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Isolation and characterization of a recombinant class C acid phosphatase from Sphingobium sp. RSMS strain

Tributyl phosphate (TBP) is extensively used in nuclear industry and is a major environmental pollutant. The mechanism for TBP degradation is not identified in any TBP-degrading bacteria. Here, we report identification of an acid phosphatase from Sphingobium sp. RSMS (Aps) that exhibits high specifi...

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Detalles Bibliográficos
Autores principales: Rangu, Shyam Sunder, Singh, Rahul, Gaur, Neeraj Kailash, Rath, Devashish, Makde, Ravindra D., Mukhopadhyaya, Rita
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8857453/
https://www.ncbi.nlm.nih.gov/pubmed/35242619
http://dx.doi.org/10.1016/j.btre.2022.e00709
Descripción
Sumario:Tributyl phosphate (TBP) is extensively used in nuclear industry and is a major environmental pollutant. The mechanism for TBP degradation is not identified in any TBP-degrading bacteria. Here, we report identification of an acid phosphatase from Sphingobium sp. RSMS (Aps) that exhibits high specific activity towards monobutyl phosphate (MBP) and could be a terminal component of the TBP degradation process. A genomic DNA library of the bacteria was screened using a histochemical method which yielded 35 phosphatase clones. Among these, the clone that showed the highest MBP degradation was studied further. DNA sequence analysis showed that the genomic insert encodes a protein (Aps) which belongs to class C acid phosphatase. The recombinant Aps was found to be a dimer and hydrolysed MBP with a K(cat) 68.1 ± 5.46 s(−)(1) and K(m) 2.5 mM ± 0.50. The protein was found to be nonspecific for phosphatase activity and hydrolyzed disparate organophosphates.