The experimental technique is presented which allows the investigation of water at the adsorbent-biopolymer interface by record of temperature dependencies of 1H NMR signals during the heating of previously frozen water suspensions. It was found that the adsorption of protein conconovalin A resulted in twofold decrease of strong bound water amount and in 70% increase of loosely bound one. The mean-value of Gibbs energy decreased twice for strong bound water and increased twice for loosely bound one. The external layer of hydrate shell of silica particles with adsorbed conconovalin A was organized by protein molecules. This conclusion is based on the observed total increase of loosely bound water amount, as a result, of protein adsorption, although its amount with respect to a protein molecule decreased.

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