University of California

Callum Ormonde

Gregory A Weiss

Colin L Raston

Stephan Timothy Kudlacek

Tom Z Yuan

A method of improving protein functionality includes obtaining a protein such as protein contained within exclusion bodies contained within bacteria or yeast used for the recombinant expression of the protein. The exclusion bodies are solubilized using a chaotropic agent such as guanidine or urea. The protein is then subject to denaturation conditions and optionally purified. A liquid containing the denatured protein is loaded into a vessel that is angled relative to horizontal. The vessel is then rotated in the angled configuration at a rate within that is less than 10,000 RPM for period of time. Refolded protein is formed by the high shear conditions formed in the thin film of fluid formed in the inner surface of the rotating vessel. Refolding can be performed in a batch mode or a continuous mode. The process may be scaled up for industrial applications by using multiple vessels.

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Nedlands, WA, United States of America

Callum Ormonde