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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 35 (1991), S. 766-770 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Axisymmetric drop shape analysis by profile (ADSA-P) is a technique developed in colloid and surface science to simultaneously determine the contact angle and liquid surface tension from the profile of a droplet resting on a solid surface. In this paper is described how ADSA-P can be employed to assess bacterial biosurfactant production. Nine Streptococcus mitis strains, two of which are known to produce biosurfactants, and two S. salivarius strains, which do not produce biosurfactants, were suspended at two concentrations in a 10-mm potassium phosphate buffer, pH 7.0. Subsequently, a 100-μl droplet of each suspension was put on a fluoroethylenepropylene surface and the profile of the droplet determined with a contour monitor as a function of time up to 2 h. The surface tension of these suspensions was then calculated from the droplet profiles with ADSA-P. The surface tension of suspensions of the two non-producing strains remained stable within 4 mJ·m−2, whereas the surface tension of suspensions of five out of the nine S. mitis strains employed, including those of the known producer strains, decreased significantly (up to 26 mJ·m−2). This decrease was, in addition, concentration dependent. From these observations, we decided that all strains for which these concentration-dependent decreases were observed, could be regarded as biosurfactant producers. In order to rule out the possibility that the surface tension decreases observed were due to the collection of cells at the suspension-air interface, we investigated whether there was a relationship between surface tension decrease and hydrophobicity of the cells, as assessed by contact angle measurements and bacterial adhesion to hydrocarbons. Since no such a relationship was found, it can be concluded that ADSA-P is an excellent technique, based on using small amounts of cells to rapidly determine whether or not a bacterial strain produces biosurfactants.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1435-1536
    Keywords: Protein adsorption ; interfacial tension ; solid-liquid interface ; liquid-vapor interface
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Interfacial tension changes during protein adsorption at both the solid-liquid and the liquid-vapor interface were measured simultaneously by ADSA-P from sessile droplets of protein solutions on fluoroethylenepropylene-Teflon. Four globular proteins of similar size, viz. lysozyme, ribonuclease, α-lactalbumin and Ca2+-free α-lactalbumin, and one larger protein, serum albumin, were adsorbed from phosphate solutions at varying pH values (pH 3-12). The kinetics of the interfacial tension changes were described using a model accounting for diffusion-controlled adsorption of protein molecules and conformational changes of already adsorbed molecules. The contribution of conformational changes to the equilibrium interfacial pressure was shown to be relatively small and constant with respect to pH when compared to the contribution of adsorption of the protein molecules. The model also yields the diffusion relaxation time and the rate constant for the conformational changes at the interface. Around the isoelectric point of a protein the calculated diffusion relaxation time was minimal, which is ascribed to the absence of an energy barrier to adsorption. Energy barriers to adsorption become larger at pH values away from the isoelectric point and can therefore become rate-limiting for the adsorption process. The rate constants for conformational changes at the liquid-vapor interface were maximal around the isoelectric point of a protein, suggesting a smaller structural stability of the adsorbed protein. At the solid-liquid interface the rate constants were smaller and independent of pH. indicating that conformational changes more readily occur at the liquid-vapor than at the solid-liquid interface.
    Type of Medium: Electronic Resource
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