Enhanced refolding of lysozyme with imidazolium-based room temperature ionic liquids： Effect of hydrophobicity and sulfur residue

• Published in: Science China. Chemistry Vol. 55; no. 8; pp. 1657 - 1662
• Main Authors: Bae, Sang-Woo, Chang, Woo-Jin, Koo, Yoon-Mo, Ha, Sung Ho
• Format: Journal Article
• Language: English
• Published: Heidelberg SP Science China Press 01.08.2012; Springer Nature B.V
• Subjects: Buffers; Cations; Chemistry; Chemistry and Materials Science; Chemistry/Food Science; Dilution; Hydrophobicity; Ionic liquids; Lysozyme; Proteins; Residues; Room temperature; Sulfur; 咪唑类; 室温离子液体; 渣油; 溶菌酶; 疏水性; 硫酸盐; 稀释复性; 重组蛋白; protein refolding; sulfur; hydrophobicity; lysozyme; dilution refolding; room temperature ionic liquid

The expression of recombinant proteins in microorganism frequently leads to the formation of insoluble aggregates, inclusion bodies （IBs）. Thus, the additional in vitro protein refolding process is required to convert inactive IBs into water-soluble active proteins. This study investigated the effec...