Veratryl Alcohol Research Articles

Removal of perfluorooctanoic acid (PFOA) in the liquid culture of Phanerochaete chrysosporium

Perfluorooctanoic acid (PFOA) is becoming a concern due to its persistence, bioaccumulation, and potential harmful effects on humans and the environment. In this study, the fungus Phanerochaete chrysosporium (P. chrysosporium) was used to remove the PFOA in liquid culture system. The results showed that the average activities of laccase (Lac), lignin peroxidase (LiP), and manganese peroxidase (MnP) enzymes secreted by P. chrysosporium were 0.0003 U/mL, 0.013 U/mL, and 0.0059 U/mL, respectively, during the incubation times of 0–75 days. The pH of 3 and incubation time of 45–55 days were the optimum parameters for the three enzymes activities. The enzyme activities in P. chrysosporium incubation system were firstly inhibited by adding PFOA and then they were enhanced after 14 days. The maximum removal efficiency of PFOA (69.23%) was achieved after 35 days in P. chrysosporium incubation system with an initial PFOA concentration of 0.002 mM and no veratryl alcohol (VA). Adsorption was not a main pathway for PFOA removal and the PFOA adsorbed in fungi mycelial mat accounted for merely 1.91%. The possible products of PFOA contained partially fluorinated aldehyde, alcohol, and aromatic ring. These partially fluorinated compounds might result from PFOA degradation via a combination of cross-coupling and rearrangement of free radicals.

Green synthesis of silver nanoparticles using sustainable bio-fertilizer (Panchakavyam) for the selective oxidation of propylene glycol and veratryl alcohol

This study demonstrates the selective oxidation of propylene glycol and veratryl alcohol utilizing silver oxide nanoparticles. This work adopted employing Panchakavyam, a medicinally rich bio-fertilizer for synthesizing silver oxide nanoparticles. In the present study, panchakavyam was prepared as a supporting material for the synthesis of silver oxide nanoparticles (Ag2O NPs). The traditional source of panchakavyam makes it cost effective, eco-friendly and the positive alteration of structure and shape of the catalyst enabled to deliver high yield of value added products. The synthesized silver oxide nanoparticle’s structure, shape, reactivity, stability, nature of the catalyst, thermal behaviour were studied and analysed through standard catalyst characterization techniques. Post synthesis of nanoparticles, selective oxidation reaction was carried out by confining the silver oxide nanoparticles as a nano catalyst. The tert-butyl hydroperoxide was chosen as the solvent for the oxidation studies of propylene glycol and veratryl alcohol. This study was performed by varying the reaction parameters such as temperature, pressure, time, WHSV−1 etc., to obtain the maximum yield of most desired product. The study involving conversion of propylene glycol(PG) to hydroxy acetone(HA) showed a conversion and selectivity of 100 and 99%, respectively. Similarly conversion of veratryl alcohol(VAOL) to veratraldehyde(VAL) showed a conversion and selectivity of 100 and 97.8%, respectively. The result of the study provides a path to explore the adoption of sustainable catalyst in the conversion of propylene glycol and veratryl alcohol to an industrially important products.

In Silico Study of Enzymatic Degradation of Bioplastic by Microalgae: An Outlook on Microplastic Environmental Impact Assessment, Challenges, and Opportunities.

Microplastics are tiny pieces of non-biodegradable plastic that can take thousands of years to break down. As microplastics degrade, they release harmful compounds into the environment, which can be found in the surroundings. The microplastics found in the environment are hard to detect and remove because of their small particle sizes. Microplastics cannot decompose naturally, so they accumulate in the environment and cause pollution. As a result, bioplastics can be produced from a vast array of substrates, including biopolymers, citrus peels, leather, and feather wastes. Blue-green microalgae namely Arthrospira platensis (spirulina) contains enzymes such as laccase and catalase which can be responsible for the degradation of bioplastics. In our study, we performed molecular docking to identify the binding affinities of different enzymes such as laccase and catalase with different substrates, focusing on determining the most suitable substrate for enhancing enzyme activity for degradation of bioplastics. The analysis revealed that veratryl alcohol is the most suitable substrate for laccase, whereas lignin is the more preferred substrate for catalase with the highest binding affinity score of -5.9 and -8.1kcal/mol. Moreover, degradation, challenges, opportunities, and applications of bioplastics in numerous domains such as cosmetics, electronics, agriculture, medical, textiles, and food industries have also been highlighted.

