Characterization of a Recombinant Laccase B from Trametes hirsuta MX2 and Its Application for Decolorization of Dyes

Jia, Yitong; Huang, Qianqian; Zhu, Ling; Pan, Cong

doi:10.3390/molecules27051581

Cited by 9 publications

(2 citation statements)

References 51 publications

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“…The decolorization rates for eriochrome black T, methyl orange, and bromophenol blue were 62.3 ± 3.1%, 32.1 ± 1.3%, and 46.3 ± 2.2%, respectively ( Table 2 ). However, L01 was less satisfactory in decolorizing malachite green, crystal violet, and safranine 0, and the decolorization rates were only in the range of 10.2–15.2% within 24 h. The recombinant laccase from Trametes hirsute exhibited a more efficient decolorization ability for remazol brilliant blue R, whereas laccase from the basidiomycete Coprinopsis was efficient for indigo dye decolorization [ 28 , 29 ].…”

Section: Resultsmentioning

confidence: 99%

Characterization of a New Laccase from Vibrio sp. with pH-stability, Salt-tolerance, and Decolorization Ability

Jiang

Deng

Wang³

et al. 2023

Molecules

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Laccases have been widely used for fruit juice clarification, food modification, and paper pulp delignification. In addition, laccases exhibit remarkable performance in the degradation of toxic substances, including pesticides, organic synthetic dyes, antibiotics, and organic pollutants. Thus, the screening and development of robust laccases has attracted significant attention. In this study, Vibrio sp. LA is a strain capable of producing cold-adapted laccases. The laccase coding gene L01 was cloned from this strain and expressed in Yarrowia lipolytica, a host with good secretion ability. The secreted L01 (approximate MW of 56,000 Da) had the activity and specific activity of 18.6 U/mL and 98.6 U/mg toward ABTS, respectively. The highest activity occurred at 35 °C. At 20 °C, L01 activity was over 70% of the maximum activity in pH conditions ranging from 4.5–10.0. Several synthetic dyes were efficiently degraded by L01. Owing to its robustness, salt tolerance, and pH stability, L01 is a promising catalytic tool for potential industrial applications.

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Section: Resultsmentioning

confidence: 99%

Characterization of a New Laccase from Vibrio sp. with pH-stability, Salt-tolerance, and Decolorization Ability

Jiang

Deng

Wang³

et al. 2023

Molecules

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“…To understand the molecular basis of the degradation mechanism, oxidoreductases, such as LiP, LACs in docking, and MD Simulation with several model chemicals, including lignin models, dyes, antibiotics, and EDCs, have been investigated in recent years. [38][39][40][41][42][43][44][45][46] Therefore, it is essential to access all of the aforementioned features for the theoretical degradability using enzyme-pollutant modeling. [37,38] After that, a protein engineering strategy may be used to improve the enzyme's catalytic spectrum.…”

Section: Introductionmentioning

confidence: 99%

Computational Insights into Enzyme‐Substrate Binding Interplay Exhibit Variable Binding Attributes: A Framework for Implementing Oxidoreductase‐Based Applications

Kumar Singh,

Kumar Katari,

Umamaheswari

et al. 2024

ChemistrySelect

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Laccase (LAC) is a potent multicopper oxidase that relies on O2 for its catalytic activity. LAC has been affirmed as an environmentally friendly biocatalyst that often catalyzes a wide array of phenolic substrates. Bacterial‐derived LACs have been less investigated for non‐phenolic substrates in contrast to fungi‐derived LAC. To comprehend the substrates (3,4‐Dimethoxybenzyl alcohol, and Dimer (Guaiacyl 4‐O‐5 guaiacyl) binding interactions of LAC (Thermus thermophilus HB27) was carried out and contrasted with fungal‐derived Lignin peroxidase (LiP) (Trametes cervina) exploiting computational methods, including physicochemical properties, Sequence Annotated by Structure (SAS), Extra precision docking (Glide), and DESMOND‐directed MD‐ simulation. Protein structures exhibited by LAC, and LiP have diverse dissimilar component architects. The XP docking suggested LiP‐Dimer seems to have a comparatively lowest binding affinity (−8.413 kcal/mol), with an MMGBSA score of −33.249 kcal/mol. Further, docked complexes were validated leveraging 50 ns NPT system‐based MD‐simulation for structural and functional stability. The system achieved equilibrium and stability at the end of the simulation, with only the LiP‐3,4‐Dimethoxybenzyl alcohol complex maintained stability. The results of this study offer a framework for improving the binding ability of substrates by way of the use of in‐silico protein engineering, which might eventually result in more effective catalytic applications.

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Characterization and Degradation of Triphenylmethane Dyes and Their Leuco‐Derivatives by Heterologously Expressed Laccase From Coprinus cinerea

Qian,

Pei,

Wang

et al. 2024

Cell Biochemistry & Function

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Laccase is a copper‐containing polyphenol oxidase that can oxidize phenolic and non‐phenolic organic substrates. In the past decades, laccases had received considerable attention because of the ability to degrade various organic substances. Based on the codon preference of the Pichia pastoris expression system, this study optimized the gene structure of the laccase gene Lcc1 from Coprius cinerea through synthetic biology methods. A new gene Lcc1I was synthesized and heterologously expressed in P. pastoris. After 3 days of cultivation in a shake flask at 30°C, the transformants produced at a yield of 890 mg L−1protein. The highest production level of the recombinant laccase was 2760 U L−1. The molecular mass of the recombinant laccase was estimated at 60 kDa. The enzyme showed highest activity at pH 3.4 and 45°C. It possessed better stability at higher pH and lower temperature condition. Using 2,2'‐azino‐bis‐(3‐ethylbenzothiazoline)−6‐sulphonate (ABTS) as the substrate, the Km and Vmax values were 0.136 mM and 9778 μM min−1 mg−1, respectively. The recombinant laccase could directly oxidize some triphenylmethane dyes like leuco‐crystal violet (LCV) and leuco‐malachite green (LMG). With the help of ABTS mediator, it could oxidize and degrade 77.7% crystal violet (CV) and 79.2% malachite green (MG) within 1 h. Our results indicate that optimization of the laccase gene achieves good expression results in the host system. The dye degradation model constructed in this study may also be applied to the degradation of other organic pollutants and toxic substances, providing new solutions for environmental remediation against the increasingly severe environmental pollution.

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Characterization of a Recombinant Laccase B from Trametes hirsuta MX2 and Its Application for Decolorization of Dyes

Cited by 9 publications

References 51 publications

Characterization of a New Laccase from Vibrio sp. with pH-stability, Salt-tolerance, and Decolorization Ability

Characterization of a New Laccase from Vibrio sp. with pH-stability, Salt-tolerance, and Decolorization Ability

Computational Insights into Enzyme‐Substrate Binding Interplay Exhibit Variable Binding Attributes: A Framework for Implementing Oxidoreductase‐Based Applications

Characterization and Degradation of Triphenylmethane Dyes and Their Leuco‐Derivatives by Heterologously Expressed Laccase From Coprinus cinerea

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