[Immobilization of trypsin on polyurethane carriers].
A method of covalent immobilization of trypsin on polyurethanes containing residues of 2.4-toluene or hexamethylene diisocyanates in a side chain is developed. It is shown that the amount of the immobilized enzyme is independent of isocyanate nature, but its proteolytic activity is higher on carriers containing 2.4-toluene diisocyanate residues. This is accounted for by higher mobility of enzyme molecules due to a decrease in the number of chemical bonds between trypsin and the polymer matrix. The immobilized enzyme is stable for a long time and does not lose proteolytic activity being cyclically used for many times.
Rakhlevskiĭ
L V
LV
Grigor'eva
M V
MV
Pkhakadze
G A
GA
D003485:Cyanates / Q000737:chemistry; D004800:Enzymes, Immobilized; D006868:Hydrolysis; D017953:Isocyanates; D011140:Polyurethanes / Q000737:chemistry*; D014051:Toluene 2,4-Diisocyanate / Q000737:chemistry; D014357:Trypsin / Q000737:chemistry*
D003485:Cyanates; D004800:Enzymes, Immobilized; D017953:Isocyanates; D011140:Polyurethanes; C015262:1,6-hexamethylene diisocyanate; D014051:Toluene 2,4-Diisocyanate; D014357:Trypsin
Immobilizatsiia tripsina na poliuretanovykh nositeliakh.