Related Experiment Video
Updated: Jun 20, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Thermostable cyanuric acid hydrolase from Moorella thermoacetica ATCC 39073
Qingyan Li1, Jennifer L Seffernick, Michael J Sadowsky
1Department of Microbiology and Key Laboratory of Bioactive Materials, Ministry of Education, Nankai University, Tianjin 30071, China.
Abstract:
Cyanuric acid, a metabolic intermediate in the degradation of many s-triazine compounds, is further metabolized by cyanuric acid hydrolase. Cyanuric acid also accumulates in swimming pools due to the breakdown of the sanitizing agents di- and trichloroisocyanuric acid. Structurally stable cyanuric acid hydrolases are being considered for usage in pool water remediation. In this study, cyanuric acid hydrolase from the thermophile Moorella thermoacetica ATCC 39073 was cloned, expressed in Escherichia coli, and purified to homogeneity. The recombinant enzyme was found to have a broader temperature range and greater stability, at both elevated and low temperatures, than previously described cyanuric acid hydrolases. The enzyme had a narrow substrate specificity, acting only on cyanuric acid and N-methylisocyanuric acid. The M. thermoacetica enzyme did not require metals or other discernible cofactors for activity. Cyanuric acid hydrolase from M. thermoacetica is the most promising enzyme to use for cyanuric acid remediation applications.
Related Concept Videos
Hyperthermophilic Bacteria
Diversity of Archaea IV
Diversity of Archaea III
Diversity of Archaea I
Factors Influencing Microbial Growth: Temperature
Anoxygenic Phototrophic Bacteria

