Partial purification and biochemical characterization of a new highly acidic NYSO laccase from Alcaligenes faecalis

Abdelgalil, Soad A.; Attia, Ahmad R.; Reyed, Reyed M; Soliman, Nadia A.

doi:10.1186/s43141-020-00088-w

Cited by 16 publications

(9 citation statements)

References 36 publications

(48 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Laccases from Pycnoporus sanguineus (61.4 kDa) [ 40 ], Lentinus squarrosulus MR13 (66 kDa) [ 27 ], Trametes polyzona WRF03 (66 kDa) [ 4 ] and H. echinacea (63 kDa) (Wang and Ng, 2004) have molecular weights very close to that of Lac A. While laccases from T. harzianum strain HZN10 (56 kDa) [ 44 ] and Alcaligenes faecalis (50 kDa) [ 45 ] have a molecular weight close to that of Lac B. A lower molecular weight of 34 kDa is seen in P. eryngii laccase [ 46 ], whereas Trametes versicolor [ 47 ] and T. harzianum WL1 [ 5 ] laccases have larger molecular weights of 97 kDa and 79 kDa, respectively.…”

Section: Resultsmentioning

confidence: 99%

Purification and biochemical characterization of two laccase isoenzymes isolated from Trichoderma harzianum S7113 and its application for bisphenol A degradation

et al. 2023

View full text Add to dashboard Cite

Two laccase isoenzymes (LacA and LacB) were isolated from a novel Trichoderma harzianum S7113 isolate employing ammonium sulfate precipitation, Sephadex G100, and DEAE Sepharose ion exchange chromatography. The molecular weights of the purified LacA and LacB laccases were estimated to be 63 and 48 kDa, respectively. The two isoenzymes had their optimum activities at the same temperature (50 °C), but at slightly different pH values (pH 3.0 for LacA and pH 2.5 for LacB). LacA and LacB had the same thermal stability at 40 °C and pH stability at pH 9.0. The two isoenzymes also showed a high level of specific activity toward ABTS, where the Km values of LacA and LacB were 0.100 and 0.065 mM, whereas their Vmax values were 0.603 and 0.182 µmol min−1, respectively. LacA and LacB catalytic activity was stimulated by Mg2+, Zn2+, K+, and Ni2+, whereas it was inhibited by Hg2+ and Pb2+, β-mercaptoethanol, EDTA, and SDS, and completely inhibited by sodium azide. Our findings indicate that purified laccase has a promising capacity for bisphenol A (BPA) bioremediation across a broad pH range. This finding opens up new opportunities for the commercialization of this technique in a variety of biotechnology-based applications, particularly for removing endocrine chemicals from the environment.

show abstract

Section: Resultsmentioning

confidence: 99%

Purification and biochemical characterization of two laccase isoenzymes isolated from Trichoderma harzianum S7113 and its application for bisphenol A degradation

et al. 2023

View full text Add to dashboard Cite

show abstract

“…A previous study described Lac purification from Coriolopsis gallica with a 4.9-fold increase and an overall yield of 60.6% [33]. The molecular mass of laccase was coincident with most laccases that are monomeric proteins, as confirmed with non-denaturing PAGE, with a molecular weight of ~50 to 80 KDa [6,[34][35][36].…”

Section: Production Of Purified Laccase From P Expansiummentioning

confidence: 88%

“…coincident with most laccases that are monomeric proteins, as confirm denaturing PAGE, with a molecular weight of ~50 to 80 KDa [6,[34][35][36].…”

Section: Production Of Purified Laccase From P Expansiummentioning

confidence: 99%

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

El-Shora

Khateb

Darwish

et al. 2022

JoF

View full text Add to dashboard Cite

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 (Kcat/Km) 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.

show abstract

“…Currently fungal laccase is used in majority of biotechnological application. It has been found that the fungal enzymes are able to function efficiently only under slightly acidic conditions (5 > and < 7), while for catalytic activity to occur, a temperature range of 20–35 °C has been found to be most suitable (Abdelgalil et al 2020 ). On the other hand, very little is known about bacterial laccase, which has wide substrate specificities that can be utilized in industrial settings (Chandra and Chowdhary 2015 ).…”

Section: Discussionmentioning

confidence: 99%

Optimization of laccase from Stenotrophomonas maltophilia E1 by submerge fermentation using coconut husk with its detoxification and biodecolorization ability of synthetic dyes

Albulaihed,

Adnan,

Jamal

et al. 2023

Bioresour. Bioprocess.

View full text Add to dashboard Cite

Enzymatic degradation of synthetic dyes holds an immense promise for addressing the environmental concerns associated with the textile and dye industries. This study aimed to isolate bacteria capable of producing laccase enzymes from an anthropogenic environment. Subsequently, viability of utilizing cost-effective agricultural residues as substrates for laccase production was assessed. Response Surface Methodology (RSM) and the One Variable at a Time (OVAT) approach was pursued for the optimization of laccase production, followed by pH and temperature stability, dye degradation and decolorization experiments, toxicological studies on the degraded dye metabolites. In results, laccase-producing bacterial strain was identified as Stenotrophomonas maltophilia strain E1 (S. maltophilia). Among variety of substrates, coconut husk exhibited optimal efficacy. In a statistical optimization study, it was found that S. maltophilia was capable of producing laccase 51.38 IU/mL, i.e., three times higher than the amount of laccase produced by unoptimized medium (16.7 IU/mL), and the enzyme activity was found to be steady at an acidic pH, and a mesophilic temperature range. The laccase obtained from S. maltophilia E1 demonstrated proficient dye decolorization capabilities, achieving a notable 92.1% reduction in Malachite green dye coloration at a concentration of 500 ppm. Gas chromatography–mass spectrometry (GC–MS) analysis of the decolorized derivatives of Malachite green revealed a conversion into a distinct compounds. Moreover, after undergoing laccase treatment, Malachite green exhibited decreased phytotoxic effects on Oryza sativa, pointing to enzymatic detoxification. Collectively, insights gained from the present study will contribute to the development of efficient enzymatic approaches for addressing the environmental pollution caused by synthetic dyes. Graphical Abstract

show abstract

Partial purification and biochemical characterization of a new highly acidic NYSO laccase from Alcaligenes faecalis

Cited by 16 publications

References 36 publications

Purification and biochemical characterization of two laccase isoenzymes isolated from Trichoderma harzianum S7113 and its application for bisphenol A degradation

Purification and biochemical characterization of two laccase isoenzymes isolated from Trichoderma harzianum S7113 and its application for bisphenol A degradation

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

Optimization of laccase from Stenotrophomonas maltophilia E1 by submerge fermentation using coconut husk with its detoxification and biodecolorization ability of synthetic dyes

Contact Info

Product

Resources

About