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NMR Study of Non-freezing Water in Protein-Modified Carbon Adsorbents

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Abstract

Temperature dependences of 1H NMR spin–spin relaxation were studied for the non-freezing water at the surface of carbon matrices modified with proteins (human serum albumin (HSA) and mouse immunoglobulin (MIG)) in the presence of water-soluble carbodiimide. The entropy, ΔS ≠, and enthalpy, ΔH ≠, values characterizing molecular mobility in non-freezing water were estimated. The compensation effect was observed for all modified samples, which is well approximated by the linear dependence of the type ΔH ≠ = T 0ΔS ≠ + ΔH ≠ 0. The compensation temperature T 0 = 231 ± 33 corresponds to such a state of non-freezing water, when the effect of modifying additives on the isobaric potential of molecular mobility activation in the non-freezing water, ΔG ≠, is minimal. The ΔG ≠ has approximately constant value equal to ΔH ≠ 0 = 24.2 ± 0.5 kJ/mol. Modification of the base carbon matrix with MIG protein results in higher structurization of the non-freezing water, whereas HSA reduces this structurization. The observed effects are explained in terms of the hydration of modifying agents and also by the peculiarities of their location on the surface of carbon adsorbent.

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Authors and Affiliations

  1. National Academy of Sciences of Ukraine, Institute of Physics, pr. Nauki 46, Kiev, 02022, Ukraine

    T. A. Alekseeva

  2. National Academy of Sciences of Ukraine, Ovcharenko Institute of Biocolloid Chemistry, bul'v. Vernadskogo 42, Kiev, 03142, Ukraine

    N. I. Lebovka

  3. School of Pharmacy & Biomolecular Sciences, University of Brighton, Brighton, BN2 4GJ, UK

    S. V. Mikhailovsky

Authors
  1. T. A. Alekseeva
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  2. N. I. Lebovka
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  3. S. V. Mikhailovsky
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Alekseeva, T.A., Lebovka, N.I. & Mikhailovsky, S.V. NMR Study of Non-freezing Water in Protein-Modified Carbon Adsorbents. Colloid Journal 65, 275–279 (2003). https://doi.org/10.1023/A:1024286102129

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