Pall vows to end bottlenecks in biopharmaceutical manufacturing

By Gregory Roumeliotis

- Last updated on GMT

Related tags Protein

As demand for protein-based drugs increases, Pall has introduced a
new type of mixed-mode chromatography sorbents that make protein
purification faster and cheaper.

Chromatography is one of the most efficient, versatile and viable methods in the biopharmaceutical industry for both laboratory and production scale separation and purification and proteomic applications are shaping up to be a significant driving force in this area.

The sorbents address the downstream production bottlenecks caused by new technologies which have been adopted upstream in biopharmaceutical production and have resulted in increased biomass producing higher concentrations.

Because they do not require lyotropic or other salt additives, Pall's BioSepra PPA and HEA HyperCel sorbents reduce harmful processing conditions that can lead to protein aggregation and impact stability, thus contributing to cost savings by eliminating the expenses associated with salt recycling and waste disposal.

By reducing the need for preparing - and disposing of - complex high salt buffers, and by giving multiple re-use resistance to 1N sodium hydroxide, cost of operations are expected to be significantly reduced as well.

For example, PPA and HEA HyperCel facilitate binding from feedstock or intermediate-stage product pools that cannot be directly applied to traditional ion exchange or hydrophobic interaction chromatography (HIC) sorbents, while also avoiding expensive and environmentally unfriendly salt recycling.

In addition, the ability of these new sorbents to purify many different kinds of molecules allows users to develop platform technologies that can reduce not only the number of process steps, but also costs associated with having to inventory numerous different matrices.

The mixed-mode sorbents can distinguish proteins that have similar or very close isoelectric points, a separation that cannot be achieved with a single ion exchange step.

Moreover, the HIC interaction is achieved at considerably less salt concentrations than that required with traditional HIC.

"These sorbents are competitively priced with traditional HIC sorbents and significantly lower in cost than many affinity matrices,"​ Ian Sellick, Pall's director of marketing, told​.

"This value is added to by the lower cost of ownership."

The ability to adjust selectivity for different proteins enables the sorbents to be used in a wide range of applications, including monoclonal antibodies (MAbs), enzymes, vaccines, recombinant proteins and plasma fractions.

These sorbents are ligands based on phenylpropylamino or hexylamino functional groups, enabling a HIC-like interaction to occur without the need to include lyotropic or other salt additives in the binding step.

They can also be easily packed and unpacked in columns, and can be operated at flow rates up to 1,000 cm per hour with low backpressure, typically less than one bar with a 20 cm bed height.

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