Novel Thermophilic Bacterial Laccase for the Degradation of Aromatic Organic Pollutants

Sharma, Nabangshu; Leung, Ivanhoe K. H.

doi:10.3389/fchem.2021.711345

Cited by 26 publications

(7 citation statements)

References 65 publications

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“…Laccases, enzymes found in various organisms, including bacteria, fungi, and plants, possess a wide range of redox potentials. These enzymes play a significant role in the degradation or removal of compounds like BPA [46][47][48]. Bacterial laccases, derived from different bacterial species, exhibit varying redox potentials depending on their specific sources.…”

Section: Biodegradation Of Bpa By Bacteriamentioning

confidence: 99%

Research Progress of Methods for Degradation of Bisphenol A

Han,

Dai,

Rong

et al. 2023

Molecules

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Bisphenol A (BPA), an endocrine disruptor widely used in industrial production, is found in various environmental sources. Despite numerous reports on BPA degradation and removal, the details remain unclear. This paper aims to address this gap by providing a comprehensive review of BPA degradation methods, focusing on biological, physical, and chemical treatments and the factors that affect the degradation of BPA. Firstly, the paper uses VOSviewer software (version 1.6.15) to map out the literature on BPA degradation published in the past 20 years, which reveals the trends and research focus in this field. Next, the advantages and limitations of different BPA degradation methods are discussed. Overall, this review highlights the importance of BPA degradation to protect the environment and human health. The paper provides significant insights for researchers and policymakers to develop better approaches for BPA degradation and removal.

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Section: Biodegradation Of Bpa By Bacteriamentioning

confidence: 99%

Research Progress of Methods for Degradation of Bisphenol A

Han,

Dai,

Rong

et al. 2023

Molecules

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“…However, their application is usually hampered due to the long fermentation periods, acidic pH optima, intolerance to extreme conditions, and difficulty in overproducing in heterologous hosts (Baldrian, 2006 ; Kim et al, 2010 ; Du et al, 2015 ). Meanwhile, small laccases, both three- and two-domain laccases, from bacterial sources have gained attention recently, due to their exceptional attributes such as ability to withstand wide temperature and pH ranges, ease in genetic manipulation, and tremendous stability even when inhibitory agents are present (Mukhopadhyay et al, 2013 ; Chauhan et al, 2017 ; Arregui et al, 2019 ; Gianolini et al, 2020 ; Sharma and Leung, 2021 ). In addition, a short generation time of bacteria makes it easier to scale up laccase production processes on a commercial scale (Brugnari et al, 2021 ; Akram et al, 2022 ).…”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of a New Serratia proteamaculans Strain That Naturally Produces Significant Amount of Extracellular Laccase

et al. 2022

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Natural biodegradation processes hold promises for the conversion of agro-industrial lignocellulosic biomaterials into biofuels and fine chemicals through lignin-degrading enzymes. The high cost and low stability of these enzymes remain a significant challenge to economic lignocellulosic biomass conversion. Wood-degrading microorganisms are a great source for novel enzyme discoveries. In this study, the decomposed wood samples were screened, and a promising γ-proteobacterial strain that naturally secreted a significant amount of laccase enzyme was isolated and identified as Serratia proteamaculans AORB19 based on its phenotypic and genotypic characteristics. The laccase activities in culture medium of strain AORB19 were confirmed both qualitatively and quantitatively. Significant cultural parameters for laccase production under submerged conditions were identified following a one-factor-at-a-time (OFAT) methodology: temperature 30°C, pH 9, yeast extract (2 g/l), Li+, Cu2+, Ca2+, and Mn2+ (0.5 mM), and acetone (5%). Under the selected conditions, a 6-fold increase (73.3 U/L) in laccase production was achieved when compared with the initial culturing conditions (12.18 U/L). Furthermore, laccase production was enhanced under alkaline and mesophilic growth conditions in the presence of metal ions and organic solvents. The results of the study suggest the promising potential of the identified strain and its enzymes in the valorization of lignocellulosic wastes. Further optimization of culturing conditions to enhance the AORB19 strain laccase secretion, identification and characterization of the purified enzyme, and heterologous expression of the specific enzyme may lead to practical industrial and environmental applications.

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“…An increasing number of bacterial laccase genes have been well studied and characterized, including Bacillus genera-derived CotA-laccases from B. subtilis [ 3 , 4 ], B. pumilus [ 5 ], B. licheniformis [ 6 ] B. amyloliquefaciens [ 7 ], B. sphaericus [ 8 ], B. altitudinis [ 9 ], B. safensis [ 10 ], and B. cereus [ 11 ]. Furthermore, Bacillus laccase has been reported to be a potential biocatalyst for various industrial applications, like pulp biobleaching [ 12 ], degrading organ-phosphorous pesticides [ 13 ], degrading aromatic organic pollutants [ 14 ], etc.…”

Section: Introductionmentioning

confidence: 99%

Improving Degradation of Polycyclic Aromatic Hydrocarbons by Bacillus atrophaeus Laccase Fused with Vitreoscilla Hemoglobin and a Novel Strong Promoter Replacement

Wang

Tan

Sun

et al. 2022

Biology

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Laccases catalyze a variety of electron-rich substrates by reducing O2 to H2O, with O2 playing a vital role as the final electron acceptor in the reaction process. In the present study, a laccase gene, lach5, was identified from Bacillus atrophaeus through sequence-based screening. LacH5 was engineered for modification by fusion expression and promoter replacement. Results showed that the purified enzyme LacH5 exhibited strong oxidative activity towards 2,2’-azinobis(3-ehtylbenzothiazolin-6-sulfnic acid) ammonium salt (ABTS) under optimum pH and temperature conditions (pH 5.0, 60 °C) and displayed remarkable thermostability. The activity of the two fusion enzymes was enhanced significantly from 14.2 U/mg (LacH5) to 22.5 U/mg (LacH5-vgb) and 18.6 U/mg (Vgb-lacH5) toward ABTS after LacH5 fusing with Vitreoscilla hemoglobin (VHb). Three of six tested polycyclic aromatic hydrocarbons (PAHs) were significantly oxidized by two fusion laccases as compared with LacH5. More importantly, the expression level of LacH5 and fusion protein LacH5-vgb was augmented by 3.7-fold and 7.0-fold, respectively, by using a novel strong promoter replacement. The results from the current investigation provide new insights and strategies for improving the activity and expression level of bacterial laccases, and these strategies can be extended to other laccases and multicopper oxidases.

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Novel Thermophilic Bacterial Laccase for the Degradation of Aromatic Organic Pollutants

Cited by 26 publications

References 65 publications

Research Progress of Methods for Degradation of Bisphenol A

Research Progress of Methods for Degradation of Bisphenol A

Identification and Characterization of a New Serratia proteamaculans Strain That Naturally Produces Significant Amount of Extracellular Laccase

Improving Degradation of Polycyclic Aromatic Hydrocarbons by Bacillus atrophaeus Laccase Fused with Vitreoscilla Hemoglobin and a Novel Strong Promoter Replacement

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