Journal
CHEMBIOCHEM
Volume 16, Issue 3, Pages 393-396Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201402427
Keywords
green chemistry; protein expression; protein folding; shear stress
Funding
- National Institute of General Medical Sciences of the NIH [R01 GM100700-01]
- Australian Research Council [ARC DP1092810, DP130100066]
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Recombinant protein overexpression of large proteins in bacteria often results in insoluble and misfolded proteins directed to inclusion bodies. We report the application of shear stress in micrometer-wide, thin fluid films to refold boiled hen egg white lysozyme, recombinant hen egg white lysozyme, and recombinant caveolin-1. Furthermore, the approach allowed refolding of a much larger protein, cAMP-dependent protein kinase A (PKA). The reported methods require only minutes, which is more than 100 times faster than conventional overnight dialysis. This rapid refolding technique could significantly shorten times, lower costs, and reduce waste streams associated with protein expression for a wide range of industrial and research applications.
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