Identification of a robust bacterial pyranose oxidase that displays an unusual pH dependence.

ABSTRACT: Pyranose oxidases are valuable biocatalysts, yet only a handful of bacterial pyranose oxidases are known. These bacterial enzymes exhibit noteworthy distinctions from their extensively characterized fungal counterparts, encompassing variations in substrate specificity and structural attributes. Herein a bacterial pyranose oxidase from Oscillatoria princeps (OPOx) was biochemically characterized in detail. In contrast to the fungal pyranose oxidases, OPOx could be well expressed in Escherichia coli as soluble, fully flavinylated, and active oxidase. It was found to be highly thermostable (melting temperature >90 °C) and showed activity on glucose, exhibiting an exceptionally low K_M value (48 μM). Elucidation of its crystal structure revealed similarities with fungal pyranose oxid

SUBMITTER: Santema LL 

PROVIDER: S-EPMC11650716 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature