Open AccessThermostable Cyanuric Acid Hydrolase from Moorella thermoacetica ATCC 39073
Author(s) -
Qingyan Li,
Jennifer L. Seffernick,
Michael J. Sadowsky,
Lawrence P. Wackett
Publication year - 2009
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.01605-09
Subject(s) - cyanuric acid , biochemistry , hydrolase , chemistry , enzyme , melamine , organic chemistry
Cyanuric acid, a metabolic intermediate in the degradation of manys -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 thermophileMoorella thermoacetica ATCC 39073 was cloned, expressed inEscherichia 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 andN -methylisocyanuric acid. TheM. thermoacetica enzyme did not require metals or other discernible cofactors for activity. Cyanuric acid hydrolase fromM. thermoacetica is the most promising enzyme to use for cyanuric acid remediation applications.