Evaluation of a dye-decolorizing peroxidase from Comamonas serinivorans for lignin valorization potentials

Although dye-decolourising peroxidases (DyPs) are well-known for lignin degradation, a comprehensive understanding of their mechanism remains unclear. Therefore, studying the mechanism of lignin degradation by DyPs is necessary for industrial applications and enzyme engineering. In this study, a dye-decolourising peroxidase (CsDyP) gene from C. serinivorans was heterologously expressed and studied for its lignin degradation potential. Molecular docking analysis predicted the binding of 2, 2-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), veratryl alcohol (VA), 2, 6-dimethylphenol (2, 6- DMP), guaiacol (GUA), and lignin to the substrate-binding pocket of CsDyP. Evaluation of the enzymatic properties showed that CsDyP requires pH 4.0 and 30 °C for optimal activity and has a high affinity for ABTS. In addition, CsDyP is stable over a wide range of temperatures and pH and can tolerate 5.0 mM organic solvents. Low NaCl concentrations promoted CsDyP activity. Further, CsDyP significantly reduced the chemical oxygen demand decolourised alkali lignin (AL) and milled wood lignin (MWL). CsDyP targets the β-O-4, CO, and CC bonds linking lignin's G, S, and H units to depolymerize and produce aromatic compounds. Overall, this study delivers valuable insights into the lignin degradation mechanism of CsDyP, which can benefit its industrial applications and lignin valorization.

Exoproteomic Study and Transcriptional Responses of Laccase and Ligninolytic Peroxidase Genes of White-Rot Fungus Trametes hirsuta LE-BIN 072 Grown in the Presence of Monolignol-Related Phenolic Compounds.

Being an abundant renewable source of aromatic compounds, lignin is an important component of future bio-based economy. Currently, biotechnological processing of lignin through low molecular weight compounds is one of the conceptually promising ways for its valorization. To obtain lignin fragments suitable for further inclusion into microbial metabolism, it is proposed to use a ligninolytic system of white-rot fungi, which mainly comprises laccases and peroxidases. However, laccase and peroxidase genes are almost always represented by many non-allelic copies that form multigene families within the genome of white-rot fungi, and the contributions of exact family members to the overall process of lignin degradation has not yet been determined. In this article, the response of the Trametes hirsuta LE-BIN 072 ligninolytic system to the presence of various monolignol-related phenolic compounds (veratryl alcohol, p-coumaric acid, vanillic acid, and syringic acid) in culture media was monitored at the level of gene transcription and protein secretion. By showing which isozymes contribute to the overall functioning of the ligninolytic system of the T. hirsuta LE-BIN 072, the data obtained in this study will greatly contribute to the possible application of this fungus and its ligninolytic enzymes in lignin depolymerization processes.

A copper decorated porphyrin-based porous organic polymer: Evaluation in the oxidation of lignin model compounds

A novel porous organic polymer containing porphyrin units was synthesized and decorated with copper to produce the metallated POP, Cu-TriPOP. The native POP, Nat-TriPOP and metal-decorated Cu-TriPOP exhibited BET surface areas of 595 m2/g and 373 m2/g, respectively. Excellent thermal stability up to 300 °C was observed by thermogravimetric analysis. Transmission electron microscopy (TEM) showed a sea urchin/bush-like morphology. The metal-decorated POP, Cu-TriPOP, was evaluated in the oxidation of veratryl alcohol and other related substrates. Excellent catalytic performance was achieved with conversions of around 80%. The addition of ascorbic acid, a well-known radical scavenger, significantly reduced the activity, suggesting that a radical mechanism is most likely operative. In addition, excellent catalyst recovery and recyclability were achieved for up to five cycles with minimal decrease in activity.

Isolation and Characterization of Potential Lignin Peroxidase-Producing Bacteria from Compost Samples at Richards Bay (South Africa).

Lignin recalcitrance is a key issue in producing value-added products from lignocellulose biomass. In situ biodegradable lignin-modifying enzymes-producing bacteria are considered a suitable solution to lignin biodegradation problems, but exploitation of ligninolytic bacteria is still limited to date. Hence, this study aimed to isolate and characterize potential lignin peroxidase ligninolytic bacteria from decomposing soil, sawdust, and cow dung at Richard Bay, South Africa. The samples were collected and cultured in the lignin-enriched medium. Pure isolated colonies were characterized through 16S rRNA gene sequencing. The ability of the isolates to grow and utilize aromatic monomers (veratryl and guaiacol alcohol) and decolorize lignin-like dyes (Azure B, Congo Red, Remazol Brilliant Blue R) was evaluated. Of the twenty-six (26) bacteria isolates 10 isolates, including Pseudomonas spp. (88%), Enterobacter spp. (8%), and Escherichia coli (4%) were identified as true lignin peroxidase producers. Pseudomonas aeruginosa (CP031449.2) and E. coli (LR025096.1) exhibited the highest ligninolytic activities. These isolates could potentially be exploited in the industry and wastewater treatment as effective lignin degrading agents.

