High Temperature Increases the Refolding Yield of Reduced Lysozyme: Implication for the Productive Process for Folding
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- 作者：Ryusuke Sakamoto ; Shingo Nishikori ; and Kentaro Shiraki
- 刊名：Biotechnology Progress
- 出版年：2004
- 出版时间：August 2004
- 年：2004
- 卷：20
- 期：4
- 页码：1128 - 1133
- 全文大小：105K
- 年卷期：v.20,no.4(August 2004)
- ISSN：1520-6033
文摘
Misfolding poses a serious problem in the biotechnological field in obtaining the activeprotein from inclusion bodies. Here we show that high temperature increases therefolding yield of reduced lyosyzme by a simple dilution method. The refolding yieldsat 98 
C were three times higher than those at 20 C in the solutions tested, which isrelated to the fact that the thermally unfolded state of lysozyme is a more productiveform for folding than the denaturant-induced fully unfolded state. The thermal-assistedrefolding could be used for various reduced and denatured proteins as a result of itssimplicity and low cost.
C were three times higher than those at 20 C in the solutions tested, which isrelated to the fact that the thermally unfolded state of lysozyme is a more productiveform for folding than the denaturant-induced fully unfolded state. The thermal-assistedrefolding could be used for various reduced and denatured proteins as a result of itssimplicity and low cost.