Abstract
Foam fractionation by itself cannot effectively concentrate hydrophilic proteins such as lysozyme and cellulase. However, the addition of a detergent to a protein solution can increase the foam volume, and thus, the performance of the foam fractionation process. In this article, we propose a possible protein concentration mechanism of this detergent-assisted foam fractionation: A detergent binds to an oppositely charged protein, followed by the detergent—protein complex being adsorbed onto a bubble during aeration. The formation of this complex is inferred by a decrease in surface tension of the detergent—protein solution. The surface tension of a solution with the complex is lower than the surface tension of a protein or a detergent solution alone. The detergent can then be stripped from the adsorbed protein, such as cellulase, by an artificial chaperone such as β-cyclodextrin. Stripping the detergent from the protein allows the protein to return to its original conformation and to potentially retain all of its original activity following the foam fractionation process. Low-cost alternatives to β-cyclodextrin such as corn dextrin were tested experimentally to restore the protein activity through detergent stripping, but without success.
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Burapatana, V., Booth, E.A., Snyder, I.M., Prokop, A., Tanner, R.D. (2007). A Proposed Mechanism for Detergent-Assisted Foam Fractionation of Lysozyme and Cellulase Restored With β-Cyclodextrin. In: Mielenz, J.R., Klasson, K.T., Adney, W.S., McMillan, J.D. (eds) Applied Biochemistry and Biotecnology. ABAB Symposium. Humana Press. https://doi.org/10.1007/978-1-60327-181-3_64
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DOI: https://doi.org/10.1007/978-1-60327-181-3_64
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