Interfacial behaviour of proteins in three phase partitioning using salt containing water/tertbutanol systems Three phase partitioning (TPP) was used to investigate the partitioning of four model proteins (bovine serum albumin, ovalbumin, lysozyme and gelatine) in a system containing water, tert-butanol and an inorganic electrolyte (NH4)2SO4. Phase diagrams of the ternary (protein free) system and interfacial tensions between the equilibrium upper and lower liquid phases have been determined at 25°C. The amount of protein precipitated in the middle layer was delineated as a function of the composition of the partitioning system as well as the initial protein concentration. No dependence of the relative amount of protein accumulated in the midlayer on the total amount of protein has been observed. The constant partitioning ratio found in TPP emphasizes the partitioning character of the process. The interfacial adsorption of a single protein (indicated by the decreasing interfacial tension between the immiscible liquid phases) shows a good correlation with the accumulation of the same protein in TPP as a middle layer for the various proteins investigated.
|Number of pages||8|
|Journal||Magyar Kemiai Folyoirat, Kemiai Kozlemenyek|
|Publication status||Published - dec. 1 1998|
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