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| Natura: | Artículo científico |
| Lingua: | en |
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World journal of microbiology & biotechnology
2025
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| Accesso online: | https://pubmed.ncbi.nlm.nih.gov/39948259/ |
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| author | Lisintta, E S George, Annie Gafoor, Sona Vishnupriya, S Yousuf, Jesmi Kachiprath, Bhavya Valsa, A K Antony, Ally C Aneesa, P A Hatha, A A Mohamed |
| author_facet | Lisintta, E S George, Annie Gafoor, Sona Vishnupriya, S Yousuf, Jesmi Kachiprath, Bhavya Valsa, A K Antony, Ally C Aneesa, P A Hatha, A A Mohamed Lisintta, E S George, Annie Gafoor, Sona Vishnupriya, S Yousuf, Jesmi Kachiprath, Bhavya Valsa, A K Antony, Ally C Aneesa, P A Hatha, A A Mohamed |
| collection | PubMed - marine biology |
| contents | A psychrotolerant extracellular phosphatase from Krossfjorden sediment bacterium Bacillus cereus KR_O9: purification and functional characterization. Lisintta, E S George, Annie Gafoor, Sona Vishnupriya, S Yousuf, Jesmi Kachiprath, Bhavya Valsa, A K Antony, Ally C Aneesa, P A Hatha, A A Mohamed Bacillus cereus Geologic Sediments Hydrogen-Ion Concentration Enzyme Stability Kinetics Phosphoric Monoester Hydrolases Molecular Weight Temperature Substrate Specificity Arctic Regions Metals, Heavy Bacterial Proteins Phylogeny Metals RNA, Ribosomal, 16S This study reports the identification of a phosphatase-producing psychrotolerant bacterium, Bacillus cereus KR_O9, isolated from Arctic Krossfjorden sediments. The extracellular KR_O9 phosphatase was purified to homogeneity through acetone precipitation and ion exchange chromatography, achieving a specific activity of 12.51 U mg⁻ min⁻, a 17.3-fold purification, and a 64.94% yield. The molecular mass of the enzyme was estimated as 37 kDa by SDS-PAGE. K, and V for KR_O9 phosphatase towards substrate p-NPP were determined as 0.033 M L, 1.67 mg min. The enzyme exhibited optimal activity at 40 °C and pH 6.0, with stability up to ≤ 40 °C and at pH levels ≤ 7.0, highlighting its thermolability and sensitivity to alkaline pH. At 10 mM level, Cu, Hg, Co, Pb, urea, EDTA, and GSH significantly stimulated the enzyme, and Ca, Zn, Mn, SDS, and CTAB were, strong inhibitors. The kinetic efficiency, resilience to low to neutral pH, and tolerance to various metal ions, including heavy metals, underscore the potential of B. cereus KR_O9 phosphatase for bioremediation and biofertilizer applications, paving the way for industrial exploration. |
| format | Artículo científico |
| id | pubmed_39948259 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | World journal of microbiology & biotechnology |
| record_format | pubmed |
| spellingShingle | A psychrotolerant extracellular phosphatase from Krossfjorden sediment bacterium Bacillus cereus KR_O9: purification and functional characterization. Lisintta, E S George, Annie Gafoor, Sona Vishnupriya, S Yousuf, Jesmi Kachiprath, Bhavya Valsa, A K Antony, Ally C Aneesa, P A Hatha, A A Mohamed Bacillus cereus Geologic Sediments Hydrogen-Ion Concentration Enzyme Stability Kinetics Phosphoric Monoester Hydrolases Molecular Weight Temperature Substrate Specificity Arctic Regions Metals, Heavy Bacterial Proteins Phylogeny Metals RNA, Ribosomal, 16S A psychrotolerant extracellular phosphatase from Krossfjorden sediment bacterium Bacillus cereus KR_O9: purification and functional characterization. Lisintta, E S George, Annie Gafoor, Sona Vishnupriya, S Yousuf, Jesmi Kachiprath, Bhavya Valsa, A K Antony, Ally C Aneesa, P A Hatha, A A Mohamed Bacillus cereus Geologic Sediments Hydrogen-Ion Concentration Enzyme Stability Kinetics Phosphoric Monoester Hydrolases Molecular Weight Temperature Substrate Specificity Arctic Regions Metals, Heavy Bacterial Proteins Phylogeny Metals RNA, Ribosomal, 16S This study reports the identification of a phosphatase-producing psychrotolerant bacterium, Bacillus cereus KR_O9, isolated from Arctic Krossfjorden sediments. The extracellular KR_O9 phosphatase was purified to homogeneity through acetone precipitation and ion exchange chromatography, achieving a specific activity of 12.51 U mg⁻ min⁻, a 17.3-fold purification, and a 64.94% yield. The molecular mass of the enzyme was estimated as 37 kDa by SDS-PAGE. K, and V for KR_O9 phosphatase towards substrate p-NPP were determined as 0.033 M L, 1.67 mg min. The enzyme exhibited optimal activity at 40 °C and pH 6.0, with stability up to ≤ 40 °C and at pH levels ≤ 7.0, highlighting its thermolability and sensitivity to alkaline pH. At 10 mM level, Cu, Hg, Co, Pb, urea, EDTA, and GSH significantly stimulated the enzyme, and Ca, Zn, Mn, SDS, and CTAB were, strong inhibitors. The kinetic efficiency, resilience to low to neutral pH, and tolerance to various metal ions, including heavy metals, underscore the potential of B. cereus KR_O9 phosphatase for bioremediation and biofertilizer applications, paving the way for industrial exploration. |
| title | A psychrotolerant extracellular phosphatase from Krossfjorden sediment bacterium Bacillus cereus KR_O9: purification and functional characterization. |
| topic | Bacillus cereus Geologic Sediments Hydrogen-Ion Concentration Enzyme Stability Kinetics Phosphoric Monoester Hydrolases Molecular Weight Temperature Substrate Specificity Arctic Regions Metals, Heavy Bacterial Proteins Phylogeny Metals RNA, Ribosomal, 16S |
| url | https://pubmed.ncbi.nlm.nih.gov/39948259/ |