Enzyme Technology of Peroxidases: Immobilization, Chemical and Genetic Modification

Longoria, Adriana; Tinoco, Raunel; Torres, Eduardo

doi:10.1007/978-3-642-12627-7_9

Cited by 7 publications

(9 citation statements)

References 122 publications

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“…However, immobilization methods generally induce conformational changes in the enzymatic structure that can result in a lower catalytic efficiency. In the case of peroxidases, the balance between the gain in stability and reuse and the loss of activity is generally positive and allowed to use these systems in different biotechnological applications (Longoria et al 2010;Husain 2010).…”

Section: Introductionmentioning

confidence: 99%

Degradation of orange dyes and carbamazepine by soybean peroxidase immobilized on silica monoliths and titanium dioxide

Calza

Zacchigna

Laurenti

2016

Environ Sci Pollut Res

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In this paper, the removal of three common dyes (orange I, orange II, and methylorange) and of the anticonvulsant drug carbamazepine from aqueous solutions by means of enzymatic and photocatalytic treatment was studied. Soybean peroxidase (SBP) was used as biocatalyst, both free in solution and immobilized on silica monoliths, and titanium dioxide as photocatalyst. The combination of the two catalysts led to a faster (about two to four times) removal of all the orange dyes compared to the single systems. All the dyes were completely removed within 2 h, also in the presence of immobilized SBP. As for carbamazepine, photocatalytic treatment prevails on the enzymatic degradation, but the synergistic effect of two catalysts led to a more efficient degradation; carbamazepine's complete disappearance was achieved within 60 min with combined system, while up to 2 h is required with TiO only.

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Section: Introductionmentioning

confidence: 99%

Degradation of orange dyes and carbamazepine by soybean peroxidase immobilized on silica monoliths and titanium dioxide

Calza

Zacchigna

Laurenti

2016

Environ Sci Pollut Res

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“…Under these conditions, the protein load increased with reaction time, achieving a maximum after 17-20 h of reaction. The resultant biocatalyst with a specific activity of 18,000 U/g may be compared with the best results presented in the literature [35]. However, we noticed enzyme leaching upon incubation in buffer pH 6 at room temperature, with a 50% desorption after 2 h and 80% desorption after 5 h (Fig.…”

Section: Immobilization Of Cpo Through Tyrosine Residuesmentioning

confidence: 69%

Halogenation of β-estradiol by a rationally designed mesoporous biocatalyst based on chloroperoxidase

Salcedo¹,

Torres

Haces

et al. 2015

Biocatalysis

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Chloroperoxidase fromCaldariomyces fumago was immobilized in Eupergit ® C, a commercial mesoporous acrylic-based material. Due to low stability of the enzyme under neutral and basic pH, the usual covalent immobilization procedures cannot be applied to this enzyme. Several strategies were followed in order to achieve a stable interaction between the protein and the support. The support was efficiently functionalized with different reactive groups such as aromatic and aliphatic amines, glutaraldehyde, diazonium ions, and maleimide moieties; solvent-exposed amino acid residues in chloroperoxidase were identified or created through chemical modification, so that they were reactive under conditions where the enzyme is stable. Enzyme load and retained activity were monitored, obtaining biocatalysts with specific activity ranging from 200 to 25,000 U/g. The highest load and activity was obtained from the immobilization of a chemically-modified CPO preparation bearing a solvent-exposed free thiol group. This biocatalyst efficiently catalyzed the transformation of β-estradiol, an endocrine disruptor.

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“…The application of enzymes in environmental treatment is becoming a promising technology due to the managed reaction conditions such as low energy demand, zero sludge generation, high pollutant conversion percentages, and low product toxicity of the reaction. Some enzymes have been applied in biocatalytic formulations immobilized in membranes and tested in reactors under real conditions found in WWTP with promising results (Longoria et al 2010, Touahar et al 2014. Peroxidases and laccases have been proposed and tested against an important battery of microcontaminants, resulting in oxidized compounds with higher biodegradability.…”

Section: Discussionmentioning

confidence: 99%

Oxidation of sulfonamide micropollutants by versatile peroxidase from Bjerkandera adusta

Bairán¹,

Chávez²,

Ortiz‐Álvarez³

et al. 2022

Rev. Int. Contam. Ambie.

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The oxidation of five sulfonamide antibiotics by the versatile peroxidase (VP, EC. 1.11.1.16) from Bjerkandera adusta was quantitatively assessed. The biocatalytic activity of the enzyme was studied by assaying different reaction conditions. Conversion levels were higher than 90 % for all five sulfonamide antibiotics in the model reaction system. In addition, the enzyme performance was also studied in treated wastewater effluents, where three sulfonamide antibiotics were oxidized at a higher level (greater than 85 % oxidation) and two were oxidized at a lower level (up to 50 %). The identified reaction products for two antibiotics, sulfasalazine, and sulfamethoxazole, showed higher antimicrobial activity than the parental compounds. Docking analyses exhibited that the reaction products interacted with the catalytic pocket of the dihydropteroate synthase from Escherichia coli, similar to the parental antibiotics. Though the oxidation is carried out at high velocity and conversion rates, the application of VP in the enzymatic oxidation technology of sulfonamide antibiotics must overcome the production of more toxic products.

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Enzyme Technology of Peroxidases: Immobilization, Chemical and Genetic Modification

Cited by 7 publications

References 122 publications

Degradation of orange dyes and carbamazepine by soybean peroxidase immobilized on silica monoliths and titanium dioxide

Degradation of orange dyes and carbamazepine by soybean peroxidase immobilized on silica monoliths and titanium dioxide

Halogenation of β-estradiol by a rationally designed mesoporous biocatalyst based on chloroperoxidase

Oxidation of sulfonamide micropollutants by versatile peroxidase from Bjerkandera adusta

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