Chitosanase signal peptide from Bacillus subtilis its lead target protein to periplasmic space in Escherichia coli

DC Field Value Language
dc.contributor.author 오철홍 -
dc.contributor.author 문송 -
dc.contributor.author 조은영 -
dc.contributor.author 이수진 -
dc.contributor.author 이영득 -
dc.contributor.author 박건후 -
dc.contributor.author 권영경 -
dc.contributor.author Hettiarachchi Sachithra Amarin -
dc.contributor.author 강도형 -
dc.date.accessioned 2020-07-15T19:32:45Z -
dc.date.available 2020-07-15T19:32:45Z -
dc.date.created 2020-02-11 -
dc.date.issued 2016-11-10 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/24345 -
dc.description.abstract We isolated chitosanase secreting B. subtilis CH2 and identified the chitosanase sequence. Analyzed the sequence showed that it consisted of 813 bp, including 87 bp signal sequence. The signal sequence leads the target protein to the cell-membrane of the B. subtilis CH2 and then secret the chitosanase out of the cell. The signal peptide showed 6 amino acid deletion compared to other B. subtilis chitosnase signal peptides. The chitosanase sequence including signal peptide was cloned into pET11a vector without fusion and expressed in E. coli BL21(DE3). The expressed chitosanase in E. coli showed two distinct bands which represent the pro-chitosanase in cytoplasm and mature chitosanase in periplasm. Time frame induction and results showed that muture chitosanase was increased. Subsequently, we linked this chitosanase signal sequence in front of B. subtilis CH2 mature lichenase and xylanase sequences, and expressed it in E. coli BL21(DE3). The recombinant xylanase moved to periplasmic space. However, the recombinant lichenase did not move to periplasm.embrane of the B. subtilis CH2 and then secret the chitosanase out of the cell. The signal peptide showed 6 amino acid deletion compared to other B. subtilis chitosnase signal peptides. The chitosanase sequence including signal peptide was cloned into pET11a vector without fusion and expressed in E. coli BL21(DE3). The expressed chitosanase in E. coli showed two distinct bands which represent the pro-chitosanase in cytoplasm and mature chitosanase in periplasm. Time frame induction and results showed that muture chitosanase was increased. Subsequently, we linked this chitosanase signal sequence in front of B. subtilis CH2 mature lichenase and xylanase sequences, and expressed it in E. coli BL21(DE3). The recombinant xylanase moved to periplasmic space. However, the recombinant lichenase did not move to periplasm. -
dc.description.uri 1 -
dc.language English -
dc.publisher The Genetics Society of Korea -
dc.relation.isPartOf International Conference of the Genetics Society of Korea 2016 -
dc.title Chitosanase signal peptide from Bacillus subtilis its lead target protein to periplasmic space in Escherichia coli -
dc.type Conference -
dc.citation.conferencePlace KO -
dc.citation.endPage 182 -
dc.citation.startPage 182 -
dc.citation.title International Conference of the Genetics Society of Korea 2016 -
dc.identifier.bibliographicCitation International Conference of the Genetics Society of Korea 2016, pp.182 -
dc.description.journalClass 1 -
Appears in Collections:
Jeju Research Institute > Jeju Marine Research Center > 2. Conference Papers
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