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Protein-polysaccharide complexes as surfactants.

A N Gurov, P V Nuss

    Die Nahrung
    |January 1, 1986
    PubMed
    Summary
    This summary is machine-generated.

    Bovine serum albumin (BSA) and its complexes with dextran sulfate (DS) were studied at the decane-water interface. BSA-DS complexes showed significantly longer diffusion times and much higher maximum shear stress than BSA alone.

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    Area of Science:

    • Physical Chemistry
    • Surface Science
    • Biocolloid Science

    Background:

    • Interfacial properties of proteins are crucial in various biological and industrial applications.
    • Understanding the behavior of adsorbed proteins, like bovine serum albumin (BSA), at interfaces is essential.
    • The influence of complexation, such as with dextran sulfate (DS), on protein adsorption needs further investigation.

    Purpose of the Study:

    • To investigate the surface pressure (pi) and maximum shear stress (Ps) of decane-water interfaces with adsorbed bovine serum albumin (BSA) and BSA-dextran sulfate (DS) complexes.
    • To analyze the adsorption kinetics and interfacial rheology of BSA and BSA-DS complexes.
    • To determine the effect of protein concentration on these interfacial properties.

    Main Methods:

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  • Wilhelmy plate technique was employed to monitor surface pressure (pi) changes over time.
  • Surface viscoelastometry was utilized to measure maximum shear stress (Ps) at a constant shear rate.
  • Adsorption kinetics were analyzed by observing two distinct stages: diffusion and molecular rearrangement.

    • Main Results:

    • Adsorption of BSA and BSA-DS complexes occurred in two stages: diffusion-limited and rearrangement-limited.
    • The diffusion-controlled stage was significantly longer for BSA-DS complexes compared to BSA alone.
    • Maximum shear stress (Ps) values for BSA-DS complexes were 15-20 times higher than for free BSA, occurring at concentrations corresponding to the midpoints of surface pressure isotherms.

    Conclusions:

    • BSA-DS complexation alters the adsorption kinetics and interfacial rheology compared to BSA alone.
    • The enhanced shear stress suggests stronger interfacial films formed by BSA-DS complexes.
    • Interfacial behavior is dependent on protein concentration, with distinct optima for surface pressure and shear stress.