In this research the genes (amoA and hao) for ammonia monooxygenase (AMO) and hydroxylamine oxidoreductase (HAO) responsible for ammonia oxidation reaction in completely autotrophic nitrogen removal over nitrite process were cloned and sequenced, and the recombinant protein of AMO and HAO was expressed and characterized. The optimum temperature for AMO activity was 55 degrees C and more than 40% of the maximum activity was retained from 15-50 degrees C. The optimum pH for the enzyme was found to be pH 11.0. The highest activity for HAO was observed at 45 degrees C. More than 50% of the maximum activity was retained even at 55 degrees C. The dependence of HAO on pH was strong and only average 15% of residual activity left at pH ranging from 3.0-9.0. Study on the molecular and biochemistry properties of recombinant AMO and HAO will benefit for the manipulation of ammonia-oxidizing bacteria to achieve the goal of high efficiency of nitrogen removal.
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