Browse
Submit Data
Databases
API
Help

Dataset Information

19 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Thiolation of Myco-Synthesized Fe₃O₄-NPs: A Novel Promising Tool for Penicillium expansium Laccase Immobilization to Decolorize Textile Dyes and as an Application for Anticancer Agent.

ABSTRACT: Environmental pollution due to the continuous uncontrolled discharge of toxic dyes into the water bodies provides insight into the need to eliminate pollutants prior to discharge is significantly needed. Recently, the combination of conventional chemotherapeutic agents and nanoparticles has attracted considerable attention. Herein, the magnetic nanoparticles (Fe₃O₄-NPs) were synthesized using metabolites of Aspergillus niger. Further, the surfaces of Fe₃O₄-NPs were functionalized using 3-mercaptoproionic acid as confirmed by XRD, TEM, and SEM analyses. A purified P. expansum laccase was immobilized onto Fe₃O₄/3-MPA-SH and then the developed immobilized laccase (Fe₃O₄/3-MPA-S-S-laccase) was applied to achieve redox-mediated degradation of different dyes. The Fe₃O₄/3-MPA-S-S-laccase exhibited notably improved stability toward pH, temperature, organic solvents, and storage periods. The Fe₃O₄/3-MPA-S-S-laccase exhibited appropriate operational stability while retaining 84.34% of its initial activity after 10 cycles. The catalytic affinity (K_cat/K_m) of the immobilized biocatalyst was increased above 10-fold. The experimental data showed remarkable improvement in the dyes' decolorization using the immobilized biocatalyst in the presence of a redox mediator in seven successive cycles. Thus, the prepared novel nanocomposite-laccase can be applied as an alternative promising strategy for bioremediation of textile wastewater. The cytotoxic level of carboplatin and Fe₃O₄-NPs singly or in combination on various cell lines was concentration-dependent.

SUBMITTER: El-Shora HM

PROVIDER: S-EPMC8777717 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Similar Datasets

Nano-bioremediation of textile industry wastewater using immobilized CuO-NPs myco-synthesized by a novel Cu-resistant Fusarium oxysporum OSF18.

Project description:Currently, bionanotechnologies are attracting great interest due to their promising results and potential benefits on many aspects of life. In this study, the objectives was to biosynthesis CuO-NPs using cell-free extract(s) of copper-resistant fungi and use them in bioremediation of textile industry wastewater. Out of 18 copper-resistant fungal isolates, the novel fungus strain Fusarium oxysporum OSF18 was selected for this purpose. This strain showed a high efficiency in extracellular reducing copper ions to their nano-form. The myco-synthesized CuO-NPs were characterized using UV-Vis spectroscopy, HRTEM, FTIR, and XRD and were found to be spherical nanocrystals with the size range of 21-47 nm. The bio-synthesized CuO-NPs showed promising antimicrobial activity as well as high efficiency in removing heavy metals and textile dye from industrial wastewater. The myco-synthesized CuO-NPs immobilized in alginate beads exhibited superior microbial disinfection (99.995%), heavy metals removal (93, 55, and 30 % for Pb, Cr, and Ni, respectively), and dye decolorization (90%). Such results represent a promising step to produce an eco-friendly, cost-effective, and easy-to handle tool for the bioremediation of textile industry wastewater.

| S-EPMC9908718 | biostudies-literature

Structure and Bioactive Properties of Novel Textile Dyes Synthesised by Fungal Laccase.

Project description:Novel sustainable processes involving oxidative enzymatic catalysts are considered as an alternative for classical organic chemistry. The unique physicochemical and bioactive properties of novel bio-products can be obtained using fungal laccase as catalyst. Among them are textile biodyes synthesised during oxidation of substrates belonging to the amine and methoxy organic derivatives. The process of synthesis occurs in mild conditions of pH, temperature, and pressure, and without using harmful oxidants. The effect of fungal laccase activity on the substrates mixture transformation efficiency was analysed in terms of antimicrobial dye synthesis on a large scale. Three new phenazine dyes, obtained in the presence of laccase from Cerrena unicolor, were studied for their structure and properties. The phenazine core structure of the products was a result of tri-molecular transformation of aminomethoxybenzoic acid and aminonaphthalene sulfonic acid isomers. One of the compounds from the synthesised dye, namely 10-((2-carboxy-6-methoxyphenyl)amino)-11-methoxybenzo[a]phenazine-8-carboxylic acid, was able to inhibit the growth of Staphylococcus aureus. The high concentration of substrates (5 g/L) was efficiently transformed during 72 h in the mild conditions of pH 4 with the use of laccase with an activity of 200 U per g of the substrates mixture. The new bioactive dye exhibited excellent dyeing properties with concomitant antibacterial and antioxidative activity. The proposed enzyme-mediated synthesis represents an alternative eco-friendly route for the synthesis of novel antimicrobial compounds with high importance for the medical textile industry.

