Abstract
A Pseudomonas putida strain, named ER1, was isolated from an agricultural soil and found to actively degrade the herbicide butachlor. The enzyme extracted from ER1 could degrade butachlor. Furthermore, incubation of ER1 in a medium containing 50 mg/kg of butachlor after 3 days resulted in the high butachlor-degrading enzyme activity of ER1. Response of ER1 to butachlor might be related to changes in protein composition at both quantitative and qualitative levels. Total proteins were extracted from control strain (incubated in the medium without butachlor) and the treated strain (incubated in the medium with butachlor). The proteins were separated by two-dimensional gel electrophoresis. Of the total number of ER1 protein, 11 spots were significantly changed under butachlor stress. Analysis by matrix-assisted laser desorption/ionization mass spectrometry and tandem mass spectrometry coupled with database searching allowed the function of some proteins which were similar to the hydrolases activity or oxidoreductase activity.
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