Plasmid-encoded enzymatic degradation of dimethoate

Abstract

Dimethoate-degrading enzymatic activity in Bacillus licheniformis, Pseudomonas aeruginosa, Aeromonas hydrophila, Proteus mirabilis and Bacillus pumilus was found to be 6.4, 1.760, 4.09, 1.196 and 0.505 units/mg protein, respectively. The Escherichia coli C600 transconjugants of the isolated bacterial strains also exhibited dimethoate-degrading enzymatic activities. The cured derivatives did not show any decrease in the amount of dimethoate substrate and did not harbour plasmid as found in the original and transconjugant strains. Thus, the ability of enzymatic degradation of dimethoate was plasmidmediated in B. licheniformis, Ps. aeruginosa, A. hydrophila, P. mirabilis and B. pumilus.