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Achromobacter denitrificans SP1 produces pharmaceutically active 25C prodigiosin upon utilizing hazardous di(2-ethylhexyl)phthalate

[Display omitted] •A novel therapeutically significant prodigiosin from A. denitrificans SP1 demonstrated.•A.denitrificans SP1 produced 25C prodigiosin in situ and ex situ.•Characterized an unusual 25C prodigiosin analog with a 5C extension on the typical 20C prodigiosin.•Hazardous DEHP bioremediate...

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Bibliographic Details
Published in:Bioresource technology 2014-11, Vol.171, p.482-486
Main Authors: Pradeep, S., Sarath Josh, M.K., Balachandran, S., Sudha Devi, R., Sadasivam, R., Thirugnanam, P.E., Doble, Mukesh, Anderson, Robin C., Benjamin, Sailas
Format: Article
Language:English
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Summary:[Display omitted] •A novel therapeutically significant prodigiosin from A. denitrificans SP1 demonstrated.•A.denitrificans SP1 produced 25C prodigiosin in situ and ex situ.•Characterized an unusual 25C prodigiosin analog with a 5C extension on the typical 20C prodigiosin.•Hazardous DEHP bioremediated into a pharmaceutically significant drug.•In silico studies showed activation of Jak 3, Zap 70 kinases. This first report describes the purification and identification of an orange-red pigment produced by Achromobacter denitrificans strain SP1 (isolated from sewage sludge heavily contaminated with plastics) during its growth in a simple basal salt medium supplemented with the hazardous di(2-ethylhexyl)phthalate (DEHP) blended in PVC blood bag (in situ) or free DEHP (ex situ) as carbon source. The cell-bound pigment was elucidated, characterized at molecular level, and described as an unusual 25C prodigiosin analog for the first time. At laboratory conditions (in flasks), the dry cell mass was 75.2mg/g blood bag, which upon extraction yielded 7.1mg prodigiosin; at this stage the pH of the medium was dropped from 7.2 to 3.5. Considering its pharmaceutical importance, taking 10 known prodigiosins as controls, this 25C prodigiosin was subjected to molecular docking studies, showed comparable and promising binding efficiencies with the crucial molecular human targets like cycloxygenase-2, ZAP-70 kinase and Jak-3 kinase.
ISSN:0960-8524
1873-2976
DOI:10.1016/j.biortech.2014.08.077