Harnessing Bacterial IBs for Recombinant Protein Production

Bacterial inclusion bodies (IBs) in recombinant protein production offer ease of separation, stability, high expression, and degradation resistance, and can express toxic proteins with biological activity. Advances in IB understanding open new avenues for processing, with challenges and solutions identified for future research.

Yaohai Bio-Pharma has more than 10 years of experience in the production of recombinant proteins using microbial fermentation systems. Our strong and professional team of experts guarantees that the purified refolded protein can reach 1.5 g/L.

Processing Strategies and Challenges of IBs

Separation of IBs Methods for IB separation depend on protein structure-function and application needs. Physical methods disrupt cells but may harm protein quality. Enzymatic methods improve purity but are costly. Gentle detergents work for classical IBs, not non-classical. pH control is crucial for solubility. Electrophoresis deposition is simple but not scalable for biologically active proteins.

Solubilization of IBs Solubilizing IBs is crucial for recovering active proteins. Strong denaturants damage native structure, while non-denaturants are not suitable for classical IBs. Gentle solubilizers can dissolve IBs while protecting protein structure, but not all proteins. Future work needs better algorithms to select solubilizers.

Renaturation Strategies Protein renaturation is vital for functionality. In vitro renaturation faces challenges. Solubilizer choice, protein concentration, conditions, and methods affect outcome. Gentle solubilizers protect native structure and improve quality. Moderate concentrations and optimized conditions reduce aggregation. Column-based methods with monolithic matrices offer higher purity and yield.

Purification of Renatured Proteins Further purification separates misfolded from correctly folded proteins. Traditional chromatography struggles with similar proteins. Alternative methods offer advantages but require target protein-specific selection. Developing a universal purification method remains a challenge.

Conclusion

IBs offer advantages in recombinant protein production but pose processing challenges. With a deeper understanding of protein structure-function within IBs and advancements in separation, solubilization, renaturation, and purification, high-throughput recovery of active proteins may soon be achieved. This will lower costs and accelerate biopharmaceutical R&D, driving industry growth.

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