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Immobilized Soybean Peroxidase Hybrid Biocatalysts for Efficient Degradation of Various Emerging Pollutants.

ABSTRACT: In the present study, soybean peroxidase (SBP) was covalently immobilized onto two functionalized photocatalytic supports (TiO₂ and ZnO) to create novel hybrid biocatalysts (TiO₂-SBP and ZnO-SBP). Immobilization caused a slight shift in the pH optima of SBP activity (pH 5.0 to 4.0), whereas the free and TiO₂-immobilized SBP showed similar thermal stability profiles. The newly developed hybrid biocatalysts were used for the degradation of 21 emerging pollutants in the presence and absence of 1-hydroxy benzotriazole (HOBT) as a redox mediator. Notably, all the tested pollutants were not equally degraded by the SBP treatment and some of the tested pollutants were either partially degraded or appeared to be recalcitrant to enzymatic degradation. The presence of HOBT enhanced the degradation of the pollutants, while it also inhibited the degradation of some contaminants. Interestingly, TiO₂ and ZnO-immobilized SBP displayed better degradation efficiency of a few emerging pollutants than the free enzyme. Furthermore, a combined enzyme-chemical oxidation remediation strategy was employed to degrade two recalcitrant pollutants, which suggest a novel application of these novel hybrid peroxidase-photocatalysts. Lastly, the reusability profile indicated that the TiO₂-SBP hybrid biocatalyst retained up to 95% degradation efficiency of a model pollutant (2-mercaptobenzothiazole) after four consecutive degradation cycles.

SUBMITTER: Morsi R

PROVIDER: S-EPMC8235338 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:In this study, we immobilized pectinase preparation on porous zeolite ZSM-5 as an enzyme carrier. We realized this immobilized enzyme catalyst, pectinase preparation@ZSM-5, via a simple combined strategy involving the van der Waals adsorption of pectinase preparation followed by crosslinking of the adsorbed pectinase preparation with glutaraldehyde over ZSM-5. Conformal pectinase preparation coverage of various ZSM-5 supports was achieved for the as-prepared pectinase preparation@ZSM-5. The porous pectinase preparation@ZSM-5 catalyst exhibited ultra-efficient biocatalytic activity for hydrolyzing the β-glycosidic bonds in the model substrate 4-nitrophenyl β-D-glucopyranoside, with a broad operating temperature range, high thermal stability, and excellent reusability. The relative activity of pectinase preparation@ZSM-5 at a high temperature (70 °C) was nine times higher than that of free pectinase preparation. Using thermal inactivation kinetic analysis based on the Arrhenius law, pectinase preparation@ZSM-5 showed higher activation energy for denaturation (315 kJ mol-1) and a longer half-life (62 min-1) than free pectinase preparation. Moreover, a Michaelis-Menten enzyme kinetic analysis indicated a higher maximal reaction velocity for pectinase preparation@ZSM-5 (0.22 µmol mg-1 min-1). This enhanced reactivity was attributed to the microstructure of the immobilized pectinase preparation@ZSM-5, which offered a heterogeneous reaction system that decreased the substrate-pectinase preparation binding affinity and modulated the kinetic characteristics of the enzyme. Additionally, pectinase preparation@ZSM-5 showed the best ethanol tolerance among all the reported pectinase preparation-immobilized catalysts, and an activity 247% higher than that of free pectinase preparation at a 10% (v/v) ethanol concentration was measured. Furthermore, pectinase preparation@ZSM-5 exhibited potential for practical engineering applications, promoting the hydrolysis of β-glycosidic bonds in baicalin to convert it into baicalein. This was achieved with a 98% conversion rate, i.e., 320% higher than that of the free enzyme.

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Immobilized Soybean Peroxidase Hybrid Biocatalysts for Efficient Degradation of Various Emerging Pollutants.

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