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Microbial uricase enzymes in hyperuricemia management: Sources, challenges, and technological advances.
Sneha O Pustake1, Prashant Bhagwat2, Santhosh Pillai2
1Department of Biochemistry, Shivaji University, Kolhapur 416004, India.
Journal of Microbiological Methods
|September 19, 2025
Summary
Uricase enzyme activity regulates uric acid levels, crucial for preventing gout and hyperuricemia. Novel recombinant uricase variants offer improved stability and reduced immunogenicity for effective gout treatment.
Area of Science:
- Biochemistry
- Enzymology
- Pharmacology
Background:
- Uric acid metabolism is regulated by uricase enzyme.
- Elevated uric acid (hyperuricemia) causes gout.
- Current recombinant uricases (rasburicase, pegloticase) have limitations like immunogenicity and short half-life.
Purpose of the Study:
- Review alternative uricase sources and properties.
- Discuss clinical implications of uricase.
- Explore potential of novel recombinant uricase variants.
Main Methods:
- Literature review of uricase sources, properties, and applications.
- Analysis of recombinant uricase technology.
- Discussion of uricase-based biosensors and nanocomposites.
Main Results:
- Uricase is found in microbial, plant, and animal sources.
- Recombinant uricases show therapeutic promise but require improvement.
- Genetically modified and PEG-conjugated uricases are promising.
- Uricase-based biosensors enable facile uric acid detection.
Conclusions:
- Novel uricase variants with lower immunogenicity and enhanced stability are needed.
- Recombinant uricase holds significant potential for treating hyperuricemia and gout.
- Uricase-based diagnostics and therapeutics are advancing clinical applications.
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