| S-EPMC7139866 | biostudies-literature

Effective removal of anionic textile dyes using adsorbent synthesized from coffee waste.

Project description:Adsorption of Reactive Black 5 and Congo Red from aqueous solution by coffee waste modified with polyethylenimine was investigated. The removal percentages of both dyes increased with amount of polyethyleneimine in the modified adsorbent. Characterization revealed that polyethyleneimine modification improved the adsorbent surface chemistry, while slight improvement of adsorbent textural properties was also observed. The adsorbent's excellent performance was demonstrated by high removal percentages towards the anionic dyes in most experimental runs. The modelling result showed that anionic dyes adsorption occurred via monolayer adsorption, and chemisorption was the rate-controlling step. The adsorbent possesses higher maximum adsorption capacity towards Reactive Black 5 (77.52?mg/g) than Congo Red (34.36?mg/g), due to the higher number of functional groups in Reactive Black 5 that interact with the adsorbent. This study reveals the potential of adsorbent derived from coffee waste in textile wastewater treatment. Furthermore, surface chemistry modification is proven as an effective strategy to enhance the performance of biowaste-derived adsorbents.

| S-EPMC7031400 | biostudies-literature

A novel laccase from Trametes polyzona with high performance in the decolorization of textile dyes.

Project description:Laccases are multicopper oxidases able to oxidize several phenolic compounds and find application in numerous industrial applications. Among laccase producers, white-rot fungi represent a valuable source of multiple isoforms and isoenzymes of these multicopper oxidases. Here we describe the identification, biochemical characterization, and application of laccase 2 from Trametes polyzona (TP-Lac2), a basidiomycete fungus emerged among others that have been screened by plate assay. This enzyme has an optimal temperature of 50 °C and in acidic conditions it is able to oxidize both phenolic and non-phenolic compounds. The ability of TP-Lac2 to decolorize textile dyes was tested in the presence of natural and synthetic mediators at 30 °C and 50 °C. Our results indicate that TP-Lac2 most efficiently decolorizes (decolorization rate > 75%) malachite green oxalate, orange G, amido black10B and bromocresol purple in the presence of acetosyringone and 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate)-ABTS. Overall, the laccase mediator system consisting of TP-Lac2 and the natural mediator acetosyringone has potential as an environmentally friendly alternative for wastewater treatment in the textile industry.

| S-EPMC10954600 | biostudies-literature

Purification and characterization of laccase from Marasmius species BBKAV79 and effective decolorization of selected textile dyes.

Project description:A novel laccase-producing white-rot fungus, Marasmius sp. BBKAV79 (Genbank Accession Number-KP455496, KP455497), was isolated and subjected to purification, characterization and dye decolorization study. The purified enzyme was obtained with a specific activity of 0.226 U mg-1 protein and a final yield of 13.5 %. The enzyme was found to be a monomeric protein with a molecular mass of ~75 kDa as estimated by non-denaturing polyacrylamide gel electrophoresis (PAGE) and further confirmed with zymogram analysis. The optimal pH and temperature of the laccase was recorded to be 5.5 and 40 °C, respectively. The metal ions Hg2+ and Ag+ were found to drastically inhibit the activity of laccase at the rate of 96.6 and 96.5 %, respectively. Nevertheless, Fe3+ was found to inhibit laccase activity at 40 %. Phenylmethanesulfonyl fluoride (PMSF) strongly inhibited the laccase activity, and additives viz, sodium dodecyl sulfate (SDS), hydrogen peroxide (H2O2) and sodium chloride (NaCl) were known to follow the earlier pattern of enzyme inhibition. The values of kinetic parameters K m and V max for purified laccase were noted at 3.03 mM and 5 μmol min-1, respectively, for guaiacol as substrate. The textile dyes were decolorized at a range of 72-76 % and 88-93 % when treated with Marasmius sp. BBKAV79 and purified laccase, respectively. Based on the outcome of the present investigation, it could be, therefore, inferred that laccase isolated from Marasmius sp. BBKAV79 effectively decolorizes the textile dyes; however, the metal ions Hg2+, Ag+ and Fe3+ and agents like PMSF, SDS, H2O2 and NaCl pose an effective inhibitory potential under specified physicochemical conditions.

| S-EPMC5010537 | biostudies-literature

Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes.

