The invention discloses a separation matrix comprising a plurality of multimodal ligands covalently coupled to a support, wherein said support is a membrane comprising nonwoven polymer fibers and wherein said ligands are capable of interacting with a target biomacromolecule. Further, the invention discloses separation methods using the separation matrix.

A molded body includes a shape memory material. The molded body has a three-dimensional surface structure which, in a permanent shape, at least in part has a superhydrophobic surface and/or a hydrophobic surface, on which water droplet contact angles of 120° to 150° are found.

The present invention describes a simple purification process for recombinant human serum albumin. The process results in highly purified protein with limited number of purification steps. The broth containing human albumin is clarified by centrifugation and microfiltration, diafiltered and captured by cation exchange chromatography by a process that allows 140-230 mg of albumin to be captured per mi of resin. Product related impurities are removed by hydrophobic interaction chromatography, optimised to allow 87-97% recovery in flow through mode. The final series of processes are so combined that there is easy transition from one step to the next with minimal interventions and adjustments. The entire process of purification is completed within two days from harvest to final product. Thus a cost-effective process with improved recovery of protein at each step is developed. The purified human serum albumin is analyzed for purity and shows physicochemical characteristics that are similar to standard albumin.

The present invention refers to a method for the separation of peptide aggregates and fragments from solutions containing target peptide.

Chromatography resins having mixed mode ligands and methods of using such resins are provided.

Chromatography resins having mixed mode ligands and methods of using such resins are provided.

A method for depletion or removal of endotoxins from a known or suspected endotoxin-containing source by virtue of a solid phase extraction material in an essentially aqueous system comprising the steps of—providing a known or suspected endotoxin-containing source, —contacting the known or suspected endotoxin-containing source with a positively charged solid phase material having a surface on which ferric iron is immobilised, wherein the solid phase extraction material has immobilised the ferric iron by (2-aminoethyl)amine (TREN) ligand—incubating the known or suspected endotoxin-containing source for a period of time sufficient to bind endotoxin to the porous solid phase material, —separating the solid phase material from the essentially aqueous system, —optionally isolating the essentially aqueous system freed or depleted from endotoxin.

The present invention relates to a method for separating at least one soluble protein fraction from an aggregated casein-containing material, the method comprises the steps of: (i) providing the aggregated casein-containing material; (ii) Contacting the aggregated casein-containing material with a chromatographic support allowing one or more soluble protein(s) present in the aggregated casein-containing material to be retained by the chromatographic support; (iii) Obtaining a permeate fraction from the chromatographic support comprising aggregated casein; (iv) Optionally washing the chromatographic support; (v) Subjecting the chromatographic support to at least one elution buffer obtaining at least one soluble protein fraction from the chromatographic support; and wherein the chromatographic support comprises one or more mixed-mode ligands capable of binding the soluble proteins from the aggregated casein-containing material.

The present invention relates to a method for separating at least one soluble protein fraction from an aggregated casein-containing material, the method comprises the steps of: (i) providing the aggregated casein-containing material; (ii) Contacting the aggregated casein-containing material with a chromatographic support allowing one or more soluble protein(s) present in the aggregated casein-containing material to be retained by the chromatographic support; (iii) Obtaining a permeate fraction from the chromatographic support comprising aggregated casein; (iv) Optionally washing the chromatographic support; (v) Subjecting the chromatographic support to at least one elution buffer obtaining at least one soluble protein fraction from the chromatographic support; and wherein the chromatographic support comprises one or more mixed-mode ligands capable of binding the soluble proteins from the aggregated casein-containing material.

A bioprocessing system for protein manufacturing from human blood is provided that is compact, integrated and suited for on-demand production and delivery of therapeutic proteins to patients. The patient's own blood can be used as the source of cell extracts for the production of the therapeutic proteins.