Study of the photochemical immobilization of alkaline proteinase and chymotrypsin on the solid phase of O-hydroxyethylcellulose.

Stability of the photochemically immobilized alkaline proteinase (E.C. 3.4.21.14) and chymotrypsin (E.C. 3.4.21.1.) onto the gel of O-hydroxyethylcellulose has been studied. For the purpose of immobilization the photochemical generation of nitrene radicals caused by the photolysis of an azido group of bifunctional 4,4'-bis-azidostilbene-2,2'-disodium-sulphate and the newly synthetized O-(3-azidophthaloyl)-O-hydroxyethylcellulose have been employed. The immobilized alkaline proteinase demonstrated a decreased ability of denaturation and an increased laboratory stability.