Immobilized Enzymes:The Catalytic Properties of Lactate Dehydrogenase Covalently Attached to Glass Beads,

摘要

Chick LDH (H4 & M4) has been covalently attached to aryl and alkyl amine glass using sodium nitrite and glutaraldehyde respectively. These immobilized enzymes remain active for months at 0C and exhibit Km values similar to those of the soluble enzyme;however,they have pH-rate profiles that are independent of pH and show decreased substrate inhibition. Disaggregation followed by reassociation indicate the enzymes are bound by all four subunits and the resulting activity restored to the native,aryl amine and glutaraldehyde bound enzyme are 33, 25,and 90% respectively. At a pH of 3.2and 25C,the soluble and aryl amine glass LDH's are rapidly denatured while the glutaraldehyde bound enzyme shows no loss of activity for at least 35days.