Enzymatic Activity Can be Recovered from Solvent-Denatured Catalase

Abstract

The correlation of solvent precipitation data with conformational changes is reviewed briefly. For catalase, additional information about the conformation can be gained from shifts in the Soret spectrum upon treating with dithionite. Here we report observations for crude catalase and compare these with previous work using crystalline catalase; some reinterpretation of earlier conclusions is warranted. Furthermore, this knowledge of the conformational state allows design of processes so as to optimize the yield during purification. For example, catalase which had been denatured during an alcohol precipitation may be partially renatured by redissolving in water and then precipitating with ammonium sulfate.