[Immobilization of trypsin on polyurethane matrix]

A method is developed to bind trypsin with the polyurethane matrix. At the first stage the reaction between trypsin and toluylendiisocyanate (TD1) was performed. At the second stage polyisocyanate obtained on the base of TDI-trypsin was sewn with polyoxypropylene glycol with a molecular weight of 1500. 2,4,6-Tris(dimethylaminomethyl)phenol served as an accelerator of the reaction. The polymer obtained is fine-porous and high-elastic. The chemical interaction of trypsin with the polymer is confirmed by the method of IR-spectroscopy and a decrease in the amount of free isocyanate groups. It is shown that the enzymic activity of trypsin chemically bound with the polymer is preserved at a room temperature for several months. When the polymeric net is formed from macrodiisocyanate in the presence of trypsin under conditions when the chemical interaction between the polymer and enzyme activity is also preserved, its value in this case being dependent on the relative content of the enzyme in the polymer -- it is higher in the case when the relative content of the enzyme is less, that may indicate the role of the polymer as a heterogenic cocatalyst or activator. The value of the proteolytic activity of the polymer with the chemically added trypsin is practically constant with its washing off in the column for 24h with 0,05 M veronal buffer whereas under these conditions the polymer with "free" trypsin loses completely the enzymic activity.