Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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A Kinetic Study on the Adsorptionof Compact, Water-soluble Proteins onto Aqueous Surfaces

  • Published : 1999.09.20
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Abstract

Two compact sized globular proteins, β-lactoglobulin and α-lactalbumin were kinetically characterized at the aqueous solution surface with the measurement of surface pressure (π) and surface concentration (Γ) via a radiotracer method. The adsorption kinetics was of diffusion control at early times, the rates of increase of πand Γ being lower at longer times due to growing energy barrier. At low concentrations, an apparent time lag was observed in the evolution of π for β-lactoglobulin but not for α-lactalbumin which was shown to be due to the non-linear nature of the p- G relationship for the former. The area per molecule of an adsorbed β-lactoglobulin during adsorption was smaller than that for spread monolayer since β-lactoglobulin was not fully unfolded during the adsorption. For α-lactalbumin, however, no such difference in the molecular areas for adsorbed and spread monolayer was observed indicating thereby that α-lactalbumin unfolded much more rapidly (has looser tertiary structure) than β-lactoglobulin. Surface excess concentrations of α-lactalbumin was found to evolve in two steps possibly due to the change in the orientation of the adsorbed protein from a side-on to an end-on orientation.

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