Abstract

A previously reported method for the preparation of organic solvent soluble lipase in high yield has been applied to the partitioning of a protein mixture using a mixture of six known proteins as a model system. The organic solvent soluble complex of these proteins was obtained according to the previously reported method. In order to extract the proteins from the complex, the latter was dissolved in dichloromethane followed by the addition of buffer and triethylamine. By using this procedure, the proteins could be recovered from the complex formed with the detergent. It was found that the composition of the solvent used to prepare the complex influenced the ability of each protein to form a complex with the detergent. By making use of the differences in the efficiency of each protein to form a complex, several crude lipases could be successfully purified; in addition, their activities were retained during the purification procedure. The results suggest that the application of a synthetic detergent may be effective for the purification of proteins and enzymes.

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