NDLI: Heterologous expression of lipase in Escherichia coli is limited by folding and disulfide bond formation

Content Provider	Springer Nature Link
Author	Xu, Yali Yasin, Amrita Tang, Raymond Scharer, Je M. Moo Young, Murray Chou, C. Perry
Copyright Year	2008
Abstract	Functional expression of lipase B from Pseudozyma antarctica (PalB) in the cytoplasm of Escherichia coli BL21(DE3) and its mutant derivative Origami B(DE3) was explored. Coexpression of DsbA was found to be effective in enhancing PalB expression. The improvement was particularly pronounced with Origami B(DE3) as a host, suggesting that both folding and disulfide bond formation may be major factors limiting PalB expression. Fusion tag technique was also explored by constructing several PalB fusions for the evaluation of their expression performance. While the solubility was enhanced for most PalB fusions, only the DsbA tag was effective in boosting PalB activity, possibly by both enhanced solubility and correct disulfide bond formation. Our results suggest that PalB activity is closely associated with correct disulfide bond formation, and increased solubilization by PalB fusions does not necessarily result in activity enhancement.
Starting Page	79
Ending Page	87
Page Count	9
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	81
Issue Number	1
e-ISSN	14320614
Language	English
Publisher	Springer-Verlag
Publisher Date	2008-08-29
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Disulfide bond formation Fusion tag Escherichia coli Lipase Recombinant protein production Microbial Genetics and Genomics Microbiology Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

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Heterologous expression of lipase in Escherichia coli is limited by folding and disulfide bond formation