博碩士論文 88224008 完整後設資料紀錄

DC 欄位 語言
DC.contributor生命科學系zh_TW
DC.creator林奕成zh_TW
DC.creatorYi-Chen Linen_US
dc.date.accessioned2001-7-20T07:39:07Z
dc.date.available2001-7-20T07:39:07Z
dc.date.issued2001
dc.identifier.urihttp://ir.lib.ncu.edu.tw:88/thesis/view_etd.asp?URN= 88224008
dc.contributor.department生命科學系zh_TW
DC.description國立中央大學zh_TW
DC.descriptionNational Central Universityen_US
dc.description.abstractLinear alkylbenzene sulfonates (LAS) are the most widely used anionic surfactants today. These compounds accumulate in the environment and show toxic effects on organisms in polluted water. This strain utilized sodium dodecylbenzene sulfonate (DBS) as sole source of sulfur in a minimal salts medium containing 0.3 % succinate. The bacterium can’t be identified by BioLog method in Gram-negative database. Further identification by 16S rDNA sequence was performed and showed 98 % identity to many Enterobacter species. Phylogenetic tree was constructed from an alignment of 1,193 nucleotides of 16S rDNA sequences showing the highest phylogenic relationship with Enterobacter agglomerans. And the bacterium was designated Enterobacter sp. SH3. The growth of strain was demonstrated as a function in the decreasing of DBS, which was analyzed by liquid chromatography-mass spectroscopy (LC-MS). It’s specific that Enterobacter. sp. SH3 can utilize several alkanesulfonates and aromatic sulfonates as sole sulfur source to grow. The action of the release of sulfite from DBS was measured using Ellman’s reagent followed by the absorbance increased at 430 nm as an enzyme assay. The highest enzyme activity was observed in the addition of 500 mM NADPH and 3 mM FMN in 0.3 ml 10 mM Tris-HCl, pH 9.0. The preliminary biochemical feature of the enzyme acting in Enterobacter sp. SH3 was showed to be similar to an FMNH2-dependent alkanesulfonate monooxygenase from Escherichia coli EC1250. A series of column chromatography was applied to purify the desulfonation enzyme. The active fraction from chromatofocusing chromatography was at pI of 5.18-4.12. The native molecular weight was at the range of 60-150 kDa by Sephacryl S-200 gel filtration chromatography. This highly purified desulfonation enzyme pool (240 mg) was further separated by 2D-gel electrophoresis and identified by MALDI-TOFen_US
DC.subject界面活性劑zh_TW
DC.subject生物分解zh_TW
DC.subject菌種鑑定zh_TW
DC.subject脫磺酸zh_TW
DC.subjectsurfactanten_US
DC.subjectbiodegradationen_US
DC.subjectbacterium identificaen_US
DC.title 陰離子界面活性劑sodium dodecylbenzene sulfonate分解菌篩選與脫磺酸酵素研究zh_TW
dc.language.isozh-TWzh-TW
DC.title Isolation of a bacterium degrading sodium dodecylbenzene sulfonate and characterization of desulfonation enzymeen_US
DC.type博碩士論文zh_TW
DC.typethesisen_US
DC.publisherNational Central Universityen_US

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