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- W2075899157 abstract "The viscosity of solutions of four proteins (Bovine Serum Albumin, Ovalbumin, α s -1 Casein, Lysozyme), brought to the random coil conformation, has been measured over a large concentration range extending into the entanglement region. A master curve is obtained in the dilute and semi-dilute regions with the reduced variables ( tilde eta = {eta _{sp}}/left[ eta right]c ) and ( tilde c = c/y ) of Simha and Utracki.By using Graessley’s expression for the polymer coil expansion at a given concentration in the semi-dilute region (c* ≤ c ≤ c**), a simple equation is established giving the relative viscosity η r , as a function of concentration c: for ( {c^ * } leqslant c leqslant {c^{ * * }},;{text{in}};{eta _r} = 2aleft[ eta right]{c^ * }{left( {c/{c^ * }} right)^{1/2a}} - (2a - 1)left[ eta right]{c^ * }; ) where c* is the incipient overlap concentration, [η] the intrinsic viscosity, and a the Mark-Houwink exponent for the polymer-solvent considered.This equation fits well the experimental results. The adjustment yields for the parameter a values which are comprised between 0.6 and 0.7, as expected, for Bovine Serum Albumin and Ovalbumin, but very close to 0.5 for α s -1 Casein and Lysozyme. This can be explained by the fact that the molecular weights of the two latter proteins are lower than, or very close, the critical molecular weight; the critical molecular weight is estimated to be about 20000." @default.
- W2075899157 created "2016-06-24" @default.
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- W2075899157 date "1982-01-01" @default.
- W2075899157 modified "2023-10-18" @default.
- W2075899157 title "Viscosity of concentrated protein solutions" @default.
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- W2075899157 doi "https://doi.org/10.1007/978-3-662-12809-1_69" @default.
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