Protein refolding in predominantly organic media markedly enhanced by common salts

✍ Scribed by Roman V. Rariy; Alexander M. Klibanov

• Book ID: 101241948
• Publisher: John Wiley and Sons
• Year: 1999
• Tongue: English
• Weight: 112 KB
• Volume: 62
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/(sici)1097-0290(19990320)62:6<704::aid-bit9>3.0.co;2-s

✦ Synopsis

The refolding/reoxidation of unfolded/reduced hen egg-white lysozyme was investigated in a variety of predominantly nonaqueous media consisting of proteindissolving organic solvents and water. It was discovered that LiCl and other common salts dramatically (up to more than 100-fold) increased the refolding yield of lysozyme in such nonaqueous systems, while reducing it in water. The mechanism of this surprising phenomenon appears to involve salt-induced suppression of nonspecific lysozyme aggregation during refolding due to an enhanced protein solubility.