Project description:Although laccase has been recognized as a wonder molecule and green enzyme, the use of low yielding fungal strains, poor production, purification, and low enzyme kinetics have hampered its large-scale application. Thus,this study aims to select high yielding fungal strains and optimize the production, purification, and kinetics of laccase of Aspergillus sp. HB_RZ4. The results obtained indicated that Aspergillus sp. HB_RZ4 produced a significantly large amount of laccase under meso-acidophilic shaking conditions in a medium containing glucose and yeast extract. A 25 μM CuSO4 was observed to enhance the enzyme yield. The enzyme was best purified on a Sephadex G-100 column. The purified enzyme resembled laccase of A. flavus. The kinetics of the purified enzyme revealed high substrate specificity and good velocity of reaction,using ABTS as a substrate. The enzyme was observed to be stable over various pH values and temperatures. The peptide structure of the purified enzyme was found to resemble laccase of A. kawachii IFO 4308. The fungus was observed to decolorize various dyes independent of the requirement of a laccase mediator system.Aspergillus sp. HB_RZ4 was observed to be a potent natural producer of laccase, and it decolorized the dyes even in the absence of a laccase mediator system. Thus, it can be used for bioremediation of effluent that contains non-textile dyes.

| S-EPMC7272029 | biostudies-literature

α-Cellulose Fibers of Paper-Waste Origin Surface-Modified with Fe3O4 and Thiolated-Chitosan for Efficacious Immobilization of Laccase.

Project description:The utilization of waste-paper-biomass for extraction of important α-cellulose biopolymer, and modification of extracted α-cellulose for application in enzyme immobilization can be extremely vital for green circular bio-economy. Thus, in this study, α-cellulose fibers were super-magnetized (Fe3O4), grafted with chitosan (CTNs), and thiol (-SH) modified for laccase immobilization. The developed material was characterized by high-resolution transmission electron microscopy (HR-TEM), HR-TEM energy dispersive X-ray spectroscopy (HR-TEM-EDS), X-ray diffraction (XRD), vibrating sample magnetometer (VSM), X-ray photoelectron spectroscopy (XPS), and Fourier transform infrared spectroscopy (FT-IR) analyses. Laccase immobilized on α-Cellulose-Fe3O4-CTNs (α-Cellulose-Fe3O4-CTNs-Laccase) gave significant activity recovery (99.16%) and laccase loading potential (169.36 mg/g). The α-Cellulose-Fe3O4-CTNs-Laccase displayed excellent stabilities for temperature, pH, and storage time. The α-Cellulose-Fe3O4-CTNs-Laccase applied in repeated cycles shown remarkable consistency of activity retention for 10 cycles. After the 10th cycle, α-Cellulose-Fe3O4-CTNs possessed 80.65% relative activity. Furthermore, α-Cellulose-Fe3O4-CTNs-Laccase shown excellent degradation of pharmaceutical contaminant sulfamethoxazole (SMX). The SMX degradation by α-Cellulose-Fe3O4-CTNs-Laccase was found optimum at incubation time (20 h), pH (3), temperatures (30 °C), and shaking conditions (200 rpm). Finally, α-Cellulose-Fe3O4-CTNs-Laccase gave repeated degradation of SMX. Thus, this study presents a novel, waste-derived, highly capable, and super-magnetic nanocomposite for enzyme immobilization applications.

| S-EPMC7919293 | biostudies-literature

Improvement of Laccase Activity Via Covalent Immobilization over Mesoporous Silica Coated Magnetic Multiwalled Carbon Nanotubes for the Discoloration of Synthetic Dyes.

