Improvement of interfacial protein stability by CHAPS.
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.
Sah
Hongkee
H
College of Pharmacy, Ewha Womans University, 11-1 Daehyun-Dong, Seodaemun-Gu, Seoul 125-720, Korea. hsah@ewha.ac.kr
Kim
Kil-Soo
KS
D002793:Cholic Acids / Q000737:chemistry* / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D045703:Emulsifying Agents / Q000737:chemistry; D007782:Lactoglobulins / Q000737:chemistry; D008751:Methylene Blue / Q000737:chemistry; D010047:Ovalbumin / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012995:Solubility / Q000187:drug effects; D013501:Surface-Active Agents / Q000737:chemistry*; D013656:Taurocholic Acid / Q000737:chemistry / Q000494:pharmacology
D002793:Cholic Acids; D045703:Emulsifying Agents; D007782:Lactoglobulins; D011506:Proteins; D013501:Surface-Active Agents; D013656:Taurocholic Acid; D010047:Ovalbumin; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate; D008751:Methylene Blue