TiO2/SO4/Ni@SBA-15 catalysts for the selective oxidation of veratryl alcohol to veratraldehyde in a continuous reactor

Veratraldehyde is a crucial industrial component used to make important chemicals, drugs, flavours, perfumes, mosquito repellents and cancer-fighting substances. This research focuses on the continuous processing of veratryl alcohol to veratraldehyde using the catalyst system composed of SBA-15/TiO2/SO4/Ni. The objective of this study is to explore variations in continuous processing parameters and catalyst loading to achieve maximum conversion and selectivity of veratraldehyde. The catalyst was synthesized and then characterized using the X-ray diffraction (XRD), Fourier Transform infrared spectroscopy (FT-IR), Brunauer-Emmett-Teller (BET) surface area analysis, and transmission electron microscopy (TEM), and Temperature Programmed Desorption (TPD). The catalyst was successfully synthesized, and the results of these characterization procedures revealed its particular porosity structure and composition. By attaining maximum conversion and selectivity at a lower temperature of 90 °C, the continuous process highlighted the catalyst's energy efficiency. The findings demonstrated that the highest veratraldehyde selectivity and yield were obtained under optimal reaction conditions, including a reaction time of 2 h for the catalyst SBA-15/TiO2/SO4/Ni(8%). This catalyst produced the best results, with a veratraldehyde selectivity and conversion of 100 and 99.5%, respectively. In addition to optimising the reaction conditions, the catalyst's reusability was assessed by running the same catalyst through the reaction seven times. The outcomes demonstrated that even after numerous applications, the catalyst maintained good activity and selectivity. This shows the promise of the SBA-15/ TiO2/SO4/Ni(8) catalyst system for the selective oxidation of veratryl alcohol to veratraldehyde in terms of excellent selectivity, good yield, and reusability. Veratraldehyde could be produced industrially at low cost and with minimal impact on the environment thanks to this investigation of a continuous process.

Controlled Immobilization of a Palladium Complex/Laccase Hybrid into a Macrocellular Siliceous Host.

This study investigates the site-directed immobilization of a hybrid catalyst bearing a biquinoline-based-Pd(II) complex (1) and a robust laccase within cavities of a silica foam to favor veratryl alcohol oxidation. We performed the grafting of 1 at a unique surface located lysine of two laccase variants, either at closed (1⊂UNIK157 ) or opposite position (1⊂UNIK71 ) of the enzyme oxidation site. After immobilization into the cavities of silica monoliths bearing hierarchical porosity, we show that catalytic activity is dependent on the orientation and loading of each hybrid, 1⊂UNIK157 being twice as active than 1⊂UNIK71 (203 TON vs 100 TON) when operating under continuous flow. These systems can be reused 5 times, with an operational activity remaining as high as 40 %. We show that the synergy between 1 and laccase can be tuned within the foam. This work is a proof of concept for controlling the organization of a heterogeneous hybrid catalyst using a Pd/laccase/silica foam.

Laccase-immobilized on superparamagnetic iron oxide nanoparticles incorporated polymeric ultrafiltration membrane for the removal of toxic pentachlorophenol

A biocatalytic membrane offers an ideal alternative to the conventional treatment process for the removal of toxic pentachlorophenol (PCP). The limelight of the study is to utilize superparamagnetic iron oxide nanoparticles (SPIONs) incorporated (poly (methyl vinyl ether-alt-maleic acid) (PMVEAMA) and poly (ether - ether) sulfone (PEES)) membrane for immobilization of laccase and its application towards the removal of PCP. In regard to immobilization of Tramates versicolor laccase onto membranes, 5 mM glutaraldehyde with 10 h cross-linking time was employed, yielding 76.92% and 77.96% activity recovery for PEES/PMVEAMA/La and PEES/PMVEAMA/SPIONs/Lac, respectively. In the context of kinetics and stability studies, the immobilized laccase on PEES/PMVEAMA/Lac membrane outperforms the free and PEES/PMVEAMA laccases. At pH 7.0, the free enzyme loses half of its activity, while the immobilized laccases maintained more than 87% of their initial activity even after 480 min. With regard to PCP removal, the removal efficiency of immobilized laccase on the membrane was more than free enzyme. With 100 ppm of PCP, immobilized laccase on PEES/PMVEAMA/SPIONs membrane at pH 4.0 and 50 °C had a removal efficacy of 61.65% in 24 h. Furthermore, to perk up the removal of PCP, the laccase-aided system with mediators was investigated. Amongst, veratryl alcohol displayed 71.04% of PCP removal using immobilized laccase. The reusability of the laccase heightened after immobilization on PEES/PMVEAMA/SPIONs portraying 62.44% of the residual activity with 39.4% of PCP removal even after five cycles. The current investigation reveals the efficacy of the mediator-aided PEES/PMVEAMA/lac membrane system towards removing PCP from the aqueous solution, which can also be proposed for a membrane bioreactor.

