However, some of this advantage is lost if the feed is a mixture of BSA and Tg since, in this case, Tg binding leads to greater diffusional hindrance for BSA.Ĭore-shell resins Diffusional hindrance Dynamic binding capacity Flow-through purification Modeling.Ĭopyright © 2021. Column measurements show that, despite the higher static capacity of Capto Core 400 for BSA, the dynamic binding capacity is greater for Capto Core 700 as a result of its faster kinetics. Adsorbed Tg further hinders diffusion of BSA in both resins. These values decrease dramatically for Tg to 0.022 × 10 -7 and 0.088 × 10 -7 cm 2/s and to 0.13 × 10 -7 and 0.59 × 10 -7 cm 2/s for Capto Core 400 and 700, respectively. For BSA, core and shell effective pore diffusivities are about 0.25 × 10 -7 and 0.6 × 10 -7 cm 2/s, respectively, for Capto Core 400, and about 1.6 × 10 -7 and 2.6 × 10 -7 cm 2/s, respectively, for Capto Core 700. Mass transfer in both resins is affected by diffusional resistances through the shell and within the adsorbing core. However, for the much larger Tg, the attainable capacity is substantially larger for Capto Core 700. Because of the smaller pores and higher surface area, the BSA binding capacity of Capto Core 400 is approximately double that of Capto Core 700. Although shell thicknesses are comparable (3.6 and 4.2 µm for Capto Core 400 and 700, respectively), the two resins differ substantially in pore size (pore radii of 19 and 50 nm, respectively). ![]() ![]() ![]() The 400 and 700 reflect the MWCO of the outer. We have Capto Core 400 and Capto Core 700. The virus will pass through due to the size, and the impurities will go into the pores and bind the ligand (octylamine) inside. Both resins are agarose-based and contain an adsorbing core surrounded by an inert shell. How does Capto Core technology work for AAV purification This is a flow-through procedure. Structural and functional characteristics of the two core-shell resins Capto™ Core 400 and 700, which are useful for the flow-through purification of bioparticles such as viruses, viral vectors, and vaccines, are compared using bovine serum albumin (BSA) and thyroglobulin (Tg) as models for small and large protein contaminants.
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