KINETICS OF LYSOZYME REFOLDING FACILITATED BY MOLECULAR CHAPERONE GroEL
An apparent kinetic model for lysozyme refolding was established,and the refolding behavior of denatured lysozyme facilitated by the molecular chaperone GroEL was studied.The effects of denatured lysozyme concentration, adenosine triphosphate (ATP) concentration, and the molar ratio of GroEL to lysozyme on the refolding yield and the refolding rate constant were investigated.The lysozyme concentration showed more significant effect on the refolding rate constant than on the refolding yield.Both refolding yield and refolding rate constant increased with increasing ATP concentration.At a definite protein concentration, optimal concentrations of both GroEL and ATP existed to give maximum refolding yield and refolding rate constant.