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Purification of proteins using foam fractionation
C E Lockwood1, P M Bummer, M Jay
1Department of Medicinal Chemistry and Pharmaceutics, University of Kentucky College of Pharmacy, Lexington 40536-0082, USA.
Pharmaceutical Research
|January 22, 1998
Summary
Foam fractionation offers a potentially cost-effective method for purifying recombinant proteins in pharmaceutical production. This review explores recent advancements in foam fractionation for protein systems, focusing on pharmaceutical applications.
Area of Science:
- Biochemical Engineering
- Separation Science
- Pharmaceutical Manufacturing
Background:
- Recombinant protein purification is critical for pharmaceutical production.
- Conventional chromatography methods significantly impact manufacturing costs.
- Novel separation techniques are needed to reduce production expenses.
Purpose of the Study:
- To review recent studies on foam fractionation for protein purification.
- To assess foam fractionation's potential as a cost-effective purification method.
- To highlight foam fractionation applications relevant to pharmaceutical product requirements.
Main Methods:
- Review of recent scientific literature on foam fractionation.
- Analysis of foam fractionation principles and mechanisms.
- Evaluation of foam fractionation's applicability to protein systems.
Main Results:
- Foam fractionation utilizes differences in component affinities for the gas/aqueous interface.
- Recent studies demonstrate its potential for protein separation.
- The technique shows promise for cost-effective pharmaceutical purification.
Conclusions:
- Foam fractionation is a promising alternative to conventional purification methods.
- Further research can optimize foam fractionation for industrial-scale pharmaceutical production.
- This technique can contribute to reducing the overall cost of recombinant protein-based drugs.