1992
DOI: 10.1016/0021-9797(92)90148-f
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Surface hydrophobic influences on β-lactoglobulin adsorption kinetics

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Cited by 74 publications
(67 citation statements)
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“…For enzymes with strong intermolecular interactions, structural rearrangements do not contribute significantly to the adsorption process. Such enzymes are easily adsorbed on hydrophobic surfaces; however, they can adsorb on hydrophilic surfaces only if they are electrostatically attracted (Krisdhasima et al 1992, Norde, 1986, 2003.…”
Section: Deformation Of Enzyme On Soil Surfacementioning
confidence: 99%
See 1 more Smart Citation
“…For enzymes with strong intermolecular interactions, structural rearrangements do not contribute significantly to the adsorption process. Such enzymes are easily adsorbed on hydrophobic surfaces; however, they can adsorb on hydrophilic surfaces only if they are electrostatically attracted (Krisdhasima et al 1992, Norde, 1986, 2003.…”
Section: Deformation Of Enzyme On Soil Surfacementioning
confidence: 99%
“…an electrostatically repelling surface. In such a case, structural rearrangements are the main driving force for adsorption (Krisdhasima et al, 1992;Malmsten, 1998;Norde, 2003).…”
Section: Deformation Of Enzyme On Soil Surfacementioning
confidence: 99%
“…The refractive index gives information about the compactness and hydration of the protein layer, whereas its thickness is related to the molecular dimensions and hence suggests possible orientations or restructuring of the adsorbed molecules. Unfortunately, in most of the ellipsometric studies reported so far only the adsorbed amount was monitored as a function of the different variables mentioned previously and very low attention was paid to the concomitant changes in the refractive index and layer thickness, with the consequent loss of valuable information about the system studied (23)(24)(25)(26). In the cases where the thickness and refractive index have been calculated together with the adsorbed amount, side-on orientation, end-on orientation, surface restructuring, bilayer formation, and multilayer formation have been proposed in order to explain the experimental data (22,27,28).…”
Section: Introductionmentioning
confidence: 99%
“…Experimental techniques that directly provide information about changes in the secondary structure include ATR-IR [108,111,112] and CD spectroscopy [53,91,104,113] whereas the elution properties are amenable through adsorption and desorption kinetics. Significant conformational changes of a protein are usually slow processes since often a whole cascade of angular rotations takes place [114][115][116][117]. Many proteins initially bind loosely on the surface and only increase their surface affinity afterwards in time by structural changes.…”
Section: Conformational Changesmentioning
confidence: 99%