Purification and characterization of a new peptidase, bacillopeptidase DJ-2, having fibrinolytic activity: produced by Bacillus sp. DJ-2 from Doen-Jang

Cited 0 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorNack Shick Choi-
dc.contributor.authorKi Hyun Yoo-
dc.contributor.authorJeung Ho Hahm-
dc.contributor.authorKab Seog Yoon-
dc.contributor.authorKyu Tae Chang-
dc.contributor.authorByung Hwa Hyun-
dc.contributor.authorP J Maeng-
dc.contributor.authorSeung Ho Kim-
dc.date.accessioned2017-04-19T09:02:33Z-
dc.date.available2017-04-19T09:02:33Z-
dc.date.issued2005-
dc.identifier.issn1017-7825-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6867-
dc.description.abstractA new Bacillus peptidase, bacillopeptidase DJ-2 (bpDJ-2), with molecular mass of 42 kDa and isoelectric point (pI) of 3.5-3.7, was purified to homogeneity from Bacillus sp. DJ-2 isolated from Doen-Jang, a traditional Korean soybean fermented food. The enzyme was identified as an extracellular serine fibrinolyfic protease. The optimal conditions for the reaction were pH 9.0 and 60°C. The first 18 amino acid residues of the N-terminal amino acid sequence of bpDJ-2 were TDGVEWNVDQIDAPKAW, which is identical to that of bacillopeptidase F (bpf). However, based on their N-terminal amino acid sequence, molecular size, and pI, it is different from that of bpf and extracellular 90 kDa. The whole (2,541 bp, full-bpDJ-2) and mature (1,956 bp, mature-bpDJ-2) genes were cloned, and its nucleotide sequence and deduced amino acid sequence were determined. The expressed proteins, full-bpDJ-2 and mature-bpDJ-2, were detected on SDSPAGE at expected sizes of 92 and 68 kDa, respectively.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titlePurification and characterization of a new peptidase, bacillopeptidase DJ-2, having fibrinolytic activity: produced by Bacillus sp. DJ-2 from Doen-Jang-
dc.title.alternativePurification and characterization of a new peptidase, bacillopeptidase DJ-2, having fibrionlytic activity: produced by Bacillus sp. DJ-2 from Doen-Jang-
dc.typeArticle-
dc.citation.titleJournal of Microbiology and Biotechnology-
dc.citation.number1-
dc.citation.endPage79-
dc.citation.startPage72-
dc.citation.volume15-
dc.contributor.affiliatedAuthorNack Shick Choi-
dc.contributor.affiliatedAuthorKi Hyun Yoo-
dc.contributor.affiliatedAuthorJeung Ho Hahm-
dc.contributor.affiliatedAuthorKab Seog Yoon-
dc.contributor.affiliatedAuthorKyu Tae Chang-
dc.contributor.affiliatedAuthorByung Hwa Hyun-
dc.contributor.affiliatedAuthorSeung Ho Kim-
dc.contributor.alternativeName최낙식-
dc.contributor.alternativeName유기현-
dc.contributor.alternativeName함정호-
dc.contributor.alternativeName윤갑석-
dc.contributor.alternativeName장규태-
dc.contributor.alternativeName현병화-
dc.contributor.alternativeName맹필재-
dc.contributor.alternativeName김승호-
dc.identifier.bibliographicCitationJournal of Microbiology and Biotechnology, vol. 15, no. 1, pp. 72-79-
dc.subject.keywordbacillopeptidase-
dc.subject.keywordbacillus sp. DJ-2-
dc.subject.keywordDoen-Jang-
dc.subject.keywordfibrinolytic enzyme-
dc.subject.keywordserine protease-
dc.subject.keywordzymography-
dc.subject.localbacillopeptidase-
dc.subject.localbacillus sp. DJ-2-
dc.subject.localdoenjang-
dc.subject.localDoenjang-
dc.subject.localdoen-jang-
dc.subject.localDoen-Jang-
dc.subject.localFibrinolytic enzyme-
dc.subject.localFibrinolytic enzymes-
dc.subject.localfibrinolytic enzyme-
dc.subject.localSerine protease-
dc.subject.localserine protease-
dc.subject.localZymography-
dc.subject.localzymography-
dc.description.journalClassY-
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.