Open AccessDeveloping an objective function to characterize the tradeoffs in salting out and the foam and droplet fractionation processes
Author(s) -
Justin Cherry,
SooByung Ko,
Reid J. Grainger,
Andreas Prokop,
Robert D. Tanner
Publication year - 2000
Publication title -
brazilian journal of chemical engineering/brazilian journal of chemical engineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.313
H-Index - 52
eISSN - 1678-4383
pISSN - 0104-6632
DOI - 10.1590/s0104-66322000000200011
Subject(s) - fractionation , foam fractionation , chromatography , isoelectric point , chemistry , cellulase , adsorption , salting out , precipitation , separation process , enzyme , biochemistry , aqueous solution , organic chemistry , pulmonary surfactant , physics , meteorology
There are many methods for separating and purifying proteins from dilute solutions, such as salting out/precipitation, adsorption/chromatography, foam fractionation, and droplet fractionation. In order to determine the optimal condition for a selected separation and purification process, an objective function is developed. The objective function consists of three parameters, which are the protein mass recovery, the separation ratio, and the enzymatic activity ratio. In this paper the objective function is determined as a function of the pH of the bulk solution for egg albumin, cellulase, and sporamin (for foam fractionation) and invertase ( for droplet fractionation). It is found that the optimal pH for all the systems except for cellulase is near their isoelectric point