A method for producing ACE Inhibitor peptides from a protein source or plasma is disclosed. The method utilizes proteolysis by intestinal, blood-circulating, or membrane-bound proteases. The initial synthesis step could require obtaining a protein source either from a human or animal. A protease is added to either a given plasma protein or plasma and incubated. Following incubation, the protease activity must be quenched using a protease inhibitor to inactivate the protease. After incubation with protease inhibitor, the solution will contain a mixture of bioactive ACE inhibitory peptides and inert peptides. This mixture may be purified to select for the ACE inhibitory peptides through centrifugation. The mixture may also be sterilized to remove any microbial contaminants. The ACE inhibitory peptides can be mixed with protein powders, incorporated into baked good and put into other food products to provide food products with the added benefit of lowering blood pressure.

The present invention relates to polypeptide variants of porcine trypsin, to nucleic acid molecules encoding these variants, and to host cells comprising such nucleic acid molecules. It also relates to the use of these variants in methods for producing insulin. The invention further relates to the use of these variants as medicaments, as food ingredients, or as feed ingredients and to the use of these variants within a process of manufacturing a food ingredient or a feed ingredient.

The present invention is directed to non-soy oilseed protein products, very low in, or free of, beany, green, vegetable or similar flavour notes and useful for the fortification of food and beverage products and prepared without the use of salt in the process. The non-soy oilseed protein products of the present invention are obtained by extracting non-soy oilseed protein source with water to form an aqueous non-soy oilseed protein solution, at least partially separating the aqueous non-soy oilseed protein solution from residual non-soy oilseed protein source, adjusting the pH of the aqueous non-soy oilseed protein solution to a pH between about 1.5 and a value about 1 pH unit lower than the typical pH of isoelectric precipitation to solubilize the bulk of the protein and form an acidified non-soy oilseed protein solution then separating the acidified non-soy oilseed protein solution from the acid insoluble solid material. The acidified non-soy oilseed protein solution may be dried following optional concentration and diafiltration to form a non-soy oilseed protein product, which may be an isolate. The acid insoluble solid material may be washed with acidified water and then dried to form another non-soy oilseed protein product. These products may be dried at the acidic pH at which they were prepared or may be adjusted in pH before drying.

The present invention is directed to non-soy oilseed protein products, very low in, or free of, beany, green, vegetable or similar flavour notes and useful for the fortification of food and beverage products and prepared without the use of salt in the process. The non-soy oilseed protein products of the present invention are obtained by extracting non-soy oilseed protein source with water to form an aqueous non-soy oilseed protein solution, at least partially separating the aqueous non-soy oilseed protein solution from residual non-soy oilseed protein source, adjusting the pH of the aqueous non-soy oilseed protein solution to a pH between about 1.5 and a value about 1 pH unit lower than the typical pH of isoelectric precipitation to solubilize the bulk of the protein and form an acidified non-soy oilseed protein solution then separating the acidified non-soy oilseed protein solution from the acid insoluble solid material. The acidified non-soy oilseed protein solution may be dried following optional concentration and diafiltration to form a non-soy oilseed protein product, which may be an isolate. The acid insoluble solid material may be washed with acidified water and then dried to form another non-soy oilseed protein product. These products may be dried at the acidic pH at which they were prepared or may be adjusted in pH before drying.

A process for refolding recombinant chymotrypsin produced from prokaryote host cells is described. In particular, the present invention provides a process for refolding recombinant chymotrypsin produced from E. coli is described.

A process for producing recombinant trypsin from prokaryote host cells in high yield and high specific activity is described. In particular, a process for producing recombinant trypsin from E. coli is described.

This present invention relates to a chemically stable hollow spherical covalent organic framework having mesoporous walls with high surface area and a process for synthesis thereof. Further the immobilization and adsorption ability of the said COF's is disclosed in the present invention.

The present invention relates to trypsin variants with improved enzymatic properties, and particularly relates to a mutated trypsin comprising an amino acid substitution at least at two amino acid positions leading to an increased affinity for the nucleophilic substrate and/or at least at two amino acid positions leading to a reduced hydrolysis activity.

This invention is in the field of medicinal pharmacology. In particular, the invention relates to protease activated receptor type 2 (PAR2) modulating compounds (e.g., mimetic peptides), compositions comprising such modulating compounds, and their use as therapeutics for the treatment of conditions involving PAR2 activity.

A method for producing ACE Inhibitor peptides from a protein source or plasma is disclosed. The method utilizes proteolysis by intestinal, blood-circulating, or membrane-bound proteases. The initial synthesis step could require obtaining a protein source either from a human or animal. A protease is added to either a given plasma protein or plasma and incubated. Following incubation, the protease activity must be quenched using a protease inhibitor to inactivate the protease. After incubation with protease inhibitor, the solution will contain a mixture of bioactive ACE inhibitory peptides and inert peptides. This mixture may be purified to select for the ACE inhibitory peptides through centrifugation. The mixture may also be sterilized to remove any microbial contaminants. The ACE inhibitory peptides can be mixed with protein powders, incorporated into baked good and put into other food products to provide food products with the added benefit of lowering blood pressure.