In situ treatment of real textile effluent in constructed furrows using consortium of Canna indica and Saccharomyces cerevisiae and subsequent biochemical and toxicity evaluation

Emerging contaminants removals like dyes and heavy metals from the textile effluent have an immense challenge. The present study focuses on the biotransformation and detoxification of dyes and in situ textile effluent treatment by plants and microbes efficiently. A mixed consortium of perennial herbaceous plant Canna indica and fungi Saccharomyces cerevisiae showed decolorization of di-azo dye Congo red (CR, 100 mg/L) up to 97% within 72 h. Root tissues and Saccharomyces cerevisiae cells revealed induction of various dye-degrading oxidoreductase enzymes such as lignin peroxidase, laccase, veratryl alcohol oxidase and azo reductase during CR decolorization. Chlorophyll a, Chlorophyll b and carotenoid pigments were notably elevated in the leaves of a plant during the treatment. Phytotransformation of CR into its metabolic constituents was detected by using several analytical techniques, including FTIR, HPLC, and GC-MS and its non-toxic nature was confirmed by cyto-toxicological evaluation on Allium cepa and on freshwater bivalves. Mix consortium of plant Canna indica and fungi Saccharomyces cerevisiae efficiently treated textile wastewater (500 L) and reduced ADMI, COD, BOD, TSS and TDS (74, 68, 68, 78, and 66%) within 96 h. In situ textile wastewater treatment for in furrows constructed and planted with Canna indica, Saccharomyces cerevisiae and consortium-CS within 4 days reveals reduced ADMI, COD, BOD, TDS and TSS (74, 73, 75, 78, and 77%). Comprehensive observations recommend this is an intelligent tactic to exploit this consortium in the furrows for textile wastewater treatment.

Nanosponge-C3N4 composites as photocatalysts for selective partial alcohol oxidation in aqueous suspension.

A set of four composite materials was prepared, consisting of a nanosponge matrix based on β-cyclodextrin in which carbon nitride was dispersed. The materials were characterized by the presence of diverse cross-linker units joining the cyclodextrin moieties, in order to vary the absorption/release abilities of the matrix. The composites were characterized and used as photocatalysts in aqueous medium under UV, visible and natural solar irradiation for the photodegradation of 4-nitrophenol, and for the selective partial oxidation of 5-hydroxymethylfurfural and veratryl alcohol to the corresponding aldehydes. The nanosponge-C3N4 composites showed higher activity than the pristine semiconductor, which can probably be attributed to the synergic effect of the nanosponge, capable of increasing the substrate concentration near the surface of the photocatalyst.

Characterization of Lignin Peroxidase from Cryptococcus neoformans for Bioremediation of Pulp and Paper Mill Effluent

Eight fungal strains (F1–F8) isolate from the sediment core and degraded wood of the Pulp and Paper Mill effluent and Phanerochaete chrysosporium are tested for different cellulolytic (CMcase, FPase, Xylanases) and lignolytic (lignin peroxidase) enzyme activity in pulp. F-3 (Cryptococcus neoformans) strain shows higher enzyme activity compare to other fungi isolated from effluent. Weight loss, cellulose loss, and organic carbon contents are found maximum in F-3 (C. neoformans) strain. Reducing sugar, protein content, and color removing potential are also higher in C. neoformans. The culture extract of F-3 strain grows in presence of pulp fractionated into five protein fractions has indicated two fractions of molecular weight, 38,000 and 40,000 Da, having lignin peroxidase activity. Lignin peroxidase has optimum activity at pH 2–3 and temperature 20–30 °C, maximum activity at 6–48 mM veratryl alcohol concentration and 256 mM H2O2, however, sodium azide inhibits the enzyme activity. Different metals (CoCl2, HgSO4, CaCl2, SnCl2, FeSO4, CuSO4, and ZnSO4) also affect the lignin peroxidase activity. Characterization study is performed for significant analysis.

