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Selective affinity separation of yeast alcohol dehydrogenase by reverse micelles with unbound triazine dye
Alternative TitleChin. J. Chem. Eng.
Zhang, TX; Liu, HZ; Chen, JY
2001-08-01
Source PublicationCHINESE JOURNAL OF CHEMICAL ENGINEERING
ISSN1004-9541
Volume9Issue:3Pages:314-318
AbstractThe 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.; 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.
KeywordReversed Micelles Yeast Alcohol Dehydrogenase Protein Purification Affinity Technology Cetyltrimethylammonium Bromide
SubtypeArticle
WOS HeadingsScience & Technology ; Technology
URL查看原文
Indexed BySCI
Language英语
WOS KeywordPROTEIN EXTRACTION ; PHOSPHORIC-ACID ; PURIFICATION ; ENZYMES
WOS Research AreaEngineering
WOS SubjectEngineering, Chemical
WOS IDWOS:000170765800016
Citation statistics
Cited Times:4[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/5785
Collection研究所(批量导入)
AffiliationChinese Acad Sci, Inst Chem Met, Lab Separat Sci & Engn, Beijing 100080, Peoples R China
Recommended Citation
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.
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