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Cooperative Effect of Artificial Chaperones and Guanidinium Chloride on Lysozyme Renaturation at High Concentrations
Author(s) -
Dong XiaoYan,
Shi JinHui,
Sun Yan
Publication year - 2002
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/bp0200191
Subject(s) - guanidinium chloride , lysozyme , chemistry , chaperone (clinical) , bromide , reaction rate constant , chloride , biophysics , chromatography , enzyme , biochemistry , kinetics , inorganic chemistry , organic chemistry , biology , medicine , physics , pathology , quantum mechanics
It has been recognized that the artificial chaperone system, cetyltrimethylammonium bromide and β‐cyclodextrin, is effective for enhancing protein renaturation. In this work, we studied the effect of the artificial chaperone system and guanidinium chloride (GdmCl) on the oxidative renaturation of lysozyme at 0.21–1.05 mg/mL, and a kinetic model based on the competition between protein folding and aggregation was employed to express the renaturation process. The refolding rate constant increased, while the aggregation rate constant decreased, with increasing concentration of the artificial chaperones. With increasing GdmCl concentration (0.28–2 M), both rate constants decreased, but there existed a specific GdmCl concentration that maximized the ratio of the two rate constants and thus the renaturation yield. The results obviously indicated the cooperative effect of GdmCl and the artificial chaperones on enhancing protein renaturation.