Effect of Culture Conditions and Signal Peptide on Production of Human Recombinant N-Acetylgalactosamine-6-Sulfate Sulfatase in Escherichia coli BL21
분야
자연과학 > 생물
저자
( Hernandez Alejandra ) , ( Olga Velasquez ) , ( Felice Leonardi ) , ( Carlos Soto ) , ( Alexander Rodriguez ) , ( Lina Lizaraso ) , ( Angela Mosquera ) , ( Jorge Bohorquez ) , ( Alejandra Coronado ) , ( Angela Espejo ) , ( Rocio Sierra ) , ( Oscar F Sanc
발행기관
한국미생물생명공학회(구 한국산업미생물학회)
간행물정보
Journal of Microbiology and Biotechnology 2013년, 제23권 제5호, 689~698페이지(총10페이지)
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05212272.pdf [무료 PDF 뷰어 다운로드]
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    영문초록
    The production and characterization of an active recombinant N-acetylgalactosamine-6-sulfate sulfatase (GALNS) in Escherichia coli BL21(DE3) has been previously reported. In this study, the effect of the signal peptide (SP), inducer concentration, process scale, and operational mode (batch and semi-continuous) on GALNS production were evaluated. When native SP was presented, higher enzyme activity levels were observed in both soluble and inclusion bodies fractions, and its removal had a significant impact on enzyme activation. At shake scale, the optimal IPTG concentrations were 0.5 and 1.5 mM for the strains with and without SP, respectively, whereas at bench scale, the highest enzyme activities were observed with 1.5 mM IPTG for both strains. Noteworthy, enzyme activity in the culture media was only detected when SP was presented and the culture was carried out under semi-continuous mode. We showed for the first time that the mechanism that in prokaryotes recognizes the SP to mediate sulfatase activation can also recognize a eukaryotic SP, favoring the activation of the enzyme, and could also favor the secretion of the recombinant protein. These results offer significant information for scaling-up the production of human sulfatases in E. coli.
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