Thermostabilization of enzymes by the chaperonin GroEL

Summary The influence of GroEL on the heat-inactivation of nine enzymes was analyzed. Five dehydrogenases and four other unrelated enzymes were heat-inactivated in the absence and presence of GroEL, at three different temperatures. GroEL protected most enzymes against inactivation and prevented their aggregation. Further, the formation of a highly stable complex was observed when rhodanese was thermoinactivated in the presence of GroEL.