Analysis of catalytic properties of quinoprotein glycerol dehydrogenase and its application

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Quinoprotein glycerol dehydrogenase (GLDH) is a membrane-bound enzyme, which is found in Gluconobacter having attractive industrial applications. In this study, the primary structure of GLDH was compared with other quinoproteins to understand its unique catalytic properties, and then mutant GLDH was prepared in heterologous expression in Gluconobacter.This study provided the following finding. (i) The propeller structure of PQQ enzyme, especially W1 and W2, are important for GLDH activity. (ii) Heterologous expression system in acetic acid bacteria was constructed to prepare mutant GLDH (iii) GLDH mutants that improved PQQ-binding stability, were prepared by the point mutation based on comparative analysis among PQQ-enzymes. The data will lead to improvement in oxidative fermentation of 5-keto-D-gluconate and others.