Designing a purification step for a complex target molecule is challenging as the tentative combinations of conditions and chromatography media (resins) are many. One of the responses of major interest in an intermediate purification step is selectivity. This presentation will focus on the methodology used to design a step that follows on enzymatic cleavage of pro-insulin into main product, insulin, and the C-peptide. In order to speed up process development and keep sample amounts low it is advantageous to use a parallel format with low resin volumes. The 96-well batch format meets these demands and was used to screen for most promising resins and conditions, both with respect to yield and purity. The knowledge gained from an elution study utilizing 20 �l resin per well, followed by optimization in small columns, was scaled up to a  400 mL column scale intermediate purification of insulin to more than 90% purity.

Development of intermediate purification step in insulin process using a high throughput approach

245th National Meeting (2013)

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