Separation of amphipathic proteins based on adsorption to hexadecane:water interfaces.
A method is proposed for the relatively simple and rapid separation of amphipathic biopolymers, based on adsorption onto and desorption from the surface of hexadecane droplets. Adsorption to the hexadecane:water interface was carried out by mixing hexadecane with aqueous protein solutions at room temperature. Desorption was performed by consecutive solidification and melting of the liquid hydrocarbon (m.p. 18 degrees C), resulting in coalescence of the droplets and reappearance of the desorbed moiety in the bulk aqueous phase. Of interest was the observation that lysozyme remains enzymatically active following this procedure.
D000327:Adsorption; D000473:Alkanes; D000818:Animals; D002645:Chickens; D006801:Humans; D009113:Muramidase / Q000302:isolation & purification; D011506:Proteins / Q000302:isolation & purification; D012463:Saliva / Q000201:enzymology; D012995:Solubility; D013329:Structure-Activity Relationship; D013696:Temperature; D014867:Water
D000473:Alkanes; D011506:Proteins; D014867:Water; D009113:Muramidase; C007932:n-hexadecane