文摘
The feasibility of controlling the selective precipitation of pancreatic proteins was investigated using designedorganic antisolvents in a drowning-out process. First, the solubility of pancreatin was measured in water-organic solutions when the organic species and their composition in the solution were varied. Due to thehydrophilicity of the proteins, solubility was rapidly reduced when the organic species fraction in the solutionwas increased. This reduced solubility was further amplified with a less polar organic species. Plus, thepancreatin solubility as a predictor was found to agree well with the solution polarity as a single parameter,expressed in terms of the Hildebrand solubility parameter. The precipitation of pancreatin was then carriedout with various antisolvents composed of alcoholic and nonalcoholic species. The precipitation was promotedalong with an antisolvent of a lower polarity, which was also functionally related to the solution polarity. Theamylase, lipase, and protease proteins contained in the pancreatin displayed different precipitation behaviorsdepending on the polarity of the antisolvent. Thus, it was possible to selectively separate the proteins andcontrol their composition in the precipitated pancreatin.