DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jeong, Gu Min | ko |
dc.contributor.author | Lee, Yong Jae | ko |
dc.contributor.author | Kim, Yong Sung | ko |
dc.contributor.author | Jeong, Ki Jun | ko |
dc.date.accessioned | 2015-01-27T01:56:18Z | - |
dc.date.available | 2015-01-27T01:56:18Z | - |
dc.date.created | 2014-06-23 | - |
dc.date.created | 2014-06-23 | - |
dc.date.issued | 2014-06 | - |
dc.identifier.citation | JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY, v.41, no.6, pp.989 - 996 | - |
dc.identifier.issn | 1367-5435 | - |
dc.identifier.uri | http://hdl.handle.net/10203/193044 | - |
dc.description.abstract | Recently, as a new non-immunoglobulin-based protein scaffold, a human kringle domain was successfully engineered toward biologically functional agonists and antagonists. In this study, the fed-batch cultivation conditions were optimized for enhanced production of an Fc-fused kringle domain (KD548-Fc) in Pichia pastoris. Fed-batch cultivations were performed in 5-l laboratory-scale bioreactors, and in order to find the optimal conditions for high-level production of KD548-Fc, several parameters including the initial carbon source (glycerol) concentration, temperature, and pH were investigated. When cells were cultivated at pH 4.0 and 25 A degrees C with 9.5 % glycerol in the initial medium, the highest production yield (635 mg/l) was achieved with high productivity (7.2 mg/l/h). Furthermore, functional KD548-Fc was successfully purified from the culture broth using a simple purification procedure with high purity and recovery yield. | - |
dc.language | English | - |
dc.publisher | SPRINGER HEIDELBERG | - |
dc.subject | FED-BATCH FERMENTATION | - |
dc.subject | PROTEIN-PRODUCTION | - |
dc.subject | MOLECULAR RECOGNITION | - |
dc.subject | RECOMBINANT PROTEIN | - |
dc.subject | EXPRESSION SYSTEM | - |
dc.subject | BINDING-PROTEINS | - |
dc.subject | DEATH RECEPTORS | - |
dc.subject | OPTIMIZATION | - |
dc.subject | STRATEGIES | - |
dc.subject | ANTIBODIES | - |
dc.title | High-level production of Fc-fused kringle domain in Pichia pastoris | - |
dc.type | Article | - |
dc.identifier.wosid | 000336223200009 | - |
dc.identifier.scopusid | 2-s2.0-84901337926 | - |
dc.type.rims | ART | - |
dc.citation.volume | 41 | - |
dc.citation.issue | 6 | - |
dc.citation.beginningpage | 989 | - |
dc.citation.endingpage | 996 | - |
dc.citation.publicationname | JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY | - |
dc.identifier.doi | 10.1007/s10295-014-1435-2 | - |
dc.contributor.localauthor | Jeong, Ki Jun | - |
dc.contributor.nonIdAuthor | Kim, Yong Sung | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | Kringle domain | - |
dc.subject.keywordAuthor | Fc-fusion protein | - |
dc.subject.keywordAuthor | Pichia pastoris | - |
dc.subject.keywordAuthor | Fed-batch fermentation | - |
dc.subject.keywordPlus | FED-BATCH FERMENTATION | - |
dc.subject.keywordPlus | PROTEIN-PRODUCTION | - |
dc.subject.keywordPlus | MOLECULAR RECOGNITION | - |
dc.subject.keywordPlus | RECOMBINANT PROTEIN | - |
dc.subject.keywordPlus | EXPRESSION SYSTEM | - |
dc.subject.keywordPlus | BINDING-PROTEINS | - |
dc.subject.keywordPlus | DEATH RECEPTORS | - |
dc.subject.keywordPlus | OPTIMIZATION | - |
dc.subject.keywordPlus | STRATEGIES | - |
dc.subject.keywordPlus | ANTIBODIES | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.