Cited 9 time in
Cloning and Expression of a bpr Gene Encoding Bacillopeptidase F from Bacillus amyloliquefaciens CH86-1
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Kwon, Gun-Hee | - |
| dc.contributor.author | Park, Jae-Yong | - |
| dc.contributor.author | Kim, Jong-Sang | - |
| dc.contributor.author | Lim, Jinkyu | - |
| dc.contributor.author | Park, Cheon-Seok | - |
| dc.contributor.author | Kwon, Dae Young | - |
| dc.contributor.author | Kim, Jeong Hwan | - |
| dc.date.accessioned | 2022-12-27T03:05:52Z | - |
| dc.date.available | 2022-12-27T03:05:52Z | - |
| dc.date.issued | 2011-05 | - |
| dc.identifier.issn | 1017-7825 | - |
| dc.identifier.issn | 1738-8872 | - |
| dc.identifier.uri | https://scholarworks.gnu.ac.kr/handle/sw.gnu/23744 | - |
| dc.description.abstract | A gene encoding bacillopeptidase F, bpr86-1, was cloned from B. amyloliquefaciens CH86-1 isolated from cheonggukjang. This gene could encode a preproenzyme of 1,431 amino acids. When bpr86-1 was introduced into B. subtilis WB600 via pHY300PLK, an E. coli Bacillus shuttle vector, the transformant showed fibrinolytic activity. During growth on LB, the fibrinolytic activity of cells increased sharply when they entered the stationary phase. The highest activity (761.4 mU/mg protein) was observed at 96 h of cultivation. | - |
| dc.format.extent | 4 | - |
| dc.language | 영어 | - |
| dc.language.iso | ENG | - |
| dc.publisher | KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY | - |
| dc.title | Cloning and Expression of a bpr Gene Encoding Bacillopeptidase F from Bacillus amyloliquefaciens CH86-1 | - |
| dc.type | Article | - |
| dc.publisher.location | 대한민국 | - |
| dc.identifier.doi | 10.4014/jmb.1010.10061 | - |
| dc.identifier.scopusid | 2-s2.0-79958056966 | - |
| dc.identifier.wosid | 000291130900010 | - |
| dc.identifier.bibliographicCitation | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.21, no.5, pp 515 - 518 | - |
| dc.citation.title | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY | - |
| dc.citation.volume | 21 | - |
| dc.citation.number | 5 | - |
| dc.citation.startPage | 515 | - |
| dc.citation.endPage | 518 | - |
| dc.type.docType | Article | - |
| dc.identifier.kciid | ART001553030 | - |
| dc.description.isOpenAccess | N | - |
| dc.description.journalRegisteredClass | scie | - |
| dc.description.journalRegisteredClass | scopus | - |
| dc.description.journalRegisteredClass | kci | - |
| dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
| dc.relation.journalResearchArea | Microbiology | - |
| dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
| dc.relation.journalWebOfScienceCategory | Microbiology | - |
| dc.subject.keywordPlus | KDA FIBRINOLYTIC ENZYME | - |
| dc.subject.keywordPlus | DEFICIENT | - |
| dc.subject.keywordAuthor | Bacillus amyloliquefaciens CH86-1 | - |
| dc.subject.keywordAuthor | bacillopeptidase F | - |
| dc.subject.keywordAuthor | bpr gene | - |
| dc.subject.keywordAuthor | fibrinolytic enzymes | - |
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