Polycationic amino acid tags enhance soluble expression of Candida antarctica lipase B in recombinant Escherichia coli
DC Field | Value | Language |
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dc.contributor.author | Jung, Hyun-Jung | - |
dc.contributor.author | Kim, Sun-Ki | - |
dc.contributor.author | Min, Won-Ki | - |
dc.contributor.author | Lee, Sung-Suk | - |
dc.contributor.author | Park, Kyungmoon | - |
dc.contributor.author | Park, Yong-Cheol | - |
dc.contributor.author | Seo, Jin-Ho | - |
dc.date.accessioned | 2021-12-15T02:42:02Z | - |
dc.date.available | 2021-12-15T02:42:02Z | - |
dc.date.created | 2021-12-10 | - |
dc.date.issued | 2011-09 | - |
dc.identifier.issn | 1615-7591 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hongik/handle/2020.sw.hongik/19817 | - |
dc.description.abstract | Lipase (EC 3.1.1.3) is a popular enzyme used as an ingredient in detergents and biocatalyst in many biochemical reactions. Lipase is usually expressed in Escherichia coli as an inactive inclusion body and at a low level. In this study, Candida antarctica lipase B (CalB) was fused with various polycationic amino acid tags and expressed in E. coli in order to increase a soluble expression level. By induction with 1.0 mM IPTG, the authentic and fused CalBs were expressed at 27-56% of total protein. The 10-arginine and 10-lysine tags fused at the C-terminal of CalB significantly increased the solubility of CalB by five- to ninefold, relative to the case of the authentic CalB expressed in a recombinant E. coli Origami 2(TM) (DE3) strain. Among a series of the C-terminal poly-arginine tags, the recombinant CalB combined with the 10-arginine tag (CalB-R10) possessed the highest lipase specific activity of 9.5 +/- A 0.03 U/mg protein, corresponding to a fourfold enhancement compared with the authentic CalB. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | SPRINGER | - |
dc.subject | DISULFIDE BOND FORMATION | - |
dc.subject | FUNCTIONAL EXPRESSION | - |
dc.subject | CATION-EXCHANGER | - |
dc.subject | CLONING | - |
dc.subject | CYTOPLASM | - |
dc.subject | PROTEINS | - |
dc.subject | SYSTEM | - |
dc.subject | YIELD | - |
dc.title | Polycationic amino acid tags enhance soluble expression of Candida antarctica lipase B in recombinant Escherichia coli | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Park, Kyungmoon | - |
dc.identifier.doi | 10.1007/s00449-011-0533-z | - |
dc.identifier.scopusid | 2-s2.0-80052378833 | - |
dc.identifier.wosid | 000293896200007 | - |
dc.identifier.bibliographicCitation | BIOPROCESS AND BIOSYSTEMS ENGINEERING, v.34, no.7, pp.833 - 839 | - |
dc.relation.isPartOf | BIOPROCESS AND BIOSYSTEMS ENGINEERING | - |
dc.citation.title | BIOPROCESS AND BIOSYSTEMS ENGINEERING | - |
dc.citation.volume | 34 | - |
dc.citation.number | 7 | - |
dc.citation.startPage | 833 | - |
dc.citation.endPage | 839 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Engineering | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Engineering, Chemical | - |
dc.subject.keywordPlus | DISULFIDE BOND FORMATION | - |
dc.subject.keywordPlus | FUNCTIONAL EXPRESSION | - |
dc.subject.keywordPlus | CATION-EXCHANGER | - |
dc.subject.keywordPlus | CLONING | - |
dc.subject.keywordPlus | CYTOPLASM | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordPlus | YIELD | - |
dc.subject.keywordAuthor | Candida antarctica lipase B | - |
dc.subject.keywordAuthor | Escherichia coli | - |
dc.subject.keywordAuthor | Polycationic amino acid tag | - |
dc.subject.keywordAuthor | Soluble expression | - |
dc.subject.keywordAuthor | Inclusion body | - |
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