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Protein refolding in predominantly organic media markedly enhanced by common salts
Author(s) -
Rariy Roman V.,
Klibanov Alexander M.
Publication year - 1999
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19990320)62:6<704::aid-bit9>3.0.co;2-s
Subject(s) - chemistry , biochemistry
The refolding/reoxidation of unfolded/reduced hen egg‐white lysozyme was investigated in a variety of predominantly nonaqueous media consisting of protein‐dissolving 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. © 1999 John Wiley & Sons, Inc. Biotechnol Bioeng 62: 704–710, 1999.