| 초록 |
Biological methods for producing high-value glycerol products have recently received a great deal of attention. Glycerol dehydratase (GDHt) is an enzyme that dehydrates glycerol to form 3-hydroxypropanal (3-HPA). By joining the and subunits, the dissociation of the subunit during purification was avoided, which has the interesting effect of increasing the catalytic activity of the linked enzyme. Computational approaches such as protein modeling, molecular mechanics, and thermodynamics were used to compare the interface changes. The WT and fGDHt enzymes were cloned, expressed, and their activity, biochemical properties, and inactivation rate were all investigated. Overall, our findings indicate that linker-based fusion of the and subunits affects GDHt and the bound coenzymes, potentially delaying enzyme inactivation. |
