity while displaying reduced or eliminated allergenicity. Epitopes which bind to anti-patatin antibodies were identified, and removed via site directed mutagenesis. Tyrosines were observed to generally contribute to the allergenic properties of palatin proteins. Removal of glycosylation sites was observed to reduce or eliminate antibody binding. Permuteins are also disclosed which have a rearranged amino acid sequence while retaining enzymatic activity. Deallergenized proteins and permuteins can be used as insecticidal materials, as nutritional supplements, and as immunotherapeutic agents.

Abstract: Modified proteins are disclosed that maintain enzymatic and insecticidal activity while displaying reduced or eliminated allergenicity. Epitopes which bind to anti-patatin antibodies were identified, and removed via site directed mutagenesis. Tyrosines were observed to generally contribute to the allergenic properties of patatin proteins. Removal of glycosylation sites was observed to reduce or eliminate antibody binding.

Abstract: Modified proteins are disclosed that maintain enzymatic and insecticidal activity while displaying reduced or eliminated allergenicity. Epitopes which bind to anti-patatin antibodies were identified, and removed via site directed mutagenesis. Tyrosines were observed to generally contribute to the allergenic properties of patatin proteins. Removal of glycosylation sites was observed to reduce or eliminate antibody binding. Permuteins are also disclosed which have a rearranged amino acid sequence while retaining enzymatic activity. Deallergenized proteins and permuteins can be used as insecticidal materials, as nutritional supplements, and as immunotherapeutic agents.

Abstract: Modified proteins are disclosed that maintain enzymatic and insecticidal activity while displaying reduced or eliminated allergenicity. Epitopes which bind to anti-patatin antibodies were identified, and removed via site directed mutagenesis. Tyrosines were observed to generally contribute to the allergenic properties of patatin proteins. Removal of glycosylation sites was observed to reduce or eliminate antibody binding.