Developing an objective function to characterize the tradeoffs in salting out and the foam and droplet fractionation processes
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 objectiv...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Brazilian Society of Chemical Engineering
2000-06-01
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| Series: | Brazilian Journal of Chemical Engineering |
| Subjects: | |
| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322000000200011 |
| Summary: | 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. |
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| ISSN: | 0104-6632 1678-4383 |