| 초록 |
Recently biological processes to produce high-value products from glycerol have drawn much attention. Glycerol dehydratase (GDHt) is involved in the dehydration of glycerol to form 3-hydroxypropanal (3-HPA). The dissociation of β subunit in purification has been circumvented through the linking of α and β subunits which interestingly increases the catalytic activity of the linked enzyme. Protein modeling, molecular mechanics, and thermodynamics computational approaches were utilized to comparatively monitor the intra- and inter-subunits interface changes. Cloning, expression, and activity assay were performed on the WT and fGDHt to evaluate the enzyme activity, biochemical properties, and inactivation rate. Overall, our findings suggest that linker-based fusion of the α and β subunits affect the stability of GDHt and the bound coenzymes, which may delay the inactivation of the enzyme. |