Project description:Due to its environmental friendliness and biodegradable ability, the enzymatic decolorization of azo dyes is the best option. However, the free enzyme suffers from various limitations, including poor stability, no repeatable use, and a high expense, which is the key drawback for its practical use. In this analysis, the laccase enzyme was immobilized in mesoporous silica coated magnetic multiwalled carbon nanotubes (Fe3O4-MWCNTs@SiO2) by a glutaraldehyde cross-linker to create an easily separable and stable enzyme. Fourier transform infrared (FTIR) spectroscopy, scanning electron microscopy (SEM), and energy-dispersive X-ray spectroscopy (EDX) were used to characterize the as-synthesized Fe3O4-MWCNTs@SiO2. Laccase immobilized in Fe3O4-MWCNTs@SiO2 showed a good improvement in temperature, pH, and storage stability. Moreover, the operational stability of the biocatalyst was improved, retaining 87% of its original activity even after 10 cycles of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) oxidation. The biocatalysts were applied for the decolorization of selected azo dyes without a mediator, and up to 99% of Eriochrome Black T (EBT), 98% of Acid Red 88 (AR 88), and 66% of Reactive Black 5 (RB5) were decolorized. Based on these properties, the biocatalysts can be potentially utilized in various environmental and industrial applications.

| S-EPMC7860064 | biostudies-literature

Textile Dye Decolorizing Synechococcus PCC7942 Engineered With CotA Laccase.

Project description:Cyanobacteria are prokaryotic phototrophs capable of achieving high cellular densities with minimal inputs. These prokaryotic organisms can grow using sunlight as energy source and carbon dioxide as carbon source what makes them promising candidates as microbial cell factories for the production of numerous compounds such as chemicals, fuels, or biocatalysts. In this study, we have successfully designed and constructed using synthetic biology approach two recombinant strains of Synechococcus elongatus PCC7942 for heterologous expression of the industrially relevant Bacillus subtilis CotA laccase. One of the strains (PCC7942-NSI-CotA) was constructed through integration of the laccase gene into neutral site I of the cyanobacterial genome whilst the other (PCC7942-NSII-CotA) targeted neutral site II of the genome. Of the two strains the one with CotA laccase integrated in neutral site II (PCC7942-NSII-CotA) was superior in terms of growth rate and enzymatic activity toward typical laccase substrates: ABTS [2,2-azino-bis (3-ethylbenzothiazoline-6-sulfonate)] and syringaldazine. That may suggest that two of the traditionally used neutral sites of S. elongatus PCC7942 are not equally suitable for the expression of certain transgenes. The PCC7942-NSII-CotA produced protein was capable of decolourising three classes of dyes namely: anthraquinonic-, azo-, and indigoid-type over 7 days of incubation making the strain a potentially useful microbial cell factory for the production of broad-spectrum biodegradation agent. Interestingly, presence of additional synthetic redox mediator ABTS had no effect on the degradation of these dyes.

| S-EPMC6052094 | biostudies-literature

Dyes Adsorption Behavior of Fe3O4 Nanoparticles Functionalized Polyoxometalate Hybrid.

Project description:The magnetic adsorbent, Fe3O4@[Ni(HL)2]2H2[P2Mo5O23]·2H2O (Fe3O4@1), is synthesized by employing the nanoparticles Fe3O4 and polyoxometalate hybrid 1. Zero-field-cooled (ZFC) and field-cooled (FC) curves show that the blocking temperature of Fe3O4@1 was at 120 K. Studies of Fe3O4@1 removing cationic and anionic dyes from water have been explored. The characterization of Fe3O4@1, effects of critical factors such as dosage, the concentration of methylene blue (MB), pH, adsorption kinetics, isotherm, the removal selectivity of substrate and the reusability of Fe3O4@1 were assessed. The magnetic adsorbent displayed an outstanding removal activity for the cationic dye at a broad range of pH. The adsorption kinetics and isotherm models revealed that the adsorption process of Fe3O4@1 was mainly governed via chemisorption. The maximum capacity of Fe3O4@1 adsorbing substance was 41.91 mg g-1. Furthermore, Fe3O4@1 showed its high stability by remaining for seven runs of the adsorption-desorption process with an effective MB removal rate, and could also be developed as a valuable adsorbent for dyes elimination from aqueous system.

| S-EPMC6749234 | biostudies-literature