Immobilization of lactate dehydrogenase on polyacrylamide beads.
Pig muscle lactate dehydrogenase (L-lactate:NAD oxidoreductase, EC 1.1.1.27) was covalently immobilized on polyacrylamide beads containing carboxylic functional groups activated by water-soluble carbodiimide. The effects of immobilization on the catalytic properties and stability of the lactate dehydrogenase were studied. There was no shift in the pH optimum of the immobilized enzyme compared to that of the soluble one. The apparent optimum temperature of the soluble enzyme was 65 degrees C, while that of the immobilized enzyme was between 50 and 65 degrees C. The apparent Km values of the immobilized enzyme with pyruvate and NADH substrates were higher than those of the soluble enzyme. As a result of immobilization, enhanced stabilities were found against heat treatment, changes in pH, and urea denaturation.
D000180:Acrylic Resins; D000818:Animals; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000032:analysis*; D008863:Microspheres; D009124:Muscle Proteins / Q000032:analysis; D009132:Muscles / Q000201:enzymology; D013552:Swine; D013696:Temperature; D014508:Urea / Q000032:analysis; D000099166:Polyacrylamides
D000180:Acrylic Resins; D004800:Enzymes, Immobilized; D007770:L-Lactate Dehydrogenase; D009124:Muscle Proteins; D014508:Urea; D000099166:Polyacrylamides