Dye-decolorizing peroxidases (DyPs)
As alternatives for the plant and animal peroxidases, the newly discovered DyP-type peroxidases (DyPs) may offer advantages. Except for facilitating the production of peroxidases and eliminating the existence of isoforms, the ability to produce DyPs in a recombinant form also allows engineering of these biocatalysts. The first DyPs were identified less than two decades ago. DyPs are unrelated in sequence and structure to known peroxidases belonging to the plant or animal peroxidase superfamilies. DyPs are typically identified by their activity on anthraquinone dyes. While DyPs are efficient in degrading these synthetic dyes, the physiological substrates for DyPs are unclear and therefore their role in nature is enigmatic. Interestingly, recent studies suggest that bacterial DyPs may play an important role in the degradation of lignin which suggests that DyPs represent the bacterial counterparts of the fungal lignin peroxidases. Except for establishing their activity on synthetic dyes and possible role in lignin degradation, little data is available concerning their biocatalytic potential.
- TfuDyP Thermobifida fusca DyP
- SviDyP Saccharomonospora viridis DyP
- YfeX Escherichia coli DyP
- PfDyP Pseudomonas fluorescens DyP
We are also offering purified basic and acidic isoforms of horseradish peroxidase (HRP).
