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MOLECULAR CLONING OF EXTRACELLULAR LEVANSUCRAE GENE OF ZYMOMNAS MOBILIS ZMIINE. COLI
宋基榜 건국대학교 1992 대학원 학술논문집 Vol.35 No.-
Leven is a fructose polymer of potential importance as fructose source or thickening agent in food industry and plasma expander in pharmaceutical industry. The extracellular levansucrase gene of Zymomonas mobilis ZM1 was cloned in E. coli by shot-gun cloning method. By the analysis of genomic librariesof Z. mobilis ZM1, 13recombinant E. coli colonies showing sucrase activity were obtained. One of these plasmids isolated from these clones was designated as pZL8 and further characterized. The plasmid pZL8 with 4.5Kb Z.mobilis ZM1 chromosomal DNA fragment inserted conferred a sucrase positive phenotype and showed transfructosylation activity(levan-like-polysaccharide formation) in minimal medium, the restriction analysis and deletion experiment revealed that levansucrase gene was included in 2.1Kb DNA fragment, polysaccharide formed in E. doli(pZL8) was identifited as leavan by TLC analysis. Electropholetic behaviour of the levansucrase produced from E. coli(pZL8) was identical to those of the extracellular levansucrase of Z. mobilis ZM1.
Bacillus subtilis의 cdd유전자의 Escherichia-Saccharomyces Shuttle Vector YRp7에의 클로닝
金榮基,宋邦鎬 경북대학교 과학교육연구소 1988 科學敎育硏究誌 Vol.12 No.-
The cdd gene enconding cytidine deaminase from Bacillus subtilis was cloned and expressed in the Saccharomyces cerevisiae D13-1A. By insertion of the 1.45 Kb of EcoRl/EcoRl fragment which containing genes fo for replication origin and trpl selective marker from Escherichia-Sac-charomyces shuttle vector YR_p7 into the EcoRl site of pS062, the Bacillus cdd gene was expressed in the yeast cells. By selection of the trp+ colonies in the SD medium. One of the transformed Saccharomyces cells were isolated as Saccharomyces cerevisiae YKl. The transformed yeast cells which carring chimeric plasmid, pYKl, was expressed the cdd activity with two folds elevated levels. For further confirming the pYKl expression in yeast cell, the pYKl which isolated from the transformed cells was recloned into the Escherichia coli KM268. The plasmid isolated from strain KM268 was identified as the same one with the original chimeric plasmid, pYKI.
SONG, KI BANG,RHEE, SANG KI 한국미생물 · 생명공학회 1992 Journal of microbiology and biotechnology Vol.2 No.2
In order to broaden the spectrum of substrate utilization of a Gram negative bacterium Zymomonas mobilis which has a great potential as an industrial ethanol producing microorganism, cloning of α-amylase gene into Z. mobilis ZM4 was tried. The α-amylase gene was isolated from Bacillus stearothermophilus. By Southern blot analysis, it was proven that the α-amylase gene fragment was originated from a naturally occuring plasmid of B. stearothermophilus ATCC31195. To place α-amylase gene under the control of Z. mobilis promoter, two different Z. mobilis expression vectors, pZA26 and pLOI204, were used. The truncated α-amylase gene was then introduced into these vectors. Both qualitative and quantitative activities of α-amylase were observed in Z. mobilis cells harboring these plasmids with the α-amylase gene inserted. Gas chromatographic analysis of ethanol showed that one of the Z. mobilis transconjugants was capable of producing 67 mM ethanol from rich medium(RM) containing 5% soluble starch as a sole carbon source.
Song, Ki Bang,Bae, Kyoung Sook,Lee, Yong Bok,Lee, Ki Young,Rhee, Sang Ki 전남대학교 약품개발연구소 2000 약품개발연구지 Vol.9 No.1
A microorganism producing levan fructotransferase was isolated from sugar-disclosed soil and it was identified as Arthrobacter ureafaciens. The major product from levee by enzyme reaction was identified as di-D-fructofuranose 2,6':6,2' dianhydride by mass spectrometry, nuclear magnetic resonance, and chemical analyses. Small amounts of several oligosaccharides and free fructose were also formed by enzyme reaction. An extracellular enzyme that produces di-D-fructofuranose 2,6':6,2' dianhydride from levan was purified from the culture broth of A. ureafaciens K2032. The enzyme had optimum activity around pH 5.8 and 45℃ and had a dimeric form in solution. The N-terminal amino acid residues of the purified enzyme were SAPGSLRAVYHMTPPSGXLXDPQ. The enzyme has narrow substrate range and converts the levee to di-D-fructofuranose 2,6':6,2' dianhydride with around 62.5% conversion yield.
Song, Ki-Bang The Korean Society for Microbiology and Biotechnol 1992 Journal of microbiology and biotechnology Vol.2 No.2
In order to broaden the spectrum of substrate utilization of a Gram negative bacterium Zymomonas mobilis which has a great potential as an industrial ethanol producing microorganism, cloning of $\alpha$-amylase gene into Z. mobilis ZM4 was tried. The $\alpha$-amylase gene was isolated from Bacillus stearothermophilus. By Southern blot analysis, it was proven that the $\alpha$-amylase gene fragment was originated from a naturally occuring plasmid of B. stearothermophilus ATCC 31195. To place $\alpha$-amylase gene under the control of Z. mobilis promoter, two different Z. mobilis expression vectors, pZA26 and pLOI204, were used. The truncated $\alpha$-amylase gene was then introduced into these vectors. Both qualitative and quantitative activities of $\alpha$-amylase were observed in Z. mobilis cells harboring these plasmids with the $\alpha$-amylase gene inserted. Gas chromatographic analysis of ethanol showed that one of the Z. mobilis transconjugants was capable of producing 67 mM ethanol from rich medium(RM) containing 5% soluble starch as a sole carbon source.