Application of immobilized horseradish peroxidase onto modified acrylonitrile copolymer membrane in removing of phenol from water

Vasileva, N.; Godjevargova, Tzonka; Ivanova, D.; Gabrovska, Katya

doi:10.1016/j.ijbiomac.2008.12.002

Cited by 53 publications

(18 citation statements)

References 20 publications

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“…So, horseradish peroxidase membrane, as a membrane bioreactor, would be a promising method for efficient, continuous, and safe treatment of phenolic effluents. Although Leirião and Vasileva briefly investigated HRP‐catalyzed membranes for removing phenol from water, their study did not achieve a satisfactory degree of phenol removal, especially for the higher concentrations.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of horseradish peroxidase on modified PAN‐based membranes for the removal of phenol from buffer solutions

Wang

Liu

Zheng³

et al. 2016

Can J Chem Eng

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Polyacrylonitrile ultrafiltration membranes have been widely used in many separation processes. In this paper, horseradish peroxidase was immobilized onto polyacrylonitrile ultrafiltration membrane by crosslinking with glutaraldehyde. The immobilized enzyme possessed a protein loading of 0.025 mg/cm2membrane and a specific activity of 105 U/mgprotein (105 μmol/min/mgprotein). The initial modified and immobilized membranes were observed using SEM and FTIR. Potential applications of HRP membranes were investigated in the removal of phenol through oxidation with the addition of hydrogen peroxide. The optimum pH of the immobilized enzyme was determined to be 6.0, and the optimum hydrogen peroxide concentration to be 30 mmol/L. Almost 100 % removal of phenol (1 ∼ 10 mg/L) from water was achieved by HRP membranes. For high concentrated solutions, successive cycles were successfully used to improve the degree of phenol oxidation. Furthermore, the immobilized horseradish peroxidase was operationally stable. These results suggest that the HRP membrane has promising applications for the removal of phenol.

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Section: Introductionmentioning

confidence: 99%

Immobilization of horseradish peroxidase on modified PAN‐based membranes for the removal of phenol from buffer solutions

Wang

Liu

Zheng³

et al. 2016

Can J Chem Eng

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“…[41]), wastewater cleanup systems ( e.g. [42]) and antibody-directed enzyme-prodrug cancer therapy ( e.g. [43]), it is highly interesting to biochemically characterize the different HRP isoenzymes to find the most suitable one for a certain application.…”

Section: Introductionmentioning

confidence: 99%

Purification and basic biochemical characterization of 19 recombinant plant peroxidase isoenzymes produced in Pichia pastoris

Krainer

Pletzenauer

Rossetti

et al. 2014

Protein Expression and Purification

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“…In particular, enzymes involved in catabolic reactions have a huge potential in the remediation of soils, sediments, or wastewater from pollutants . The use of purified enzymes for bioremediation can be significantly enhanced if coupled with immobilization techniques . Immobilization usually results in the possibility of reuse and produces an increase in protein stability and in situ persistence .…”

Section: Introductionmentioning

confidence: 99%

Ormosil gels doped with engineered catechol 1,2 dioxygenases for chlorocatechol bioremediation

Micalella

Caglio

Mozzarelli

et al. 2014

Biotech and App Biochem

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Enzymes entrapped in wet, nanoporous silica gel have great potential as bioreactors for bioremediation because of their improved thermal, chemical, and mechanical stability with respect to enzymes in solution. The B isozyme of catechol 1,2 dioxygenase from Acinetobacter radioresistens and its mutants of Leu69 and Ala72, designed for an increased reactivity toward the environmental pollutant chlorocatechols, were encapsulated using alkoxysilanes and alkyl alkoxysilanes as precursors in varying proportions. Encapsulation of the mutants in a hydrophobic tetramethoxysilane/dimethoxydimethylsilane-based matrix yielded a remarkable 10- to 12-fold enhancement in reactivity toward chlorocatechols. These gels also showed a fivefold increase in relative reactivity toward chlorocatechols with respect to the natural substrate catechol, thus compensating for their relatively low activity for these substrates in solution. The encapsulated enzyme, unlike the enzyme in solution, proved resilient in assays carried out in urban wastewater and bacteria-contaminated solutions mimicking environmentally relevant conditions. Overall, the combination of a structure-based rational design of enzyme mutants, and the selection of a suitable encapsulation material, proved to be a powerful approach for the production and optimization of a potential bioremediation device, with increased activity and resistance toward bacterial degradation.

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Application of immobilized horseradish peroxidase onto modified acrylonitrile copolymer membrane in removing of phenol from water

Cited by 53 publications

References 20 publications

Immobilization of horseradish peroxidase on modified PAN‐based membranes for the removal of phenol from buffer solutions

Immobilization of horseradish peroxidase on modified PAN‐based membranes for the removal of phenol from buffer solutions

Purification and basic biochemical characterization of 19 recombinant plant peroxidase isoenzymes produced in Pichia pastoris

Ormosil gels doped with engineered catechol 1,2 dioxygenases for chlorocatechol bioremediation

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