The disclosure provides methods of purifying native and recombinant biomolecules, e.g., proteins, from mammalian cells using purification protocols incorporating harvest recovery operations involving decanter centrifugation of at least one target biomolecule from at least one particulate component of cell culture fluid. The unexpected capacity of decanter centrifuge separation of biological materials of similar densities found in mammalian cell culture fluid has been found to yield high quantities of functional protein in efficient, low-cost harvest recovery steps of biomolecule purification protocols.

The disclosure provides methods of purifying native and recombinant biomolecules, e.g., proteins, from mammalian cells using purification protocols incorporating harvest recovery operations involving decanter centrifugation of at least one target biomolecule from at least one particulate component of cell culture fluid. The unexpected capacity of decanter centrifuge separation of biological materials of similar densities found in mammalian cell culture fluid has been found to yield high quantities of functional protein in efficient, low-cost harvest recovery steps of biomolecule purification protocols.

A method for purification of a sulfatase using metal chelating chromatography without using tags such as His-tag, etc. is disclosed. An embodiment provides a method for purifying a sulfatase including the steps of: (a) providing a sulfatase-containing solution comprising one or a plurality of impurities; (b) performing a first chromatographic separation of the sulfatase-containing solution using a metal affinity chromatography resin; (c) performing a second chromatographic separation using a cation exchange chromatography resin; and (d) performing a final chromatographic separation using an anion exchange chromatography resin, wherein the impurities are removed thereby.

A method for purification of a sulfatase using metal chelating chromatography without using tags such as His-tag, etc. is disclosed. An embodiment provides a method for purifying a sulfatase including the steps of: (a) providing a sulfatase-containing solution comprising one or a plurality of impurities; (b) performing a first chromatographic separation of the sulfatase-containing solution using a metal affinity chromatography resin; (c) performing a second chromatographic separation using a cation exchange chromatography resin; and (d) performing a final chromatographic separation using an anion exchange chromatography resin, wherein the impurities are removed thereby.

The present disclosure pertains to compositions comprising anti-VEGF and methods for producing such compositions in chemically defined media and controlling amounts of certain oxidized aflibercept variants.

The present disclosure pertains to compositions comprising anti-VEGF and methods for producing such compositions in chemically defined media and controlling amounts of certain oxidized aflibercept variants.

An ultrasound-assisted simulated digestion method of a milk protein active peptide and an application thereof in health foods, pertaining to the technical field of intensive processing of dairy products and preparation of health foods. The method firstly employs ultrasonic pretreatment of casein and β-lactoglobulin, followed by enzymatic hydrolysis with a protease to prepare casein and β-lactoglobulin polypeptide, and traces the activity of the polypeptide by simulating gastrointestinal digestion, and then simulates absorption by intestinal epithelial cells with Caco-2 cells, to characterize a highly active milk protein polypeptide digested by the gastrointestinal tract and absorbed by the Caco-2 cells simulating absorption by the inner wall of the small intestine. The method has identified five such highly active milk protein polypeptides.

An ultrasound-assisted simulated digestion method of a milk protein active peptide and an application thereof in health foods, pertaining to the technical field of intensive processing of dairy products and preparation of health foods. The method firstly employs ultrasonic pretreatment of casein and β-lactoglobulin, followed by enzymatic hydrolysis with a protease to prepare casein and β-lactoglobulin polypeptide, and traces the activity of the polypeptide by simulating gastrointestinal digestion, and then simulates absorption by intestinal epithelial cells with Caco-2 cells, to characterize a highly active milk protein polypeptide digested by the gastrointestinal tract and absorbed by the Caco-2 cells simulating absorption by the inner wall of the small intestine. The method has identified five such highly active milk protein polypeptides.

The invention relates to a method for purifying a target substance starting from a fluid to be treated which comprises at least one impurity. The method comprises treatment of a stream of the fluid to be treated using a chromatography step in a first separation unit, collection of a fraction enriched with the target substance in a first tank, and viral inactivation of the fraction enriched with the target substance. The viral inactivation comprises passing the fraction enriched with the target substance through a second separation unit, passing a viral inactivation solution through the second separation unit, mixing, and collecting the mixture in the second tank to obtain a fraction depleted of active virus. The method further comprises treatment of the fraction depleted of active virus using a chromatography step in the second separation unit and collection of a fraction more enriched with the target substance.

The invention provides a method for producing a host cell protein-(HCP) reduced antibody preparation from a mixture comprising an antibody and at least one HCP, comprising an ion exchange separation step wherein the mixture is subjected to a first ion exchange material, such that the HCP-reduced antibody preparation is obtained.