Evaluation of phosphate removal from water by immobilized phosphate-binding protein PstS

Kuroda, Akio; KUNIMOTO, HIROKAZU; Morohoshi, Toshio; Ikeda, Tsukasa; Kato, Junichi; Takiguchi, Noboru; Miya, Akiko; Ohtake, Hisao

doi:10.1016/s1389-1723(00)90020-3

Cited by 14 publications

(11 citation statements)

References 9 publications

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“…However, a maximum of only 1.4–2% of the adsorbed P i was recovered after exposing the recombinant E. coli cells to low pH (pH 3.8), high temperature (35 °C), or high ionic strength (100 mM KCl) for 3 h (Yang et al., 2016). On the other hand, Kuroda et al. (2000) reported >90% recovery of the adsorbed P i from PBP immobilized on Sepharose beads at pH 3.…”

Section: Introductionmentioning

confidence: 97%

“…(2000) reported >90% recovery of the adsorbed P i from PBP immobilized on Sepharose beads at pH 3. Although the data was not shown, Kuroda et al. (2000) stated that the immobilized PBP could be reused after neutralizing the pH.…”

Section: Introductionmentioning

confidence: 99%

“…The Pst protein complex comprises four subunits, an ATP-binding protein (pstB), two transmembrane proteins (pstA and pstC), and a periplasmic PBP (pstS) (Luecke and Quiocho, 1990; Santos-Beneit et al., 2008). The periplasmic pstS PBP has recently attracted interest as a potential high-affinity, phosphate-specific P i adsorbent (Kuroda et al., 2000; Li et al., 2009; Yang et al., 2016, 2017).…”

Section: Introductionmentioning

confidence: 99%

“…Removal of P i to ultra-low concentrations has been demonstrated using PBP expressed in bacterial cells' periplasmic space, expressed on the cells' surface, or immobilized on Sepharose beads (Choi et al., 2013; Kuroda et al., 2000; Li et al., 2009; Yang et al., 2016). For example, Choi et al.…”

Section: Introductionmentioning

confidence: 99%

“…(2013) showed that recombinant E. coli expressing PBP in the periplasmic space can remove ≥97% P i from water within 6 h (initial concentration of 0.2–0.5 mg-P i /L). Kuroda et al. (2000) demonstrated P i removal to below the detection limit (9.5 ng-P i /L) using PBP immobilized on Sepharose beads to treat an influent concentration of 15 μg-P i /L.…”

Section: Introductionmentioning

confidence: 99%

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Phosphate removal and recovery using immobilized phosphate binding proteins

et al. 2018

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Progress towards a more circular phosphorus economy necessitates development of innovative water treatment systems which can reversibly remove inorganic phosphate (P i ) to ultra-low levels (<100 μg L −1 ), and subsequently recover the P i for reuse. In this study, a novel approach using the high-affinity E. coli phosphate binding protein (PBP) as a reusable P i bio-adsorbent was investigated. PBP was expressed, extracted, purified and immobilized on NHS-activated Sepharose beads. The resultant PBP beads were saturated with P i and exposed to varying pH (pH 4.7 to 12.5) and temperatures (25–45 °C) to induce P i release. Increase in temperature from 25 to 45 °C and pH conditions between 4.7 and 8.5 released less than 20% of adsorbed P i . However, 62% and 86% of the adsorbed P i was released at pH 11.4 and 12.5, respectively. Kinetic experiments showed that P i desorption occurred nearly instantaneously (<5 min), regardless of pH conditions, which is advantageous for P i recovery. Additionally, no loss in P i adsorption or desorption capacity was observed when the PBP beads were exposed to 10 repeated cycles of adsorption/desorption using neutral and high pH (≥12.5) washes, respectively. The highest average P i adsorption using the PBP beads was 83 ± 5%, with 89 ± 4.1% average desorption using pH 12.5 washes over 10 wash cycles at room temperature. Thermal shift assay of the PBP showed that the protein was structurally stable after 10 cycles, with statistically similar melting temperatures between pH 4 and 12.5. These results indicate that immobilized high-affinity PBP has the potential to be an effective and reversible bio-adsorbent suitable for P i recovery from water/wastewater.

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Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Phosphate removal and recovery using immobilized phosphate binding proteins

et al. 2018

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Biological Removal of Phosphate at Low Concentrations Using Recombinant Escherichia coli Expressing Phosphate-Binding Protein in Periplasmic Space

Choi

Lee

et al. 2013

Appl Biochem Biotechnol

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During wastewater treatment, phosphate removal is an important and challenging process; thus, diverse technologies, including those derived from biological means, have been devised for efficient phosphate removal. Although conventional biological methods are effective in decreasing wastewater phosphate levels to ~1 mg/L, long periods of microbial adaptation are required for effective phosphate removal, and the removal efficiency of these methods is relatively poor at lower phosphate concentrations. In the present work, we constructed a recombinant Escherichia coli with periplasmic-expressed phosphate-binding protein (PBP) and investigated its biological removal ability for low phosphate levels. We found that the PBP-expressing recombinant E. coli cells showed efficient (> 94 %) removal of phosphate at low concentrations (0.2-1.0 mg/L) in a treated cell mass-dependent manner. Collectively, we propose that our PBP-expressing recombinant whole-cell system could be successfully used during wastewater treatment for the biological removal of low concentrations of phosphate.

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Fixed-bed column study of phosphate adsorption using immobilized phosphate-binding protein

Hussein

Mayer

2022

Chemosphere

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Evaluation of phosphate removal from water by immobilized phosphate-binding protein PstS

Cited by 14 publications

References 9 publications

Phosphate removal and recovery using immobilized phosphate binding proteins

Phosphate removal and recovery using immobilized phosphate binding proteins

Biological Removal of Phosphate at Low Concentrations Using Recombinant Escherichia coli Expressing Phosphate-Binding Protein in Periplasmic Space

Fixed-bed column study of phosphate adsorption using immobilized phosphate-binding protein

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