The present invention relates to a method for continuous recovering of a protein from a fluid, comprising precipitating the protein in the fluid and separating the precipitated protein from the fluid. The invention also provides an inclined plate settler that can be used for such continuous protein recovering.

The present invention in its broadest aspect relates to a method for reducing glycoalkaloid content and turbidity of an aqueous phase comprising compounds selected from two or more of PA, PI, PPO, LipO, pectin, lipid, glycoalkaloid and phenolic compounds of which at least one compound is selected from PA, PI, LipO and PPO; a) providing an aqueous phase comprising compounds selected from two or more of PA, PI, PPO, LipO, pectin, lipid, glycoalkaloid and phenolic compounds of which at least one compound is selected from PA, PI, LipO and PPO; and b) performing one or more steps to reduce the concentration of solanine in the dry matter of the aqueous phase with at least 15 percent, such as at least 20% such as at least 25% and to achieve an optical density at 620 nm of the remaining aqueous phase of less than 0.7; such as less than 0.5; such as less than 0.3; such as less than 0.2 such as less than 0.1 and thereby obtaining an aqueous phase having reduced glycoalkaloid content and turbidity compared to an untreated aqueous phase.

The present invention in its broadest aspect relates to a method for reducing glycoalkaloid content and turbidity of an aqueous phase comprising compounds selected from two or more of PA, PI, PPO, LipO, pectin, lipid, glycoalkaloid and phenolic compounds of which at least one compound is selected from PA, PI, LipO and PPO; a) providing an aqueous phase comprising compounds selected from two or more of PA, PI, PPO, LipO, pectin, lipid, glycoalkaloid and phenolic compounds of which at least one compound is selected from PA, PI, LipO and PPO; and b) performing one or more steps to reduce the concentration of solanine in the dry matter of the aqueous phase with at least 15 percent, such as at least 20% such as at least 25% and to achieve an optical density at 620 nm of the remaining aqueous phase of less than 0.7; such as less than 0.5; such as less than 0.3; such as less than 0.2 such as less than 0.1 and thereby obtaining an aqueous phase having reduced glycoalkaloid content and turbidity compared to an untreated aqueous phase.

Crystal nucleation, and associated articles, systems, and methods, are generally described.

The present invention relates to an improved method of purifying an immunoglobulin, and more particularly to a method of purifying an immunoglobulin which is capable of sufficiently removing impurities from an immunoglobulin-containing plasma protein sample through a simple process, comprising a single anion-exchange chromatography and a single cation-exchange chromatography.

The present invention relates to an improved method of purifying an immunoglobulin, and more particularly to a method of purifying an immunoglobulin which is capable of sufficiently removing impurities from an immunoglobulin-containing plasma protein sample through a simple process, comprising a single anion-exchange chromatography and a single cation-exchange chromatography.

Methods of producing multiple protein products from blood-based materials including alpha-1-proteinase inhibitor, gamma globulin, albumin, and other proteins are described herein. The inventive methods include steps of fractionation that utilize a combination of salt and organic solvent. Advantageously, the inventive methods are simple and produce alpha-1-proteinase inhibitor, gamma globulin, albumin, and other proteins in high yields. The sequence of process steps can be selected to obtain multiple products from various in-process materials, such as supernatants, pastes, chromatography flow-though, and chromatography washes.

Methods of producing multiple protein products from blood-based materials including alpha-1-proteinase inhibitor, gamma globulin, albumin, and other proteins are described herein. The inventive methods include steps of fractionation that utilize a combination of salt and organic solvent. Advantageously, the inventive methods are simple and produce alpha-1-proteinase inhibitor, gamma globulin, albumin, and other proteins in high yields. The sequence of process steps can be selected to obtain multiple products from various in-process materials, such as supernatants, pastes, chromatography flow-though, and chromatography washes.

Methods are disclosed for producing highly purified recombinant human insulin (RHI) having a purity of 99.0% (w/w) or greater, a Total Impurity (not including the related substance desamido Asn.sup.A21-RHI, as specified by USP) of 0.8% (w/w) or less, and an impurity C of 0.1% (w/w) or less. Also disclosed are API compositions of highly purified RHI having a purity of 99.0% (w/w) or greater, a Total Impurity of 0.8% (w/w) or less, and an impurity C of 0.1% (w/w) or less.

The present invention provided the techniques and recipes for enhancing recombinant peptide production in microorganism like E. coli, Saccharomyces cerevisiae, Pichia pastoris and Bacillus subtilis. The designs of fusion protein with a polypeptide and high cell density fermentation process to over express the peptides are given. Methods for separation of polypeptides from fusion protein and methods for isolation and purification of peptides are mentioned. This invention also provides an uncomplicated and unique purification processes for manufacturing of Teriparatide, Liraglutide precursor and Semaglutide precursor with purifies of >98%.