If one sterilizes pre-packed, plastic chromatography columns with an appropriate level of gamma irradiation, the resulting sterile chromatography columns maintain sufficient packing media function and maintain column mechanical properties and pressure ratings.

The invention discloses a functionalised chromatography medium, comprising: i) at least one non-woven layer (10) of polymeric nano fibres (20) comprising a plurality of nanofibre-nano fibre fusion points (30); ii) a grafted polymer coating covering the polymeric nanofibres and the nanofibre-nanofibre fusion points; iii) a plurality of ligand groups covalently bound to the grafted polymer coating, wherein the ligand groups are capable of interacting with a target biomolecule.

The present invention is directed to methods of purifying viral proteins for use in vaccine compositions. The method includes a capture step and a polish step. The capture step includes passing a solution containing a protein over a hydrophobic interaction chromatography column and eluting a crude protein eluate from the column. The polish step includes passing the crude protein eluate over a ligand affinity chromatography column and recovering a first flow through intermediate, passing the first flow through intermediate over an anion exchange chromatography column and recovering a second flow through intermediate, and passing the second flow through intermediate over another ligand affinity chromatography column and recovering a purified protein eluate. The present invention also provides a purified protein having a hydrophobic membrane domain that is produced by a baculovirus expression system in cultured insect cells, wherein the purified protein has a purity of greater than 85%.

The invention relates to a method for controlling preparative liquid chromatography, comprising the following steps, at least a part of said steps being implemented by a computer comprising a processor and a display screen coupled to said processor: (a) selecting an analytical liquid chromatography method from among thin layer chromatography (TLC) and high performance liquid chromatography (HPLC), (b) inputting analytical liquid chromatography data obtained by the method selected at step (a) for a product to be purified, (c) accessing a table of separating tools available to the user to implement said preparative liquid chromatography, (d) from said analytical liquid chromatography data and table of available separating tools, selecting an optimal separating tool from said table and computing preparative liquid chromatography operating conditions for said selected separating tool.

Chromatography resins having anionic exchange-hydrophobic mixed mode ligands and methods of using such resins are provided.

Chromatography resins having anionic exchange-hydrophobic mixed mode ligands and methods of using such resins are provided.

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 ml 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 is within the field of chromatography. More precisely, it relates to a novel chromatography medium, namely a hydrophobic medium provided with different lids excluding molecules over a certain size due to the porosity of the hydrophobic medium and/or the porosity of the lid. The invention also relates to use of the separation medium for purification of large molecules, which do not enter the separation medium, as well as small molecules, which enter the separation medium and are eluted from there.

The present invention relates to a process for purifying crude NADPH product prepared by biocatalysis. The objective of the present invention is to solve the technical problems of low yield and low purity of the purified product in the existing ion exchange resin method. The present invention comprises sequentially the following steps: pretreatment, loading onto an ion column, elution of cations, pre-elution of impurities etc. The yield of the purification process disclosed in the present invention can be up to 85% or higher and the purified NADPH has a purity of up to 98% or higher.

Provided herein is a method and system for PFAS analysis using a liquid chromatography technique that employ a first column (e.g., an isolator column) and a second column (e.g., an analytical column), wherein at least one of the first column, the second column, or both the first and second columns include mixed mode with anion exchange surface chemistry. The devices and methods provided herein are useful for improving the efficiency and/or sensitivity of systems implementing liquid chromatography for PFAS analysis. The methods of the present disclosure are particularly beneficial for trace level (e.g., ppm level or lower) analysis of PFAS. Further, the methods of the present disclosure allow improved separation of short-chain and ultrashort-chain PFAS.