| Autor: |
Richins RD; Department of Chemical Engineering, University of California, Riverside 92521, USA., Kaneva I, Mulchandani A, Chen W |
| Jazyk: |
angličtina |
| Zdroj: |
Nature biotechnology [Nat Biotechnol] 1997 Oct; Vol. 15 (10), pp. 984-7. |
| DOI: |
10.1038/nbt1097-984 |
| Abstrakt: |
Organophosphorus hydrolase (OPH) was displayed and anchored onto the surface of Escherichia coli using an Lpp-OmpA fusion system. Production of the fusion proteins in membrane fractions was verified by immunoblotting with OmpA antisera. Inclusion of the organophosphorus hydrolase signal sequence was necessary for achieving enzymatic activity on the surface. More than 80% of the OPH activity was located on the cell surface as determined by protease accessibility experiments. Whole cells expressing OPH on the cell surface degraded parathion and paraoxon very effectively without any diffusional limitation, resulting in sevenfold higher rates of parathion degradation compared with whole cells with similar levels of intracellular OPH. Immobilization of these live biocatalysts onto solid supports could provide an attractive means for pesticide detoxification in place of immobilized enzymes, affording a reduced diffusional barrier. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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