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High Temperature Increases the Refolding Yield of Reduced Lysozyme: Implication for the Productive Process for Folding
Author(s) -
Sakamoto Ryusuke,
Nishikori Shingo,
Shiraki Kentaro
Publication year - 2004
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp034385b
Subject(s) - protein folding , lysozyme , chemistry , yield (engineering) , folding (dsp implementation) , dilution , unfolded protein response , crystallography , biophysics , biochemistry , thermodynamics , biology , endoplasmic reticulum , physics , electrical engineering , engineering
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 °C were three times higher than those at 20 °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.