Heterologous expression of lipase in Escherichia coli is limited by folding and disulfide bond formation
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 Orig...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2008-11, Vol.81 (1), p.79-87 |
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| creator | Xu, Yali Yasin, Amrita Tang, Raymond Scharer, Jeno M Moo-Young, Murray Chou, C. Perry |
| description | 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. |
| doi_str_mv | 10.1007/s00253-008-1644-6 |
| format | Article |
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Psychology ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Fusion tag ; Gene Expression ; Genetics ; Life Sciences ; Lipase - chemistry ; Lipase - genetics ; Lipase - metabolism ; Microbial Genetics and Genomics ; Microbiology ; Mutation ; Oils & fats ; Plasmids ; Protein Disulfide-Isomerases - genetics ; Protein Disulfide-Isomerases - metabolism ; Protein Folding ; Protein Processing, Post-Translational ; Pseudozyma antarctica ; Recombinant Fusion Proteins ; Recombinant protein production ; Solubility ; Studies ; triacylglycerol lipase ; Yeast</subject><ispartof>Applied microbiology and biotechnology, 2008-11, Vol.81 (1), p.79-87</ispartof><rights>Springer-Verlag 2008</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-86b4eb316ea65a30a723034678991675ffebe2c6f4f59158cfc2ac02dde8caed3</citedby><cites>FETCH-LOGICAL-c520t-86b4eb316ea65a30a723034678991675ffebe2c6f4f59158cfc2ac02dde8caed3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-008-1644-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-008-1644-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21017809$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18758768$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xu, Yali</creatorcontrib><creatorcontrib>Yasin, Amrita</creatorcontrib><creatorcontrib>Tang, Raymond</creatorcontrib><creatorcontrib>Scharer, Jeno M</creatorcontrib><creatorcontrib>Moo-Young, Murray</creatorcontrib><creatorcontrib>Chou, C. Perry</creatorcontrib><title>Heterologous expression of lipase in Escherichia coli is limited by folding and disulfide bond formation</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>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.</description><subject>Applied Genetics and Molecular Biotechnology</subject><subject>Basidiomycota - enzymology</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chemical bonds</subject><subject>Cloning</subject><subject>Cytoplasm</subject><subject>Cytoplasm - genetics</subject><subject>Cytoplasm - metabolism</subject><subject>Disulfide bond formation</subject><subject>Disulfides - chemistry</subject><subject>Disulfides - metabolism</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. 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Perry</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heterologous expression of lipase in Escherichia coli is limited by folding and disulfide bond formation</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2008-11-01</date><risdate>2008</risdate><volume>81</volume><issue>1</issue><spage>79</spage><epage>87</epage><pages>79-87</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><coden>AMBIDG</coden><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.</abstract><cop>Berlin/Heidelberg</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><pmid>18758768</pmid><doi>10.1007/s00253-008-1644-6</doi><tpages>9</tpages></addata></record> |
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| subjects | Applied Genetics and Molecular Biotechnology Basidiomycota - enzymology Biological and medical sciences Biotechnology Chemical bonds Cloning Cytoplasm Cytoplasm - genetics Cytoplasm - metabolism Disulfide bond formation Disulfides - chemistry Disulfides - metabolism E coli Enzymes Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Fusion tag Gene Expression Genetics Life Sciences Lipase - chemistry Lipase - genetics Lipase - metabolism Microbial Genetics and Genomics Microbiology Mutation Oils & fats Plasmids Protein Disulfide-Isomerases - genetics Protein Disulfide-Isomerases - metabolism Protein Folding Protein Processing, Post-Translational Pseudozyma antarctica Recombinant Fusion Proteins Recombinant protein production Solubility Studies triacylglycerol lipase Yeast |
| title | Heterologous expression of lipase in Escherichia coli is limited by folding and disulfide bond formation |
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