A method for separating, purifying, and recovering components from a liquid feedstock. The method steps include (i) commingling the liquid feedstock with a sorbent whereby one or more components in the liquid feedstock are bound onto the sorbent, thereby producing a loaded sorbent; (ii) packing the loaded sorbent into a first temperature-controlled pressure-resistant column; (iii) sealably engaging the first temperature-controlled pressure-resistant column with a supply of water, and cooling equipment for receiving a flow of an eluate from the temperature-controlled pressure-resistant column; (iv) from the supply of water, producing a first flow of PLP water at a first selected temperature; (v) flowing the first flow of PLP water through the temperature-controlled pressure-resistant column thereby producing a first flow of the eluate therefrom, said eluate containing the one or more components; (vi) cooling the first flow of the eluate; and (vii) collecting the cooled first flow of the eluate.

The solution provides a method for separating a Chinese traditional medicine composition. To explain a pharmacological effect mechanism of a medicine made of two or more components and scientific content in rules of compatibility among components of a compound medicine, systematic researches on the material basis is very necessary. Accordingly, deep researches are done on chemical components of the pharmaceutical composition in the solution, and eight compounds are separated, which are 10-O-(p-hydroxycinnamoyl)-adoxosidic acid, aloe-emodin-8-O--D-glucopyranoside, quercitrin, matairesinol-4-O-glucoside, liquiritin apioside, epi-vogeloside, vogeloside and ethyl caffeate, which provides a new quality control method for the composition in the solution.

There is provided a method and a corresponding system for determining binding capacities of a chromatography column. The method includes detecting a feed signal representative of the composition of a feed material provided to the inlet of the column. The method further includes detecting an effluent signal representative of the composition of the effluent from the column. The method further includes using the feed signal and the effluent signal to determine binding capacities of the column.

The present invention refers to a method of purifying a glucagon-like peptide 1 analogs, the method comprising a two dimensional reversed phase high performance liquid chromatography protocol, wherein the first step is carried out at a pH value between 7.0 to 7.8 using a mobile phase comprising a phosphate buffer and acetonitrile, and the second step is carried out at a pH value below 3.0 using a mobile phase comprising trifluoroacetic acid and acetonitrile.

Provided herein are methods of performing chromatography with gamma-irradiated chromatography resin that include providing a chromatography column including a gamma-irradiated chromatography resin; performing a first cycle of chromatography through the column, where the cycle includes exposing the chromatography resin to a denaturing buffer; and performing at least one additional cycle of chromatography through the column. Also provided are integrated, closed or substantially closed, and continuous processes for manufacturing of a recombinant protein that include the use of at least one chromatography column including gamma-irradiated chromatography resin, where the gamma-irradiated chromatography resin is exposed to denaturing buffer during each cycle in the process, and reduced bioburden buffer is used in the process.

A method for monitoring, evaluating and controlling a cyclic chromatographic purification process that involves at least two adsorbers. According to the method, one step is monitoring of the chromatogram, including the measurement of at least one current concentration-proportional signal in the liquid. Another step is conducting an evaluation of the chromatogram, including a comparison of at least one of the current concentration-proportional signals measured in the monitoring step with a threshold value thereof. A further step is controlling the chromatographic purification process by adapting the termination of the currently running phase as a function of the comparison of the evaluation step and initiating the next phase. Finally, according to the method, the sequence of steps is carried out in given order at least twice.

The invention relates to a method of isolating an immunoglobulin, comprising the steps of: a) providing a separation matrix comprising at least 15 mg/ml multimers of immunoglobulin-binding alkali-stabilized Protein A domains covalently coupled to a porous support, wherein the porous support comprises cross-linked polymer particles having a volume-weighted median diameter (d50,v) of 56-70 micrometers and a dry solids weight of 55-80 mg/ml; b) contacting a liquid sample comprising an immunoglobulin with the separation matrix; c) washing the separation matrix with a washing liquid; d) eluting the immunoglobulin from the separation matrix with an elution liquid; and e) cleaning the separation matrix with a cleaning liquid comprising at least 0.5 M NaOH.

Provided herein are integrated continuous biomanufacturing processes for producing a therapeutic protein drug substance. Also provided are systems that are capable of continuously producing a therapeutic protein drug substance.

The present disclosure relates to methods and systems for the continuous production of recombinant proteins. In particular embodiments, the disclosure relates to methods and systems using capture chromatography, post-capture chromatography, virus filtration, and ultrafiltration/diafiltration for the continuous production of recombinant proteins.

The invention relates to a method of isolating an immunoglobulin, comprising the steps of: a) providing a separation matrix comprising at least 15 mg/ml multimers of immunoglobulin-binding alkali-stabilized Protein A domains covalently coupled to a porous support, wherein the porous support comprises cross-linked polymer particles having a volume-weighted median diameter (d50,v) of 56-70 micrometers and a dry solids weight of 55-80 mg/ml; b) contacting a liquid sample comprising an immunoglobulin with the separation matrix; c) washing the separation matrix with a washing liquid; d) eluting the immunoglobulin from the separation matrix with an elution liquid; and e) cleaning the separation matrix with a cleaning liquid comprising at least 0.5 M NaOH.