Behavior of enzyme activity in immobilized proteases.
Proteases such as trypsin, alpha-chymotrypsin, papain, and thermolysin were immobilized by radiation polymerization of various monomers at low temperatures, and behavior of enzyme activity in immobilized proteases was studied. The enzyme activity in immobilized proteases appeared to be different by the kind of proteases; the order of the magnitude of the enzyme activity was papain greater than trypsin greater than thermolysin greater than alpha-chymotrypsin. This difference of the enzyme activity was explained by the change of the molecular conformation in enzyme reaction.
D002918:Chymotrypsin / Q000378:metabolism* / Q000528:radiation effects; D003037:Cobalt Radioisotopes; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005720:Gamma Rays; D010206:Papain / Q000378:metabolism* / Q000528:radiation effects; D013820:Thermolysin / Q000378:metabolism* / Q000528:radiation effects; D014357:Trypsin / Q000378:metabolism* / Q000528:radiation effects
D003037:Cobalt Radioisotopes; D004800:Enzymes, Immobilized; D002918:Chymotrypsin; D014357:Trypsin; D010206:Papain; D013820:Thermolysin