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누에체액을 이용한 E.coli 재조합 단백질(β-galactosidase) 생산성 증대
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- Authors
- Advisor
- 박태현
- Issue Date
- 2003
- Publisher
- 서울대학교 대학원
- Description
- 학위논문(석사)--서울대학교 대학원 :응용화학부,2003.
- Abstract
- Silkworm hemolymph increased recombinant β-galactosidase in BmN-
4/Bombyx mori nuclearpolyhedrosis virus (BmNPV) system and
Spodoptera frugiperda /Autographa califomica nuclear polyhedrosis virus
(AcNPV) system. E. coli is a popular host for the high-level production
of recombinant proteins. So, the effect of silkworm hemolymph on
recombinant protein expression in E. coli was investigated. For the reason
that β-galactosidase is easy to assay, lacZ gene was inserted in
expression vector, pET22b(+) and then transformed to the host cell,
BL21(DE3). E. coli BL32(DE3)pET22b(+)/lacZ was cultured at various
concentrations of silkworm hemolymph (0%, 1%, 3%, 5%). The expression
efficiency of lacZ was determined by extracellular and intracellular β-
galactosidase activity. Addition of 5% silkworm hemolymph to the culture
medium increased the production of recombinant β-galactosidase by
eight-fold. To identify the effective component, the silkworm hemolymph
was fractionated by gel-filtration chromatography, five fractions were
obtained. Among these fraction, FI and FII which are the major fraction
of silkworm hemolymph were used, and the fraction FII showed a similar
effect to the whole hemolymph.
- Language
- Korean
- URI
- http://dcollection.snu.ac.kr:80/jsp/common/DcLoOrgPer.jsp?sItemId=000000057963
https://hdl.handle.net/10371/68949
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