RECOMBINANT PROTEIN PRODUCTION IN Escherichia coli BY COMBINING OF SIGNAL PEPTIDE ORIGINATED FROM Bacillus subtilis

DC Field Value Language
dc.contributor.author 오철홍 -
dc.contributor.author 이영득 -
dc.contributor.author 이수진 -
dc.contributor.author 조은영 -
dc.contributor.author Hettiarachchi Sachithra Amarin -
dc.contributor.author 강도형 -
dc.date.accessioned 2020-07-15T14:52:02Z -
dc.date.available 2020-07-15T14:52:02Z -
dc.date.created 2020-02-11 -
dc.date.issued 2017-09-26 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/23815 -
dc.description.abstract We isolated chitosanase secreting B. subtilis CH2 and identified the chitosanase nucleotide 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 acids deletion compared to other B. subtilis chitosanase 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 xylanase and human superoxide distimutase 1 (hSOD1) sequences, and expressed it in E. coli BL21(DE3). The recombinant xylanase and hSOD1 moved to periplasmic space with high efficiency. This signal sequence is useful for bio-medical protein production in E. coli. the cell-membrane of the B. subtilis CH2 and then secret the chitosanase out of the cell. The signal peptide showed 6 amino acids deletion compared to other B. subtilis chitosanase 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 xylanase and human superoxide distimutase 1 (hSOD1) sequences, and expressed it in E. coli BL21(DE3). The recombinant xylanase and hSOD1 moved to periplasmic space with high efficiency. This signal sequence is useful for bio-medical protein production in E. coli. -
dc.description.uri 1 -
dc.language English -
dc.publisher Engineering Conferences International -
dc.relation.isPartOf Enzyme Engineering XXIX -
dc.title RECOMBINANT PROTEIN PRODUCTION IN Escherichia coli BY COMBINING OF SIGNAL PEPTIDE ORIGINATED FROM Bacillus subtilis -
dc.type Conference -
dc.citation.endPage 96 -
dc.citation.startPage 96 -
dc.citation.title Enzyme Engineering XXIX -
dc.contributor.alternativeName 오철홍 -
dc.contributor.alternativeName 이영득 -
dc.contributor.alternativeName 이수진 -
dc.contributor.alternativeName 조은영 -
dc.contributor.alternativeName Amarin -
dc.contributor.alternativeName 강도형 -
dc.identifier.bibliographicCitation Enzyme Engineering XXIX, pp.96 -
dc.description.journalClass 1 -
Appears in Collections:
Jeju Research Institute > Jeju Marine Research Center > 2. Conference Papers
Jeju Research Institute > Jeju Bio Research Center > 2. Conference Papers
Jeju Research Institute > Tropical & Subtropical Research Center > 2. Conference Papers
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