Thermostable cyanuric acid hydrolase from Moorella thermoacetica ATCC 39073.

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.

journal_name

Appl Environ Microbiol

authors

Li Q,Seffernick JL,Sadowsky MJ,Wackett LP

doi

10.1128/AEM.01605-09

subject

Has Abstract

pub_date

2009-11-01 00:00:00

pages

6986-91

issue

22

eissn

0099-2240

issn

1098-5336

pii

AEM.01605-09

journal_volume

75

pub_type

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