Glycerol kinase is essential for the efficient use of glycerol as a carbon and energy source. In the presence of glycerol, GlpK is stimulated by interaction with the membrane-bound glycerol facilitator . This enzyme is particularly significant in biotechnological applications where glycerol is used as a feedstock for the production of various compounds.
The recombinant expression of glycerol kinase involves cloning the glpK gene into a suitable expression vector and transforming it into an E. coli host strain. This allows for the overproduction of the enzyme, which can then be purified and characterized for various applications. For instance, the GK gene has been synthesized and cloned into a pET-24a (+) vector and over-expressed in E. coli BL21 (DE3) .
Recombinant glycerol kinase from E. coli has been utilized in several biotechnological processes. One notable application is the production of L-phenylalanine (L-Phe) from glycerol. By increasing the gene copy numbers for glpK, along with other genes like glpX and tktA, researchers have been able to enhance L-Phe productivity without affecting the growth rate of the E. coli strains .