International Journal of Biological Macromolecules 2018, 111, 746-754. Interaction between structurally different heteroexopolysaccharides and β-lactoglobulin studied by solution scattering and analytical ultracentrifugation. Peters, Birte Svensson, Pernille Harris, Kristoffer Almdal. Sanaullah Khan, Johnny Birch, Marie-Rose Van Calsteren, Richard Ipsen, Günther H.J.International Journal of Food Properties 2021, 24 Physico-chemical and gel properties of heat-induced pasteurized liquid egg white gel: effect of alkyl chain length of alcohol. Brannan, Wilailuk Chaiyasit, Wanlop Chanasattru. Journal of Pharmaceutical Sciences 2021, 110 In-Use Interfacial Stability of Monoclonal Antibody Formulations Diluted in Saline i.v. SAXS Reveals the Stabilization Effects of Modified Sugars on Model Proteins. Ascenso, Maria Rita Ventura, Heinz Amenitsch, Paolo Moretti, Paolo Mariani, Maria Grazia Ortore, Francesco Spinozzi. Electrostatically Driven Protein Aggregation: β-Lactoglobulin at Low Ionic Strength. Vanam, Emek Seyrek, Katie Giger, and, Paul L.
The Journal of Physical Chemistry B 2007, 111 Effect of the Air−Water Interface on the Stability of β-Lactoglobulin. The Journal of Physical Chemistry B 2012, 116 Biosurfactant–Protein Mixtures: Quillaja Bark Saponin at Water/Air and Water/Oil Interfaces in Presence of β-Lactoglobulin. Marek Piotrowski, Joanna Lewandowska, and Kamil Wojciechowski.pH-Dependent Aggregation and Disaggregation of Native β-Lactoglobulin in Low Salt. Yunfeng Yan, Daniel Seeman, Bingqian Zheng, Ebru Kizilay, Yisheng Xu, and Paul L.Revealing the Dimeric Crystal and Solution Structure of β-Lactoglobulin at pH 4 and Its pH and Salt Dependent Monomer–Dimer Equilibrium. Sanaullah Khan, Richard Ipsen, Kristoffer Almdal, Birte Svensson, Pernille Harris.The Journal of Physical Chemistry B 2019, 123 Neutron Reflectometry Study on the Effect of pH. β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 3. Noskov, Reinhard Miller, Emanuel Schneck. This article is cited by 51 publications.
Panfu beta free#
As a result, the dissociation free energy has been obtained as a function of the ionic strength, yielding an excellent agreement with photon correlation spectroscopy data. A global fit of the SAXS scattered intensities at different salt concentrations using a simple electrostatic model for the aggregation mechanism is presented.
Small angle X-ray scattering measurements performed versus ionic strength (from 7 to 507 mM) in dilute solutions (10 g/L) allow an independent estimate of the dimerization fraction. From a detailed analysis, estimates of the protein charge, hydrodynamic radius, and dimeritazion fraction have been obtained. The interparticle interactions are determined by means of Photon correlation spectroscopy by following the trend of the protein diffusion coefficient versus concentration (from 0.2 to 25 g/L) at ionic strengths of 7 and 107 mM. Both experiments give a clear evidence of a protein monomer−dimer equilibrium affected by the ionic strength of the solution. Β-Lactoglobulin, a protein belonging to the lipocaline family, is studied by Photon correlation spectroscopy and small angle X-ray scattering in acidic solutions (pH = 2.3) and at ionic strengths in the range 7−507 mM.
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