High temperature increases the refolding yield of reduced lysozyme: implication for the productive process for folding.
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.
Sakamoto
Ryusuke
R
School of Materials Science, Japan Advanced Institute of Science and Technology (JAIST), 1-1 Asahidai, Tatsunokuchi, Ishikawa 923-1292, Japan.
Nishikori
Shingo
S
Shiraki
Kentaro
K
D006358:Hot Temperature; D009113:Muramidase / Q000378:metabolism*; D017510:Protein Folding
D009113:Muramidase