Harnessing the power of bacterial laccases for xenobiotic degradation in water: A 10-year overview

Rahman, Mujeeb ur; Ullah, Muhammad Wajid; Shah, Junaid Ali; Sethupathy, Sivasamy; Bilal, Hazart; Abdikakharovich, Sidikov Akmal; Khan, Afaq Ullah; Khan, Khalid Ali; Elboughdiri, Noureddine; Zhu, Daochen

doi:10.1016/j.scitotenv.2024.170498

Cited by 10 publications

(2 citation statements)

References 221 publications

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“…LEA2 may harbor copper-binding enzymes responsible for lignin utilization. Rezaei et al 47 reported a 13.7-fold increase in laccase production with the addition of 0.5 mM CuSO 4 compared to the basal medium in Aquisalibacillus elongatus . Aside from its role in enzyme production, the supply of Cu 2+ as an essential metal ion is pivotal for maintaining enzyme activity and overall lignin degradation efficiency.…”

Section: Discussionmentioning

confidence: 99%

Evaluating lignin degradation under limited oxygen conditions by bacterial isolates from forest soil

Sumranwanich,

Amosu,

Chankhamhaengdecha

et al. 2024

Sci Rep

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Lignin, a heterogeneous aromatic polymer present in plant biomass, is intertwined with cellulose and hemicellulose fibrils, posing challenges to its effective utilization due to its phenolic nature and recalcitrance to degradation. In this study, three lignin utilizing bacteria, Klebsiella sp. LEA1, Pseudomonas sp. LEA2, and Burkholderia sp. LEA3, were isolated from deciduous forest soil samples in Nan province, Thailand. These isolates were capable of growing on alkali lignin and various lignin-associated monomers at 40 °C under microaerobic conditions. The presence of Cu2+ significantly enhanced guaiacol oxidation in Klebsiella sp. LEA1 and Pseudomonas sp. LEA2. Lignin-related monomers and intermediates such as 2,6-dimethoxyphenol, 4-vinyl guaiacol, 4-hydroxybenzoic acid, benzoic acid, catechol, and succinic acid were detected mostly during the late stage of incubation of Klebsiella sp. LEA1 and Pseudomonas sp. LEA2 in lignin minimal salt media via GC–MS analysis. The intermediates identified from Klebsiella sp. LEA1 degradation suggested that conversion and utilization occurred through the β-ketoadipate (ortho-cleavage) pathway under limited oxygen conditions. The ability of these bacteria to thrive on alkaline lignin and produce various lignin-related intermediates under limited oxygen conditions suggests their potential utility in oxygen-limited processes and the production of renewable chemicals from plant biomass.

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Section: Discussionmentioning

confidence: 99%

Evaluating lignin degradation under limited oxygen conditions by bacterial isolates from forest soil

Sumranwanich,

Amosu,

Chankhamhaengdecha

et al. 2024

Sci Rep

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“…They are suitable compounds (i.e., small diffusible electron carriers) that act as intermediate substrates for the enzyme, undergoing an oxidation–reduction cycle and constituting the laccase-mediator system (LMS), which allows the degradation of recalcitrant compounds that are not directly oxidized, either because they are too large to enter the enzyme active site or because they have a redox potential higher than the laccase itself [ 44 ]. For these reasons, laccases have attracted increasing interest for biotechnological applications, especially in bioremediation of environmental emerging and persistent environmental pollutants, including antibiotics [ 45 , 46 , 47 ].…”

Section: Introductionmentioning

confidence: 99%

Evaluation of Antibiotic Biodegradation by a Versatile and Highly Active Recombinant Laccase from the Thermoalkaliphilic Bacterium Bacillus sp. FNT

Sánchez-SanMartín,

Márquez,

Espina

et al. 2024

Biomolecules

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Laccases are industrially relevant enzymes that have gained great biotechnological importance. To date, most are of fungal and mesophilic origin; however, enzymes from extremophiles possess an even greater potential to withstand industrial conditions. In this study, we evaluate the potential of a recombinant spore-coat laccase from the thermoalkaliphilic bacterium Bacillus sp. FNT (FNTL) to biodegrade antibiotics from the tetracycline, β-lactams, and fluoroquinolone families. This extremozyme was previously characterized as being thermostable and highly active in a wide range of temperatures (20–90 °C) and very versatile towards several structurally different substrates, including recalcitrant environmental pollutants such as PAHs and synthetic dyes. First, molecular docking analyses were employed for initial ligand affinity screening in the modeled active site of FNTL. Then, the in silico findings were experimentally tested with four highly consumed antibiotics, representatives of each family: tetracycline, oxytetracycline, amoxicillin, and ciprofloxacin. HPLC results indicate that FNTL with help of the natural redox mediator acetosyringone, can efficiently biodegrade 91, 90, and 82% of tetracycline (0.5 mg mL−1) in 24 h at 40, 30, and 20 °C, respectively, with no apparent ecotoxicity of the products on E. coli and B. subtilis. These results complement our previous studies, highlighting the potential of this extremozyme for application in wastewater bioremediation.

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A comprehensive review on enzymatic decolorization of various azo dyes using laccase for the abatement of industrial pollution

Rajendran,

Kalairaj,

Senthilvelan

2024

Biomass Conv. Bioref.

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Harnessing the power of bacterial laccases for xenobiotic degradation in water: A 10-year overview

Cited by 10 publications

References 221 publications

Evaluating lignin degradation under limited oxygen conditions by bacterial isolates from forest soil

Evaluating lignin degradation under limited oxygen conditions by bacterial isolates from forest soil

Evaluation of Antibiotic Biodegradation by a Versatile and Highly Active Recombinant Laccase from the Thermoalkaliphilic Bacterium Bacillus sp. FNT

A comprehensive review on enzymatic decolorization of various azo dyes using laccase for the abatement of industrial pollution

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