Overview

Protein crystallisation is an emerging purification technology in the downstream processing of therapeutic proteins, where the state-of-the-art purification technology is chromatography.

Using bovine serum albumin (BSA) as the impurity protein and lysozyme as the model protein, experimental results showed that the impurity protein could raise the solubility of the model protein and hence reduce the recovery yield of crystallisation in agreement with previous study.

The non-specific protein-protein interactions between lysozyme and BSA under different conditions were studied with small angle X-ray scattering (SAXS) to identify conditions that minimized the effects of impurity (i.e. BSA) on the solubility of lysozyme.

Speaker

Chen Wenqian, Assistant Professor, National University of Singapore

Chen obtained his MEng and PhD in chemical engineering from Imperial College London. Chen specialises in protein and peptide crystallisation for purification and formulation purposes.

The material presented has not been peer-reviewed. Any opinions are the presenter’s own and do not necessarily represent those of IChemE or the Biochemical Engineering Special Interest Group. The information is given in good faith but without any liability on the part of IChemE.

Time

09:00–10:00 GMT.

Software 

The presentation will be delivered via Microsoft Teams. We recommend downloading the app from the Microsoft website, rather than using the web portal.