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Kinetic Relationships of the Adsorption of Lysozyme and Bovine Serum Albumin onto Zeolites of BEA and MFI Structural Types

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Abstract

The kinetics of the adsorption of lysozyme and bovine serum albumin (BSA) onto zeolites of BEA and MFI structural types and onto silica adsorbents of the same structural types was studied. The rate constants of the reversible adsorption step were calculated. The adsorption rate constants are 0.4–0.8 L mol–1 s–1 for lysozyme and 0.7–1.4 L mol–1 s–1 for BSA. The rate constants of the desorption from the surface of all the samples are in the range from 1.3 × 10–5 to 1.6 × 10–5 s–1 for both enzymes.

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Funding

The synthesis of BEA zeolites, study of their physicochemical and acid properties, and study of the lysozyme adsorption kinetics were financially supported by the Russian Science Foundation (project no. 20-13-00203, https://rscf.ru/project/20-13-00203).

The kinetics of the BSA adsorption onto the surface of ZSM-5 zeolite and silicalite-1 was studied within the framework of the government assignment: Physical Chemistry of the Surface, Adsorption, and Catalysis.

Studies of the phase composition and morphology of the samples were financially supported by the Science and Universities national project.

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Atyaksheva, L.F., Dobryakova, I.V., Enbaev, Z.S. et al. Kinetic Relationships of the Adsorption of Lysozyme and Bovine Serum Albumin onto Zeolites of BEA and MFI Structural Types. Pet. Chem. (2024). https://doi.org/10.1134/S0965544124010110

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