Thermostable cyanuric acid hydrolase from Moorella thermoacetica ATCC 39073

Qingyan Li, Jennifer L. Seffernick, Michael J. Sadowsky, Lawrence P. Wackett

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)6986-6991
Number of pages6
JournalApplied and environmental microbiology
Volume75
Issue number22
DOIs
StatePublished - Nov 2009

Fingerprint Dive into the research topics of 'Thermostable cyanuric acid hydrolase from Moorella thermoacetica ATCC 39073'. Together they form a unique fingerprint.

Cite this