Enzymatic resolution of racemic phenyloxirane by a novel epoxide hydrolase from aspergillus niger sq-6 and its fed-batch fermentation
文献类型：期刊论文
| 作者 | Liu, YB; Sha, Q; Wu, S; Wang, JJ; Yang, L; Sun, WR |
| 刊名 | Journal of industrial microbiology & biotechnology
 |
| 出版日期 | 2006-04-01 |
| 卷号 | 33期号:4页码:274-282 |
| 关键词 | Aspergillus niger Epoxide hydrolase Epoxide racemase Capillary electrophoresis Stereoselectivity |
| ISSN号 | 1367-5435 |
| DOI | 10.1007/s10295-005-0062-3 |
| 通讯作者 | Sun, wr() |
| 英文摘要 | A microorganism with the ability to catalyze the resolution of racemic phenyloxirane was isolated and identified as aspergillius niger sq-6. chiral capillary electrophoresis was successfully applied to separate both phenyloxirane and phenylethanediol. the epoxide hydrolase (eh) involved in this resolution process was (r)-stereospecific and constitutively expressed. when whole cells were used during the biotransformation process, the optimum temperature and ph for stereospecific vicinal diol production were 35 degrees c and 7.0, respectively. after a 24-h conversion, the enantiomer excess of (r)phenylethanediol produced was found to be > 99%, with a conversion rate of 56%. in fed-batch fermentations at 30 degrees c for 44 h, glycerol (20 g l-1) and corn steep liquor (csl) (30 g l-1) were chosen as the best initial carbon and nitrogen sources, and eh production was markedly improved by pulsed feeding of sucrose (2 g l-1 h(-1)) and continuous feeding of csl (1 g l-1 h(-1)) at a fermentation time of 28 h. after optimization, the maximum dry cell weight achieved was 24.5 +/- 0.8 g l-1; maximum eh production was 351.2 +/- 13.1 u l-1 with a specific activity of 14.3 +/- 0.5 u g(-1). partially purified eh exhibited a temperature optimum at 37 degrees c and ph optimum at 7.5 in 0.1 m phosphate buffer. this study presents the first evidence for the existence of a predicted epoxide racemase, which might be important in the synthesis of epoxide intermediates. |
| WOS关键词 | ENANTIOSELECTIVE HYDROLYSIS ; MICROBIOLOGICAL TRANSFORMATIONS ; RECOMBINANT ENZYME ; NITROSTYRENE OXIDE ; KINETIC RESOLUTION ; LIMITING-CARBON ; PULSED ADDITION ; ORYZAE ; LEADS ; PRODUCTIVITY |
| WOS研究方向 | Biotechnology & Applied Microbiology |
| WOS类目 | Biotechnology & Applied Microbiology |
| 语种 | 英语 |
| WOS记录号 | WOS:000236954800004 |
| 出版者 | SPRINGER HEIDELBERG |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2378952 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Sun, WR |
| 作者单位 | 1.Chinese Acad Sci, Inst Microbiol, State Key Lab Microbial Resources, Beijing 100080, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing, Peoples R China |
| 推荐引用方式 GB/T 7714 | Liu, YB,Sha, Q,Wu, S,et al. Enzymatic resolution of racemic phenyloxirane by a novel epoxide hydrolase from aspergillus niger sq-6 and its fed-batch fermentation[J]. Journal of industrial microbiology & biotechnology,2006,33(4):274-282. |
| APA | Liu, YB,Sha, Q,Wu, S,Wang, JJ,Yang, L,&Sun, WR.(2006).Enzymatic resolution of racemic phenyloxirane by a novel epoxide hydrolase from aspergillus niger sq-6 and its fed-batch fermentation.Journal of industrial microbiology & biotechnology,33(4),274-282. |
| MLA | Liu, YB,et al."Enzymatic resolution of racemic phenyloxirane by a novel epoxide hydrolase from aspergillus niger sq-6 and its fed-batch fermentation".Journal of industrial microbiology & biotechnology 33.4(2006):274-282. |
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来源：中国科学院大学
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