Selective affinity separation of yeast alcohol dehydrogenase by reverse micelles with unbound triazine dye
文献类型：期刊论文
| 作者 | Zhang, TX; Liu, HZ; Chen, JY |
| 刊名 | CHINESE JOURNAL OF CHEMICAL ENGINEERING
 |
| 出版日期 | 2001-08-01 |
| 卷号 | 9期号:3页码:314-318 |
| 关键词 | reversed micelles yeast alcohol dehydrogenase protein purification affinity technology cetyltrimethylammonium bromide |
| ISSN号 | 1004-9541 |
| 其他题名 | Chin. J. Chem. Eng. |
| 中文摘要 | The reversed micelles were formed with cationic cetyltrimethylammonium bromide (CTAB) as surfactant and n-hexanol as cosolvent in the CTAB (50 mmol.L-1)/hexanol (15% by volume)/hexane system. Cibacron Blue 3GA (CB) as an affinity ligand in the aqueous phase was directly introduced to the reversed micelles with electrostatic interaction between anionic CB and cationic surfactant. High molecular weight (M-r) protein, yeast alcohol dehydrogenase (YADH, M-r = 141000) from baker's yeast, has been purified using the affinity reversed micelles by the phase transfer method. Various parameters, such as CB concentration, pH and ionic strength, on YADH forward and backward transfer were studied. YADH can be transferred into and out from the reversed micelles under mild conditions (only by regulation of solution pH and salt concentration) with the successful recovery of most YADH activity. Both forward and backward extractions occurred when the aqueous phase pH>pI with electrostatic attraction between YADH and CTAB. The recovery of YADH activity and purification factor have been improved with addition of a small amount of affinity CB. The recovery of YADH activity obtained was similar to 99% and the purification factor was about 4.0-fold after one cycle of full forward and backward extraction. The low ionic strength in the initial aqueous phase might be responsible for the YADH transfer into the reversed micellar phase. Keywords reversed micelles, yeast alcohol dehydrogenase, protein purification,affinity technology, cetyltrimethylammonium bromide. |
| 英文摘要 | The reversed micelles were formed with cationic cetyltrimethylammonium bromide (CTAB) as surfactant and n-hexanol as cosolvent in the CTAB (50 mmol.L-1)/hexanol (15% by volume)/hexane system. Cibacron Blue 3GA (CB) as an affinity ligand in the aqueous phase was directly introduced to the reversed micelles with electrostatic interaction between anionic CB and cationic surfactant. High molecular weight (M-r) protein, yeast alcohol dehydrogenase (YADH, M-r = 141000) from baker's yeast, has been purified using the affinity reversed micelles by the phase transfer method. Various parameters, such as CB concentration, pH and ionic strength, on YADH forward and backward transfer were studied. YADH can be transferred into and out from the reversed micelles under mild conditions (only by regulation of solution pH and salt concentration) with the successful recovery of most YADH activity. Both forward and backward extractions occurred when the aqueous phase pH>pI with electrostatic attraction between YADH and CTAB. The recovery of YADH activity and purification factor have been improved with addition of a small amount of affinity CB. The recovery of YADH activity obtained was similar to 99% and the purification factor was about 4.0-fold after one cycle of full forward and backward extraction. The low ionic strength in the initial aqueous phase might be responsible for the YADH transfer into the reversed micellar phase. Keywords reversed micelles, yeast alcohol dehydrogenase, protein purification,affinity technology, cetyltrimethylammonium bromide. |
| WOS标题词 | Science & Technology ; Technology |
| 类目[WOS] | Engineering, Chemical |
| 研究领域[WOS] | Engineering |
| 关键词[WOS] | PROTEIN EXTRACTION ; PHOSPHORIC-ACID ; PURIFICATION ; ENZYMES |
| 收录类别 | SCI |
| 原文出处 | |
| 语种 | 英语 |
| WOS记录号 | WOS:000170765800016 |
| 公开日期 | 2013-11-14 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/5785]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | Chinese Acad Sci, Inst Chem Met, Lab Separat Sci & Engn, Beijing 100080, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhang, TX,Liu, HZ,Chen, JY. Selective affinity separation of yeast alcohol dehydrogenase by reverse micelles with unbound triazine dye[J]. CHINESE JOURNAL OF CHEMICAL ENGINEERING,2001,9(3):314-318. |
| APA | Zhang, TX,Liu, HZ,&Chen, JY.(2001).Selective affinity separation of yeast alcohol dehydrogenase by reverse micelles with unbound triazine dye.CHINESE JOURNAL OF CHEMICAL ENGINEERING,9(3),314-318. |
| MLA | Zhang, TX,et al."Selective affinity separation of yeast alcohol dehydrogenase by reverse micelles with unbound triazine dye".CHINESE JOURNAL OF CHEMICAL ENGINEERING 9.3(2001):314-318. |
入库方式： OAI收割
来源：过程工程研究所
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