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 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, PT, 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, PT, 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, PT, 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, PT, 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.

A method for removing chromatin from a cell culture harvest comprising the steps: providing a cell culture harvest containing a desired biological product selected from the group consisting of a parvovirus or an adeno-associated virus, incubating the cell culture harvest in an aqueous medium at a pH value within the range of 3.0 to 4.0 with an ionic strength corresponding to NaCl at a concentration within the range of 3.0 M to saturation and separating the desired biological product from solids produced.

A method for removing chromatin from a cell culture harvest comprising the steps: providing a cell culture harvest containing a desired biological product selected from the group consisting of a parvovirus or an adeno-associated virus, incubating the cell culture harvest in an aqueous medium at a pH value within the range of 3.0 to 4.0 with an ionic strength corresponding to NaCl at a concentration within the range of 3.0 M to saturation and separating the desired biological product from solids produced.

Aspects of the present application relates to co-crystal of carfilzomib with maleic acid, process for the preparation of co-crystal of carfilzomib with maleic acid, process for the preparation of pure carfilzomib from co-crystal of carfilzomib with maleic acid and process for the preparation of amorphous carfilzomib.

Disclosed is a method of recovering a peptide, including: mixing a liquid sample containing a complex of peptide and protein in blood with a reagent containing a neutral amino acid, an acidic amino acid or both the neutral and acidic amino acids to liberate the peptide from the protein in blood; and recovering the liberated peptide.

Disclosed is a method of recovering a peptide, including: mixing a liquid sample containing a complex of peptide and protein in blood with a reagent containing a neutral amino acid, an acidic amino acid or both the neutral and acidic amino acids to liberate the peptide from the protein in blood; and recovering the liberated peptide.

Disclosed is a preparation method of a composition containing a nitrogen heterocyclic hexapeptide precursor, composition A and B containing a nitrogen heterocyclic hexapeptide precursor of a compound having formula I and formula II obtained by the method, and an application of the composition used for preparing a compound having formula III.

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Disclosed is a preparation method of a composition containing a nitrogen heterocyclic hexapeptide precursor, composition A and B containing a nitrogen heterocyclic hexapeptide precursor of a compound having formula I and formula II obtained by the method, and an application of the composition used for preparing a compound having formula III.

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