Technical refolding of proteins: Do we have freedom to operate?

摘要: Expression as inclusion bodies in Escherichia coli is a widely used method for the large-scale production of therapeutic proteins that do not require post-translational modifications. High expression yields and simple recovery steps from host cells are attractive features industrially. However, value an body-based process dominated by solubilization refolding technologies. Scale-invariant technologies economical applicable wide range requested industry. The main challenge to convert denatured protein into its native conformation at high yields. Refolding competes with misfolding aggregation. Thus, yield monomer depends strongly on initial concentrations solution. Reasonable attained low (≤0.1 mg/mL). large buffer tanks time-consuming concentration required. We attempt answer question extent which protected patents. Low-molecular mass additives have been developed improve through stabilization solution shielding hydrophobic patches. Progress has made field high-pressure renaturation on-column refolding. Mixing times reduced using newly devices introduction specific mixers. Concepts continuous introduced reduce tank sizes increase Some patents covering will soon expire or already expired. This gives more freedom operate.