ORIGINAL RESEARCH article
Front. Microbiol.
Sec. Microbiotechnology
Volume 16 - 2025 | doi: 10.3389/fmicb.2025.1615845
This article is part of the Research TopicIndustrial Application of Extreme Microbes: Harnessing the Power of Nature's ExtremophilesView all 6 articles
Characterization of a Thermostable Uricase Derived from Thermoactinospora rubra YIM 77501 T and Its Heat-resistant Mechanism
Provisionally accepted- 1Dali University, Dali, China
- 2Sun Yat-sen University, Guangzhou, Guangdong Province, China
- 3The First Affiliated Hospital of Kunming Medical University, Kunming, Yunnan Province, China
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Uricases are oxidative enzymes that catalyze the conversion of uric acid to allantoin and hydrogen peroxide, widely utilized in uric acid testing and the treatment of gout, hyperuricemia, and Tumor Lysis Syndrome (TLS). The search for uricases with long-term thermostability has become a significant area of research. In this study, a uricase gene (truox) was obtained from the genome of Thermoactinospora rubra YIM 77501 T , which was subsequently cloned and heterologously expressed. The resulting enzyme, TrUox, was comprehensively characterized for its biochemical properties and analyzed through molecular dynamics (MD) simulations.TrUox exhibits maximal catalytic activity at 35°C and pH 7.6 (mesophilic range). Notably, its thermostability is exceptional: the enzyme retains over 90% residual activity after 4 days of incubation at 50°C (with activity measured post-thermal treatment at 35°C) and maintains >90% activity for 10 days at physiological temperature (37°C).In vitro, 1.14 µg/mL TrUox effectively lowered serum uric acid (UA) from >700 μM to <420 μM within 2 hours in hyperuricemic models.MD simulations comparing TrUox with Rasburicase indicate it's more rigid/stable globally, less flexible, has fewer sub-states, and is more stable in FEL. These results demonstrate TrUox as a robust uricase exhibiting dual advantages of catalytic efficiency and enhanced thermostability, positioning it as a promising biocatalyst for industrial-scale production and therapeutic development. Our preliminary study into its thermostable mechanism provides a theoretical foundation for future production and research.
Keywords: Uricase, Thermoactinospora rubra YIM 77501 T, Thermostable, Heat-resistant Mechanism, Degrade uric acid
Received: 22 Apr 2025; Accepted: 30 May 2025.
Copyright: © 2025 Yin, Yan, Tang, Ortúzar, Yang, Sang, Jin, Li, Yang, Wang, Li and Hu. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence:
Yi-Rui Yin, Dali University, Dali, China
Wei Hu, The First Affiliated Hospital of Kunming Medical University, Kunming, 650032, Yunnan Province, China
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