alexa Abstract | Characterization of Alkyl sulphatase required for the biodegradation of Sodium Dodecyl Sulphate (SDS)

European Journal of Experimental Biology
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The anionic surfactant Sodium Dodecyl Sulphate (SDS), the core components of detergent and cosmetic product formulations contribute significantly to the pollution profile of sewage and wastewaters of all kinds. In this study, 44 SDS degrading strains were isolated by soil enrichment methods and the utilization efficiency was assessed by methylene Blue Active Substances (MBAS) assay and HPLC method. The most efficient isolate was identified as Pseudomonas aeruginosa MTCC 10311 based on phenotypic features and 16 S rDNA typing. The alkyl sulphatase enzyme responsible for the primary degradation of SDS degradation showed enzyme activity 0.0546 U/mg in the crude extract ,which on purification by streptomycin sulphate, dialysis, DEAE cellulose and sephadex G200 gave enzyme units of 3.04 U/mg. The partially purified enzyme could give a maximum SDS degradation of 75% at 4 % of enzyme concentration. Non denaturing PAGE at various stages of purification confirmed that sephadex200 step was particularly effective. The purity of enzyme confirmed by the presence of single band in native PAGE and the molecular mass of the native enzyme was around 77 kDa. Single band was observed in the zymogram of alkyl sulphatase. The optimum pH ,temperature and enzyme concentration of enzyme activity was 7.5,300c and 4%

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Author(s): Ambily P S and M S Jisha


Anionic surfactant, Pseudomonas aeruginosa MTCC 10311, Methylene Blue Active Substances (MBAS) assay, zymogram.

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