Described herein is a method of maintaining corn protein yield during extraction, comprising obtaining a corn gluten material, washing the corn gluten material to remove non-protein components with an ethanol-water solvent comprising at least 85 wt % ethanol to obtain a corn protein concentrate product, wherein the loss of corn protein content during extraction is less than 25% of total corn protein.

Described herein is a concentrated sweet potato leaf protein in dried form, along with methods for producing it. The concentrated leaf protein has a protein content of greater than 21% by weight, and can have other beneficial components such as polyphenols. The concentrated leaf proteins are suitable for use in food and beverages, as protein supplementation, or as agents for gelling, foaming, and whipping.

Among other aspects, the present invention provides methods for the manufacture of blood protein compositions from pooled plasma. In one embodiment, the invention provides an alcohol fractionation scheme that allows for significant increases in the yield of blood proteins purified from the starting plasma sample. In a specific embodiment, a method for fractionating pooled plasma is provided, the method comprising an initial low pH, high alcohol precipitation step. The present invention also provides pharmaceutical compositions of therapeutic blood proteins.

Provided herein are methods for producing a mung bean protein isolate having high functionality for a broad range of food applications. In some embodiments, the methods for producing the isolate comprise one or more steps selected from: (a) extracting one or more mung bean proteins from a mung bean protein source in an aqueous solution, for example, at a pH between about 6.5-10.0; (b) purifying protein from the extract using at least one of two methods: (i) precipitating protein from the extract at a pH near the isoelectric point of a globulin-rich fraction, for example a pH between about 5.0-6.0; and/or (ii) fractionating and concentrating protein from the extract using filtration such as microfiltration, ultrafiltration or ion-exchange chromatography; and (c) recovering purified protein isolate.

The present invention provides methods and protein compositions having advantageous properties, such as a high uncorrected limiting amino acid score as well as favorable amounts of essential amino acids, branched chain amino acids, as well as other amino acids more difficult to find in the regular diet. The protein composition is obtainable as taught herein from algal or microbial biomass. The protein composition produced according to the methods of the invention provides a proteinaceous food or food ingredient that is more nutritionally balanced (and therefore nutritionally superior) to protein compositions otherwise available. The protein material is advantageously used as a food or food ingredient for humans and/or animals. Also provided are methods of producing the protein material from biomass sources.

The present invention provides a downstream purification method process for the production of bispecific antigen-binding polypeptides. The method comprises at least the steps of (i) providing a separation resin comprising a polymer matrix part and a ligand part, wherein the matrix part comprises polymethacrylate and has a particle size of about 30 to 60 pm, wherein the ligand part comprises recombinant protein L, and wherein the ligand part's protein L is covalently bound to the matrix part's particles, (ii) contacting a process fluid comprising the bispecific antigen-binding polypeptide with the separation resin, (iii) capturing the bispecific antigen-binding polypeptide by the ligand part of the separation resin, wherein the bispecific antigen-binding polypeptide reversibly binds to the ligand part of the separation resin, and wherein the remainder of the process fluid does not bind to the ligand part of the separation resin, (iv) washing the bound bispecific antigen-binding polypeptide with a wash buffer which does not elute the bispecific antigen-binding polypeptide from the ligand portion, and (v) elute the bispecific antigen-binding polypeptide from the ligand part with an elution buffer at a low pH.

The present subject matter is directed to a method of manufacturing purified IVIG from Fraction III of plasma, comprising re-constituting a Fraction III paste in a buffer; adjusting the pH and temperature; adding ethanol and then gradually lowering the temperature; centrifuging and filtering the supernatant; ultra-filtrating to remove alcohol; undergoing weak anion exchange chromatography; ultra-filtrating to reach a desired protein concentration; aseptic filtrating; nano filtrating for virus removal; and incubating at low pH for virus inactivation to obtain a resulting Fraction III suspension comprising purified IVIG. The present subject matter is directed to IVIG having 14 newly-found proteins, namely KH 26, KH 27, KH 28, KH 29, KH 30, KH 31, KH 32, KH 33, KH 39, KH 40, KH 41, KH 42, KH 43, and KH 44 for both liquid and lyophilized form.

The present subject matter is directed to a method for separating proteins of plasma using pH adjustment including the steps of reconstituting Fraction III, Fraction IV, or plasma paste, in water for injection; adjusting pH value to 1 and temperature from 1° C. to 30° C.; centrifuging the resulting suspension at 6,000 rpm at 2-8° C. for 20 min; collecting the resulting paste 1 (P1) and supernatant 1 (S1); reconstituting P1 in WFI and adjust the pH to 2; and repeating step 3) to step 5) until the pH of supernatant reaches 14. According to the method, a new formulation of immunoglobulin is prepared from plasma Fraction III and Fraction IV.

The present subject matter is directed to a method of manufacturing and purifying an intravenous injection of prothrombin complex concentration (PCC) from plasma Fraction III and a method of manufacturing and purifying an intravenous injection of non-PCC from plasma Fraction IV. The intravenous injection of PCC and non-PCC obtained from the method can be administered to a patient in need thereof for stopping replication, killing and preventing HIV-1 and HIV-2 in a patient.

Disclosed is a method for producing hybrid or non-hybrid recombinant glycoprotein hormones, for example the recombinant equine chorionic gonadotropin (r-eCG), the hybrid recombinant chorionic gonadotropin, the recombinant thyroid-stimulating hormone (r-TSH), the recombinant luteinising hormone (r-LH), the luteinising hormone and the recombinant follicle-stimulating hormone (r-FSH). In addition, the present invention relates to the recombinant glycoprotein hormones comprising the equine α and β subunits, inter alia, the α subunit of mammals and equine β subunit, where the two subunits are fused in a simple chain, and chain-modifying agents, which hormones are easier to purify, more homogeneous, easier to produce on an industrial scale without using animals, in comparison with the wild glycoprotein hormone The hormones are useful for inducing animal reproduction, ovulation induction, superovulation induction, follicle growth, oestrus induction, anoestrus reversal, puberty induction in animals, both with and without commercial interest.