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.
Sroková
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I
Slovak Technical University, Faculty of Chemical Technology, Bratislava.
Cík
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G
D000818:Animals; D001407:Bacillus / Q000201:enzymology*; D002417:Cattle; D002482:Cellulose / Q000031:analogs & derivatives*; D002918:Chymotrypsin / Q000737:chemistry* / Q000528:radiation effects; D003470:Culture Media; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000528:radiation effects; D008027:Light; D010777:Photochemistry; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000528:radiation effects
D003470:Culture Media; D004800:Enzymes, Immobilized; D002482:Cellulose; C002283:hydroxyethylcellulose; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C032923:microbial serine proteinases