Affibody® molecules are small affinity proteins with great opportunities in the application of biotechnological areas. Their popularity as biomolecules in pharmaceutical applications and research entails that the purity of Affibody® molecules is essential for their use as safe medical drugs. Hydrophobic Interaction Chromatography (HIC) is a purification technique that separates molecules based on their inherent difference in hydrophobicity, and the application as a purification strategy for Affibody® molecules may be possible. This thesis investigates the implementation of HIC on Affibody® molecules by screening for differences in binding, recovery, and purity influenced by different parameters, such as resin, pH, salt type, and salt concentration, have on binding, recovery, and purity. HIC presents as a viable purification method where an approximate 97% reduction in Host Cell Proteins was obtained. The yield of the purified product also presented as promising with a recovery of approximately 82%. These results indicate that further investigation and optimization of this technique may benefit the downstream process of the investigated Affibody® molecule.
| Identifer | oai:union.ndltd.org:UPSALLA1/oai:DiVA.org:uu-415045 |
| Date | January 2020 |
| Creators | Persson, Sebastian |
| Publisher | Uppsala universitet, Institutionen för biologisk grundutbildning |
| Source Sets | DiVA Archive at Upsalla University |
| Language | English |
| Detected Language | English |
| Type | Student thesis, info:eu-repo/semantics/bachelorThesis, text |
| Format | application/pdf |
| Rights | info:eu-repo/semantics/openAccess |
| Relation | UPTEC X ; 20007 |
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