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Micellar solubilization of biopolymers in hydrocarbon solvents. I. a structural model for protein-containing reverse micelles

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Abstract

Three proteins (horse liver alcohol dehydrogenase, ribonuclease, lysozyme) were solubilized in hydrocarbon with the help of reverse micelles formed by aqueous di(2-ethyl-hexyl) sodium sulfosuccinate (AOT). Sedimentation and diffusion coefficients of the micellar aggregates were measured with an analytical ultracentrifuge. Partial specific volumes were also evaluated from density measurements. The molecular weight of the protein-containing reverse micelles (M t ) could thus be determined for each protein system at various w0 values (w0 - [H2O]/[AOT]). For horse liver alcohol dehydrogenase at w0 = 46.4, for example,M t is ca. 2,670,000 Daltons; for lysozyme at wo = 22.5,M t is ca. 323,000 Daltons and increases by increasing w0. On the basis of these experimentally determined molecular weights, a structural model for the protein-containing reverse micelle is proposed. The model is based upon the assumption that the protein is confined in the water pool of a spherical micelle, and that the inner core volume is the sum of the protein volume and the volume of all water molecules present in a micelle. It is possible then to calculate the micellar structure at each w0 value. For example, in the case of ribonuclease at w0 = 20, the inner core radius is ca. 37.5 A, and a layer of water of ca. 22 A separates the protein surface from the surfactant layer. The possible implications of this model for the reactivity of enzymes solubilized in hydrocarbons by reverse micelles are discussed.

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Authors and Affiliations

  1. Technisch-Chemisches Laboratorium der ETH-Zurich ETH-Zentrum, 8031-Zurich, Switzerland

    Francis J. Bonner, Romain Wolf & Pier Luigi Luisil

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  1. Francis J. Bonner
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  2. Romain Wolf
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  3. Pier Luigi Luisil
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Bonner, F.J., Wolf, R. & Luisil, P.L. Micellar solubilization of biopolymers in hydrocarbon solvents. I. a structural model for protein-containing reverse micelles. Journal of Solid-Phase Biochemistry 5, 255–268 (1980). https://doi.org/10.1007/BF03000661

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