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The kinetics of protein salting‐Out: Precipitation of yeast enzymes by ammonium sulfate

Protein solubility can be adequately represented by the classical Cohn equation for the salting‐out of alcohol dehydrogenase and fumarase from clarified yeast homogenate with ammonium sulfate. However, the constant β in this equation is a function of the contacting procedure employed. The kinetics of continuous salting‐out were similar for alcohol dehydrogenase and fumarase. The overall rate equation for precipitation had a variable order which was high initially, up to 3.1, but approached unity on completion of precipitation. This was followed by a partial resolution stage which was first order with respect to the concentration driving force. Precipitate particle size was estimated as 0.5 to 5 μm with continuous flow precipitation producing the largest particles.