Jan, 2010
Artificial chaperone-assisted refolding in a microchannel
BIOPROCESS AND BIOSYSTEMS ENGINEERING
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- Volume
- 33
- Number
- 1
- First page
- 171
- Last page
- 177
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.1007/s00449-009-0374-1
- Publisher
- SPRINGER
Protein refolding using a simple dilution method in a microchannel often led to the formation of protein aggregates, which bound to the microchannel wall, resulting in low refolding yields. To inhibit aggregation and improve refolding yields, an artificial chaperone-assisted (ACA) refolding, which employed detergents and beta-cyclodextrin was used. Model proteins, hen egg white lysozyme and yeast alpha-glucosidase, were successfully refolded in a microchannel. The microscopic observation showed that the ACA method suppressed protein aggregation and facilitated the refolding of lysozyme, whereas significant aggregation was observed when a simple dilution method was employed. The ACA method increased the lysozyme refolding yield by 40% over the simple dilution approach. Similarly, for alpha-glucosidase, the refolding yield using the ACA method (ca. 50%) was approximately three times compared with the simple dilution method. The ACA refolding method is a suitable approach to use in the refolding of proteins using a microfluidic system.
- Link information
- ID information
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- DOI : 10.1007/s00449-009-0374-1
- ISSN : 1615-7591
- Web of Science ID : WOS:000272910600021