Bienzymatic Cascade Combining a Peroxygenase with an Oxidase for the Synthesis of Aromatic Aldehydes from Benzyl Alcohols

Aromatic aldehydes are important aromatic compounds for the flavour and fragrance industry. In this study, a parallel cascade combining aryl alcohol oxidase from Pleurotus eryngii (PeAAOx) and unspecific peroxygenase from the basidiomycete Agrocybe aegerita (AaeUPO) to convert aromatic primary alcohols into high-value aromatic aldehydes is proposed. Key influencing factors in the process of enzyme cascade catalysis, such as enzyme dosage, pH and temperature, were investigated. The universality of PeAAOx coupled with AaeUPO cascade catalysis for the synthesis of aromatic aldehyde flavour compounds from aromatic primary alcohols was evaluated. In a partially optimised system (comprising 30 μM PeAAOx, 2 μM AaeUPO at pH 7 and 40 °C) up to 84% conversion of 50 mM veratryl alcohol into veratryl aldehyde was achieved in a self-sufficient aerobic reaction. Promising turnover numbers of 2800 and 21,000 for PeAAOx and AaeUPO, respectively, point towards practical applicability.

Selective aerobic oxidation of biomass model compound veratryl alcohol catalyzed by air-stable copper(ii) complexes in water

Three new copper(ii) complexes were synthesized and successfully utilized as effective catalysts for the selective aerobic oxidation of biomass derived veratryl alcohol to veratraldehyde in water as a green and sustainable reaction medium.

Adsorption Potential of Schizophyllum commune White Rot Fungus for Degradation of Reactive Dye and Condition Optimization: A Thermodynamic and Kinetic Study

The pollution due to dyes from textile sector is one of the major issues faced worldwide. This study was focused on the removal of the reactive dye, Drimaren Turquoise CL-B using Schizophyllum commune, a white rot fungus (WRF) keeping in mind the current environmental conditions. Different parameters like pH, sources of carbon & nitrogen, temperature, concentration of dye and C/N ratio were used to investigate their effect on the process. Maximum dye removal of 95.45% was obtained at pH 4.5, temperature 35°C, inoculum size 3 mL, veratryl alcohol (mediator), glucose (carbon source) and ammonium nitrate (nitrogen source). The enzyme activity was determined by employing enzyme assay. Laccase and Lignin peroxidase (LiP) activity was low while Manganese peroxidase (MnP) activity was highest. Maximum bio-sorption was achieved at pH 1 and 313 K. The pseudo-2nd-order kinetic model & Freundlich isotherm was best suited for the process of removal of dye. From these data, it is concluded that white rot fungus could possibly be the excellent biomaterial for elimination of synthetic dyes from wastewater.

Alginate Encapsulation Stabilizes Xylanase Toward the Laccase Mediator System.

Xylanase, a hydrolytic enzyme, is susceptible to inactivation by the oxidative conditions generated by the laccase mediator system (LMS). Given the impetus to develop a mixed enzyme system for application in biomass processing industries, xylanase was encapsulated with either Cu2+- or Ca2+-alginate and then exposed to the LMS with variations such as mediator type, mediator concentration, and treatment pH. Results demonstrate that alginate-encapsulated xylanase retains substantial activity (> 80%) when exposed to the LMS relative to non-encapsulated xylanase. Cu2+-alginate generally provided better protection than Ca2+-alginate for all mediators, and protection was observed even at a low pH, where the LMS is most potent. Despite encapsulation, xylanase was still capable of hydrolyzing its polymeric substrate xylan, given kcat/Km values within an order of magnitude of that for non-encapsulated xylanase. The alginate matrix does not impede the function of the oxidized mediator, since comparable Vmax values were observed for the conversion of veratryl alcohol to veratraldehyde by free and Cu2+-alginateencapsulated laccase. Overall, these results support development of a mixed enzyme system for biomass delignification and, more broadly, show potential for protecting protein function in an oxidative environment.

