Submitted Successfully!
To reward your contribution, here is a gift for you: A free trial for our video production service.
Thank you for your contribution! You can also upload a video entry or images related to this topic.
Version Summary Created by Modification Content Size Created at Operation
1
Daniela Chmelová
 -- 2865 2024-02-27 12:21:25 |
2 format correct
Wendy Huang
 Meta information modification 2865 2024-02-28 10:22:38 |

Video Upload Options

Do you have a full video?
Send video materials Upload full video

Confirm

Are you sure to Delete?
Yes No
Cite
If you have any further questions, please contact Encyclopedia Editorial Office.
Chmelová, D.; Ondrejovič, M.; Miertuš, S. The Removal of Analgesics and Antibiotics by Laccases. Encyclopedia. Available online: https://encyclopedia.pub/entry/55539 (accessed on 27 July 2024).
Chmelová D, Ondrejovič M, Miertuš S. The Removal of Analgesics and Antibiotics by Laccases. Encyclopedia. Available at: https://encyclopedia.pub/entry/55539. Accessed July 27, 2024.
Chmelová, Daniela, Miroslav Ondrejovič, Stanislav Miertuš. "The Removal of Analgesics and Antibiotics by Laccases" Encyclopedia, https://encyclopedia.pub/entry/55539 (accessed July 27, 2024).
Chmelová, D., Ondrejovič, M., & Miertuš, S. (2024, February 27). The Removal of Analgesics and Antibiotics by Laccases. In Encyclopedia. https://encyclopedia.pub/entry/55539
Chmelová, Daniela, et al. "The Removal of Analgesics and Antibiotics by Laccases." Encyclopedia. Web. 27 February, 2024.
The Removal of Analgesics and Antibiotics by Laccases
Edit
This entry is adapted from the peer-reviewed paper 10.3390/life14020230

Laccase is an enzyme belonging to the class of oxidoreductases. It catalyzes the four-electron oxidation of a substrate in the presence of molecular oxygen as a co-substrate to form water. The removal of pharmaceutically active substances by enzymes such as laccases has received considerable attention. Laccases were evaluated for their efficacy in degrading pharmaceutical substances across various categories, including analgesics, antibiotics, antiepileptics, antirheumatic drugs, cytostatics, hormones, anxiolytics, and sympatholytics.

enzyme wastewater laccases degradation biotransformation analgesics antibiotics

1. Introduction

The global pharmaceutical market has witnessed substantial growth, with a projected value of USD 1.48 trillion by 2022 [1]. Approximately one-third of pharmaceuticals in America end up as waste [2], leading to their detection in wastewater, groundwater, surface water, and even drinking water. Their presence raises concerns due to the documented negative environmental impact [3] and the potential emergence of new diseases through their untargeted administration [4][5][6][7][8].
Various methods, including chemical, physicochemical, or physical methods like membrane processes, advanced oxidation processes (e.g., ozonation, UV photolysis or UV/H2O2) adsorption, are employed for pharmaceutical removal. However, these methods present drawbacks such as the generation of toxic by-products in advanced oxidation processes [9][10][11][12][13], the disposal challenges associated with concentrated waste in membrane processes [14] or the difficulty of regenerating sorbents [15][16]. Biological processes, especially enzymatic processes, offer numerous advantages over physicochemical or alternative biological processes. They are inherently safer, generate less sludge, demand lower energy input, and operate without the need for additional nutrients. The resulting by-products are generally less or non-toxic, and these processes prove effective even at very low pollutant concentrations in wastewater [17][18]. Oxidoreductases, such as laccases, stand out as predominant enzymes in these processes [19][20][21][22], owing to their versatility and an active center accommodating a broad range of substrates [23]. Laccases offer the added advantage of requiring only molecular oxygen for catalyzing reactions. Moreover, their production is widespread across organisms like bacteria, fungi, and plants, with white-rot fungi, in particular, being highly efficient producers [24][25][26][27]. Fungal laccases exhibit high activity and interesting properties that are useful in bioremediation processes, such as substrate specificity, pH, and the optimum temperature of the enzyme, which are also useful in wastewater treatment plants (WWTPs) for their potential use in pollutant removal.
The removal of pharmaceutically active substances by enzymes such as laccases has received considerable attention, especially in recent years. Purified laccases were first tested on organic dyes and structurally simple substrates [19][20][21][22]. The current research deals with the use of laccase for the removal of pharmaceutically important compounds belonging to drug groups, such as analgesics, antibiotics, antiepileptics, antirheumatic drugs, cytostatics, hormones, anxiolytics and sympatholytics.

