Designing a highly active soluble PQQ–glucose dehydrogenase for efficient glucose biosensors and biofuel cells

We report for the first time a soluble PQQ–glucose dehydrogenase that is twice more active than the wild type for glucose oxidation and was obtained by combining site directed mutagenesis, modelling and steady-state kinetics. The observed enhancement is attributed to a better interaction between the cofactor and the enzyme leading to a better electron transfer. Electrochemical experiments also demonstrate the superiority of the new mutant for glucose oxidation and make it a promising enzyme for the development of high-performance glucose biosensors and biofuel cells.

Research highlights
► A new mutant of PQQ–GDH designed for glucose biosensors application.
► First mutant of PQQ–GDH with higher activity for d-glucose than the Wild type.
► Position N428 is a key point to increase the enzyme activity.
► Molecular modeling shows that the N428 C mutant displays a better interaction for PQQ than the WT.