Replacing benzyl chloride with a lignin-degradation product in cellulose etherification decreases the melting point

A cellulose ether that is easier to melt than benzyl cellulose was produced from the lignin degradation product veratryl alcohol. Veratryl chloride and bromide were synthesized from the alcohol, and these two chemicals were used to react with Avicel® cellulose to form the novel cellulose ether veratryl cellulose (VC). Spectroscopic characterisation techniques (1H NMR, FTIR) indicated the successful conversion of Avicel® cellulose to the cellulose ether VC, by both routes, at a degree of substitution of 1.4 to 1.6. Melting measurements of the VC samples showed a gradual softening from approximately 110 °C; the VC was melted below 200 °C. XRD analysis confirmed that the chemical treatments affect the degree of crystallinity. Size exclusion chromatography results showed that the products differ remarkably in molecular weight. The VC synthesized with veratryl chloride degraded almost twice as much as when veratryl bromide were used. The cellulose ethers were soluble in DMSO, DMAc, and CHCl3.

Effects of the Preferential Oxidation of Phenolic Lignin Using Chlorine Dioxide on Pulp Bleaching Efficiency.

Chlorine dioxide is widely used for pulp bleaching because of its high delignification selectivity. However, efficient and clean chlorine dioxide bleaching is limited by the complexity of the lignin structure. Herein, the oxidation reactions of phenolic (vanillyl alcohol) and non-phenolic (veratryl alcohol) lignin model species were modulated using chlorine dioxide. The effects of chlorine dioxide concentration, reaction temperature, and reaction time on the consumption rate of the model species were also investigated. The optimal consumption rate for the phenolic species was obtained at a chlorine dioxide concentration of 30 mmol·L-1, a reaction temperature of 40 °C, and a reaction time of 10 min, resulting in the consumption of 96.3% of vanillyl alcohol. Its consumption remained essentially unchanged compared with that of traditional chlorine dioxide oxidation. However, the consumption rate of veratryl alcohol was significantly reduced from 78.0% to 17.3%. Additionally, the production of chlorobenzene via the chlorine dioxide oxidation of veratryl alcohol was inhibited. The structural changes in lignin before and after different treatments were analyzed. The overall structure of lignin remained stable during the optimization of the chlorine dioxide oxidation treatment. The signal intensities of several phenolic units were reduced. The effects of the selective oxidation of lignin by chlorine dioxide on the pulp properties were analyzed. Pulp viscosity significantly increased owing to the preferential oxidation of phenolic lignin by chlorine dioxide. The pollution load of bleached effluent was considerably reduced at similar pulp brightness levels. This study provides a new approach to chlorine dioxide bleaching. An efficient and clean bleaching process of the pulp was developed.

Evaluation of application potential of dye-decolorizing peroxidase from Bacillus amyloliquefaciens in bioremediation of paper and pulp mill effluent.

Pulp and paper mill effluent is rich in recalcitrant and toxic pollutants compounds and causes pollution. To find an efficient biocatalyst for the treatment of effluent, a dye-decolorizing peroxidase from Bacillus amyloliquefaciens MN-13, which is capable of degrading lignin, was used for the bioremediation of paper and pulp mill effluent. The dye-decolorizing peroxidase from Bacillus amyloliquefaciens (BaDyP) exhibited high-redox potential to 2, 2'-azinobis (3-ethylbenzothiazoline- 6-sulfonic acid) ammonium salt (ABTS), veratryl alcohol, Mn2+, reactive blue 19, reactive black 5 and lignin dimer guaiacylglycerol-beta-guaiacyl ether (GGE). When GGE was used as substrate, BaDyP broke β-O-4 bond of GGE and then oxidize Cα to generate vanillin. The Km values for ABTS and veratryl alcohol were 2.19 mm and 0.07 mm, respectively. The Vmax for ABTS and veratryl alcohol were 1.8 mm/min and 14.12 mm/min, respectively. The BaDyP-mediated treatment of pulp and paper mill effluent led to significant reduction of chemical oxygen demand (COD) and color. When 5% (v/v) of effluent was treated with BaDyP for 12 h at 30°C and pH 2, the removal of COD, color, and lignin was achieved at 82.7, 80.2, and 78.20%, respectively. In detoxification assay, the seeds of Vigna unguiculata grown in treated effluent showed a significant increase in germination rate from 66.7% (untreated effluent) to 90%, and in radicle length from 0.68 cm (untreated effluent) to 1.26 cm, respectively. In the meanwhile, the inhibition of Escherichia coli and Bacillus subtilis by the treated effluent reduced significantly as compared to untreated effluent, indicating high detoxification performance of BaDyP for the treatment of pulp and paper mill effluent. The findings suggest that BaDyP is a potential catalyst for bioremediation of pulp and paper mill effluent, as it is effective in substantial lowering of pollutants load as well as reduces COD, color, and toxicity of effluent.