High temperature increases the refolding yield of reduced lysozyme: implication for the productive process for folding
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Updated: Aug 23, 2026

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
Published on: July 9, 2013
Ryusuke Sakamoto1, Shingo Nishikori, Kentaro Shiraki
1School of Materials Science, Japan Advanced Institute of Science and Technology (JAIST), 1-1 Asahidai, Tatsunokuchi, Ishikawa 923-1292, Japan.
Abstract:
Misfolding poses a serious problem in the biotechnological field in obtaining the active protein from inclusion bodies. Here we show that high temperature increases the refolding yield of reduced lyosyzme by a simple dilution method. The refolding yields at 98 degrees C were three times higher than those at 20 degrees C in the solutions tested, which is related to the fact that the thermally unfolded state of lysozyme is a more productive form for folding than the denaturant-induced fully unfolded state. The thermal-assisted refolding could be used for various reduced and denatured proteins as a result of its simplicity and low cost.
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