Separation of alpha-amylase by reversed micellar extraction - Effect of solvent type and cosolvent concentration on the transfer process
文献类型:期刊论文
作者 | Chang, Q. L. ; Chen, J. Y. |
刊名 | Applied Biochemistry and Biotechnology
![]() |
出版日期 | 1997 |
期号 | 2-3页码:119-129 |
关键词 | reversed micelles solvent cosolvent separation alpha-amylase liquid-liquid-extraction solubilization chymotrypsin enzymes |
其他题名 | Appl. Biochem. Biotechnol. |
中文摘要 | The recovery of alpha-amylase from the crude enzyme preparation by the reversed micellar liquid-liquid extraction was investigated. The reversed micellar solution was formed by dissolving a cationic surfactant Aliquat 336 in six different alkanes (cyclohexane, n-hexane, isooctane, n-octane, n-decane, and n-dodecane) respectively with addition of a cosolvent n-octanol. It was found that a minimal quantity of n-octanol was needed for Aliquat 336 to dissolve in apolar solvent and form reversed micelles. Furthermore, this minimal amount of n-octanol needed was found to be different when Aliquat 336 was dissolved in different alkanes. It tended to increase with the number of carbon atoms in alkane and also depended on the solvent structure. During the forward extraction process, it was revealed that a high value of solubilization of protein in Aliquat 336 reversed micelles could be achieved when four out of the six alkanes (cyclohexane, n-hexane, isooctane, n-octane) were used as the solvent for Aliquat 336. After a full forward and backward extraction cycle, however, a high recovery of both the protein mass and alpha-amylase activity in the stripping solution could be obtained only when two out of the six alkanes (n-hexane and isooctane) were used as the solvent for Aliquat 336. When n-hexane and isooctane were used as the solvent for Aliquat 336, up to 80% of the total alpha-amylase activity in the crude enzyme preparation could be recovered at the end of extraction cycle, meanwhile alpha-amylase could be concentrated about 1.4-fold. In the cases of other four alkanes (cyclohexane, n-octane, n-decane, and n-dodecane) as solvent, most of the a-amylase activity in the crude enzyme preparation would be denatured after an extraction cycle. |
收录类别 | SCI |
原文出处 | |
语种 | 英语 |
公开日期 | 2013-11-15 |
版本 | 出版稿 |
源URL | [http://ir.ipe.ac.cn/handle/122111/6061] ![]() |
专题 | 过程工程研究所_研究所(批量导入) |
推荐引用方式 GB/T 7714 | Chang, Q. L.,Chen, J. Y.. Separation of alpha-amylase by reversed micellar extraction - Effect of solvent type and cosolvent concentration on the transfer process[J]. Applied Biochemistry and Biotechnology,1997(2-3):119-129. |
APA | Chang, Q. L.,&Chen, J. Y..(1997).Separation of alpha-amylase by reversed micellar extraction - Effect of solvent type and cosolvent concentration on the transfer process.Applied Biochemistry and Biotechnology(2-3),119-129. |
MLA | Chang, Q. L.,et al."Separation of alpha-amylase by reversed micellar extraction - Effect of solvent type and cosolvent concentration on the transfer process".Applied Biochemistry and Biotechnology .2-3(1997):119-129. |
入库方式: OAI收割
来源:过程工程研究所
浏览0
下载0
收藏0
其他版本
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。