| pubmed-article:16133338 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16133338 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:16133338 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:16133338 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:16133338 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
| pubmed-article:16133338 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16133338 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:16133338 | lifeskim:mentions | umls-concept:C0870432 | lld:lifeskim |
| pubmed-article:16133338 | lifeskim:mentions | umls-concept:C0185125 | lld:lifeskim |
| pubmed-article:16133338 | lifeskim:mentions | umls-concept:C1705417 | lld:lifeskim |
| pubmed-article:16133338 | lifeskim:mentions | umls-concept:C1555465 | lld:lifeskim |
| pubmed-article:16133338 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:16133338 | pubmed:dateCreated | 2006-4-7 | lld:pubmed |
| pubmed-article:16133338 | pubmed:abstractText | We have developed a novel Escherichia coli cell surface display system by employing PgsA as an anchoring motif. In our display system, C-terminal fusion to PgsA anchor protein from Bacillus subtilis was used. The enzymes selected for display were alpha-amylase (AmyA) from Streptococcus bovis 148 and lipase B (CALB) from Candida antarctica. The molecular mass values of AmyA and CALB are approximately 77 and 34 kDa, respectively. The enzymes were displayed on the surface as a fusion protein with a FLAG peptide tag at the C terminus. Both the PgsA-AmyA-FLAG and PgsA-CALB-FLAG fusion proteins were shown to be displayed by immunofluorescence labeling using anti-FLAG antibody. The displayed enzymes were active forms, and AmyA and CALB activities reached 990 U/g (dry cell weight) and 4.6 U/g (dry cell weight), respectively. AmyA-displaying E. coli cells grew utilizing cornstarch as the sole carbon source, while CALB-displaying E. coli cells catalyzed enantioselective transesterification, indicating that they are effective whole-cell biocatalysts. Since a target enzyme with a size of 77 kDa and an industrially useful lipase have been successfully displayed on the cell surface of E. coli for the first time, PgsA protein is probably a useful anchoring motif to display various enzymes. | lld:pubmed |
| pubmed-article:16133338 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16133338 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16133338 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16133338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16133338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16133338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16133338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16133338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16133338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16133338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16133338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16133338 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16133338 | pubmed:month | May | lld:pubmed |
| pubmed-article:16133338 | pubmed:issn | 0175-7598 | lld:pubmed |
| pubmed-article:16133338 | pubmed:author | pubmed-author:SungMoon-HeeM... | lld:pubmed |
| pubmed-article:16133338 | pubmed:author | pubmed-author:FukudaHidekiH | lld:pubmed |
| pubmed-article:16133338 | pubmed:author | pubmed-author:KondoAkihikoA | lld:pubmed |
| pubmed-article:16133338 | pubmed:author | pubmed-author:NaritaJunyaJ | lld:pubmed |
| pubmed-article:16133338 | pubmed:author | pubmed-author:OkanoKenjiK | lld:pubmed |
| pubmed-article:16133338 | pubmed:author | pubmed-author:SewakiTomomit... | lld:pubmed |
| pubmed-article:16133338 | pubmed:author | pubmed-author:TatenoToshihi... | lld:pubmed |
| pubmed-article:16133338 | pubmed:author | pubmed-author:TaninoTakanor... | lld:pubmed |
| pubmed-article:16133338 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16133338 | pubmed:volume | 70 | lld:pubmed |
| pubmed-article:16133338 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16133338 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16133338 | pubmed:pagination | 564-72 | lld:pubmed |
| pubmed-article:16133338 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:16133338 | pubmed:meshHeading | pubmed-meshheading:16133338... | lld:pubmed |
| pubmed-article:16133338 | pubmed:meshHeading | pubmed-meshheading:16133338... | lld:pubmed |
| pubmed-article:16133338 | pubmed:meshHeading | pubmed-meshheading:16133338... | lld:pubmed |
| pubmed-article:16133338 | pubmed:meshHeading | pubmed-meshheading:16133338... | lld:pubmed |
| pubmed-article:16133338 | pubmed:meshHeading | pubmed-meshheading:16133338... | lld:pubmed |
| pubmed-article:16133338 | pubmed:meshHeading | pubmed-meshheading:16133338... | lld:pubmed |
| pubmed-article:16133338 | pubmed:meshHeading | pubmed-meshheading:16133338... | lld:pubmed |
| pubmed-article:16133338 | pubmed:meshHeading | pubmed-meshheading:16133338... | lld:pubmed |
| pubmed-article:16133338 | pubmed:meshHeading | pubmed-meshheading:16133338... | lld:pubmed |
| pubmed-article:16133338 | pubmed:meshHeading | pubmed-meshheading:16133338... | lld:pubmed |
| pubmed-article:16133338 | pubmed:meshHeading | pubmed-meshheading:16133338... | lld:pubmed |
| pubmed-article:16133338 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16133338 | pubmed:articleTitle | Display of active enzymes on the cell surface of Escherichia coli using PgsA anchor protein and their application to bioconversion. | lld:pubmed |
| pubmed-article:16133338 | pubmed:affiliation | Division of Molecular Science, Graduate School of Science and Technology, Kobe University, Nada-ku, Kobe, 657-8501, Japan. | lld:pubmed |
| pubmed-article:16133338 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16133338 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:945791 | entrezgene:pubmed | pubmed-article:16133338 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16133338 | lld:entrezgene |
