[Immobilization of glucoamylase and acid proteinase on modified silichrome using N-carbethoxy-2-ethoxy-1,2-dihydroquinoline].
Using N-carbethoxy-2-ethoxy-1,2-dihydrochinoline, glucoamylase and acid proteinase were immobilized on silochrome C-80 modified by gamma-aminopropyl triethoxy silane and then succinic anhydride. The maximum percentage of protein binding was 46.0 for glucoamylase and 35.0 for acid proteinase. Acid proteinase showed a decrease of specific activity.
D004800:Enzymes, Immobilized / Q000378:metabolism*; D005087:Glucan 1,4-alpha-Glucosidase / Q000378:metabolism*; D005959:Glucosidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010447:Peptide Hydrolases / Q000378:metabolism*; D011804:Quinolines
D004800:Enzymes, Immobilized; D011804:Quinolines; C000470:EEDQ; D005959:Glucosidases; D005087:Glucan 1,4-alpha-Glucosidase; D010447:Peptide Hydrolases
Immobilizatsiia gliukoamilazy i kisloĭ proteinazy na modifitsirovannom silokhrome s ispol'zovaniem N-karbetoksi-2-etoksi-1,2-digidrokhinolina.