Immobilization of pig muscle aldolase on a silica-based support.
Pig muscle aldolase was covalently attached to a silica-based support possessing aldehyde functional groups. The activity of the immobilized enzyme was 37 U/g solid, and the specific activity calculated on a bound protein basis was 1.9 U/mg protein. The optimum pH for the catalytic activity was pH 7.5. The apparent optimum temperature was found to be 45 degrees C. The Km app value of the immobilized aldolase with D-fructose 1,6-diphosphate as substrate was 1.25 X 10(-4) M. The conformational stability was improved by the immobilization. The immobilized aldolase was used for the continuous splitting of D-fructose 1,6-diphosphate.
Horváth
L
L
Department of Biochemistry, Attila József University, Szeged, Hungary.
Abrahám
M
M
Boross
L
L
Szajáni
B
B
D000818:Animals; D002384:Catalysis; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D005635:Fructosediphosphates / Q000378:metabolism; D005782:Gels; D006863:Hydrogen-Ion Concentration; D009132:Muscles / Q000201:enzymology*; D058428:Silica Gel; D012822:Silicon Dioxide; D012995:Solubility; D013552:Swine; D013696:Temperature; D014508:Urea
D004800:Enzymes, Immobilized; D005635:Fructosediphosphates; D005782:Gels; D058428:Silica Gel; D012822:Silicon Dioxide; D014508:Urea; D005634:Fructose-Bisphosphate Aldolase; C029063:fructose-1,6-diphosphate