Abstract
Aldrin used in agricultural as well as industrial or home pest control is known to be a persistent organic pollutant, having chronic adverse effects on wildlife and humans. The degradation of aldrin has drawn a lot of attentions. In this study, house fly cytochrome P450 6A1 (CYP 6A1) or both house fly cytochrome P450 6A1 and human NADPH-P450 reductase (CPR) together was expressed in Escherichia coli cells to study their activity on aldrin conversion. It was found out that the membrane fractions prepared from the recombinant E. coli cells expressing human CPR with CYP 6A1 have catalytic activity on aldrin using enzyme analysis. The catalytic activity of the recombinant E. coli cells was also investigated on aldrin. After adding aldrin to the co-expression of human CPR and CYP 6A1 recombinant E. coli cells culture with 1 µmol L-1 final concentration, 163.36 nmol L-1 of dieldrin was detected after 8 h, the product of aldrin epoxidation. These results indicate that co-expressing house fly CYP 6A1 and human CPR can convert aldrin to dieldrin. Key words: Aldrin, bioconversion, cytochrome P450 6A1, cytochrome P450 reductase, dieldrin.
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