Creating a Polymerizable Xylanase A Variant
Author Information
Author(s): Szabó Veronika, Muskotál Adél, Tóth Balázs, Mihovilovic Marko D., Vonderviszt Ferenc
Primary Institution: University of Pannonia, Hungary
Hypothesis
Can the polymerization ability of flagellin be combined with the catalytic capabilities of xylanase A by creating a fusion construct?
Conclusion
The study successfully created a fusion protein that retains both polymerization ability and catalytic activity.
Supporting Evidence
- The fusion protein exhibited both catalytic activity and polymerization ability.
- Filament formation was observed under specific conditions.
- The study demonstrated that the D3 domain of flagellin can be replaced without affecting polymerization.
Takeaway
Scientists made a new protein that can both stick together to form long strands and help break down plant materials.
Methodology
The researchers engineered a fusion protein by replacing a part of flagellin with xylanase A and tested its polymerization and catalytic properties.
Limitations
The stability of the filaments formed by the fusion protein was only maintained in the presence of high concentrations of ammonium sulfate.
Digital Object Identifier (DOI)
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