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Evaluation of p-cresol degradation with polyphenol oxidase (PPO) immobilized in various matrices.

ABSTRACT: p-Cresol is an environmental pollutant due to its vast use, toxicity and persistence, nevertheless, its degradation in an enzyme is unclear. In this study, we used Pleurotus sp. isolate VLECK02 polyphenol oxidase (PPO) for the determination of p-cresol degradation. On the basis of UV, FT-IR and chromatographic (HPLC and GC-MS) analysis, 4-methylcatechol was identified as the main metabolite of p-cresol catabolism. In addition, batch and semi-continuous degradation of p-cresol (10 and 20 mM) were studied and compared by free and immobilized PPO in different matrices like sodium alginate (SA), sodium alginate-polyvinyl alcohol (SA-PVA) and sodium alginate-polyvinyl alcohol-silver nanoparticles (SA-PVA-AgNPs). The experimental data showed that an enzyme (PPO) immobilized in SA-PVA-AgNPs was completely degraded p-cresol at initial concentrations of 10 and 20 mM within 30 h. These results suggest that the enzyme immobilized in SA-PVA-AgNPs has achieved higher degradation rates at a given time than free PPO and PPO immobilized in SA-PVA and SA. The SA-PVA-AgNPs and SA-PVA immobilized enzyme could be reused for more than 12 and 8 cycles, respectively, without losing any degradation capacity. Moreover, the immobilized PPO showed higher tolerance to various temperatures and pH than free PPO. Hence, immobilized PPO could be useful for the bioremediation of environment contaminated with phenolic compounds like p-cresol.

SUBMITTER: Edalli VA

PROVIDER: S-EPMC5082039 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

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Evaluation of p-cresol degradation with polyphenol oxidase (PPO) immobilized in various matrices.

Edalli Vijayalakshmi A VA Mulla Sikandar I SI Eqani Syed Ali Musstjab Akber Shah SA Mahadevan Gurumurthy D GD Sharma Rohit R Shouche Yogesh Y Kamanavalli Chandrappa M CM

3 Biotech 20161026 2

p-Cresol is an environmental pollutant due to its vast use, toxicity and persistence, nevertheless, its degradation in an enzyme is unclear. In this study, we used Pleurotus sp. isolate VLECK02 polyphenol oxidase (PPO) for the determination of p-cresol degradation. On the basis of UV, FT-IR and chromatographic (HPLC and GC-MS) analysis, 4-methylcatechol was identified as the main metabolite of p-cresol catabolism. In addition, batch and semi-continuous degradation of p-cresol (10 and 20 mM) were ...[more]

PMID: 28330301

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Project description:In this study, a polydopamine (PDA)-modified hollow fiber-immobilized xanthine oxidase (XOD) was prepared for screening potential XOD inhibitors from flavonoids. Several parameters for the preparation of PDA-modified hollow fiber-immobilized XOD, including the dopamine concentration, modification time, XOD concentration and immobilization time, were optimized. The results show that the optimal conditions for immobilized XOD activity were a dopamine concentration of 2.0 mg/mL in 10.0 mM Tris-HCl buffer (pH 8.5), a modification time of 3.0 h, an XOD concentration of 1000 μg/mL in 10.0 mM phosphate buffer (pH 7.5) and an immobilization time of 3.0 h. Subsequently, the enzymatic reaction conditions such as the pH value and temperature were investigated, and the enzyme kinetics and inhibition parameters were determined. The results indicate that the optimal pH value (7.5) and temperature (37 °C) of the PDA-modified hollow fiber-immobilized XOD were consistent with the free enzyme. Moreover, the PDA-modified hollow fiber-immobilized XOD could still maintain above 50% of its initial immobilized enzyme activity after seven consecutive cycles. The Michaelis-Menten constant (Km) and the half-maximal inhibitory concentration (IC50) of allopurinol on the immobilized XOD were determined as 0.25 mM and 23.2 μM, respectively. Furthermore, the PDA-modified hollow fiber-immobilized XOD was successfully applied to evaluate the inhibitory activity of eight flavonoids. Quercetin, apigenin, puerarin and epigallocatechin showed a good inhibition effect, and their percentages of inhibition were (79.86 ± 3.50)%, (80.98 ± 0.64)%, (61.15 ± 6.26)% and (54.92 ± 0.41)%, respectively. Finally, molecular docking analysis further verified that these four active compounds could bind to the amino acid residues in the XOD active site. In summary, the PDA-modified hollow fiber-immobilized XOD is an efficient method for the primary screening of XOD inhibitors from natural products.

Dataset Information

Evaluation of p-cresol degradation with polyphenol oxidase (PPO) immobilized in various matrices.

Publications

Evaluation of p-cresol degradation with polyphenol oxidase (PPO) immobilized in various matrices.

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