Improvement of interfacial protein stability by CHAPS

Biotechnology Letters
Hongkee Sah, Kil-Soo Kim

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 beta-lactoglobulin and ovalbumin recovered in water were 36 and 44%, respectively. Addition of 5 mM: CHAPS in the aqueous phase raised the degree of beta-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 >or=5 mM: , the surfactant caused unfolding of ovalbumin to make a water-soluble oligomer. CHAPS thus stabilizes proteins at an interface.

References

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Dec 29, 2004·Colloids and Surfaces. B, Biointerfaces·Abdol-Khalegh BordbarReza Hosseinzadeh
Apr 20, 2005·Journal of Colloid and Interface Science·Swati DeSusmita Das

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