Abstract
Emulsification of aqueous protein solutions in methylene chloride triggered the formation of water-insoluble aggregates at a water/methylene chloride interface. As a result, the amounts of β-lactoglobulin and ovalbumin recovered in water were 36 and 44%, respectively. Addition of 5 mm CHAPS in the aqueous phase raised the degree of β-lactoglobulin recovery to 96%. Sodium taurocholate, however, failed to improve protein recovery. The stabilizing effect of CHAPS was also protein-specific and concentration-dependent: at ≥5 mm, the surfactant caused unfolding of ovalbumin to make a water-soluble oligomer. CHAPS thus stabilizes proteins at an interface.
Original language | English |
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Pages (from-to) | 567-570 |
Number of pages | 4 |
Journal | Biotechnology Letters |
Volume | 28 |
Issue number | 8 |
DOIs | |
State | Published - Apr 2006 |
Bibliographical note
Funding Information:This study was in part supported by a RRC grant from the MOCIE.
Keywords
- CHAPS
- Interface
- Microspheres
- Protein stability
- Surfactants