2. Analgesics

Analgesics, encompassing both non-opioid and opioid varieties, serve as pain-relieving medications. In this category, laccase has been tested against nonsteroidal anti-inflammatory drugs, specifically aspirin and ketoprofen.
Aspirin (acetylsalicylic acid), a non-steroidal anti-inflammatory drug used to manage pain and fever, poses a threat to the aquatic ecosystem due to its excessive use, serving as a significant source of environmental pollution with adverse effects on the reproduction and fetal development of aquatic organisms [28]. Aspirin concentrations in wastewater vary across locations, with measurements ranging from 0.4–0.7 µg/L in India [29] to 7.3 µg/L in Japan [30]. Yersinia enterocolitica laccase, expressed in Escherichia coli, demonstrated the complete biotransformation of aspirin within 24 h at pH 9.0 [31]. Al-sareji et al. [32] used laccase from Trametes versicolor (Sigma-Aldrich, St. Louis, MO, USA) and observed a 72% removal of aspirin after 6 h of enzymatic treatment. FTIR analysis of aspirin under various pH conditions revealed changes in the stretching of C=C bonds in the benzene ring and alternations in R-C=O bonds after 1 h of incubation.
Ketoprofen (2-(3-benzoylphenyl)propionic acid), a nonsteroidal anti-inflammatory drug used to treat muscle and joint pain, along with conditions such as arthritis, gout, and rheumatoid osteoarthritis, has been found at concentrations as low as 0.16 ng/L in Italy [33] or as high as 260 μg/L in India [29]. The increasing concern arises from the presence of enantiomers in the racemic mixture used in pharmaceutical formulations and potential ecotoxicological effects of transformation products on various organisms, including vertebrates, invertebrates, plants, and microorganisms [34]. T. versicolor laccase (Sigma-Aldrich) demonstrated the removal of 70% of ketoprofen within a 6-h reaction [32]. The primary focus of the study was conducted into the reaction mechanisms of the toxicity of degradation or biotransformation products after the enzyme-catalyzed reaction.
Ibuprofen (2-methyl-4-[2-methylpropyl]phenylacetic acid), the third most widely used non-steroidal anti-inflammatory drug globally [35], is employed to alleviate pain and treat inflammatory diseases. Its concentration in the water system ranges from 3.5 to 2200 mg/L, depending on the location [36][37], posing a potential hazard to human health [38]. In the study conducted by Zhang et al. [39], T. versicolor laccase (Spectrum Labs) removed 76% of ibuprofen in 8 h at an initial concentration of 2.5 mM determined via HPLC. The kinetic parameters of the laccase-catalyzed ibuprofen removal reaction were Km 6.21 mM and Vmax 2.56 M/h. Biotransformation products were analyzed via GC-MS in the positive ion mode and FTIR, revealing a putative pathway involving the hydroxylation of ibuprofen, decarboxylation of hydroxylated ibuprofen, and subsequent dehydration.
Despite the diverse laccase producers examined in the biotransformation of analgesics (aspirin, ketoprofen, and ibuprofen), there is potential for their application in WWTPs as they demonstrated efficacy at relatively high temperatures (35–45 °C) and within a pH range of 4.0–9.0. Laccase alone proved to be sufficiently efficient in biotransforming this group of drugs (refer to Table 1), although, thus far, only laccases with a high redox potential produced by fungi have been investigated (refer to Table 2).
Table 1. Laccases and their use in biotransformation of analgesics.
Drug Concentration
[mg/L]		 Laccase Producer Laccase Activity [U/L] Enzyme Reaction Degradation/Transformation Efficiency * Ref.
Aspirin 5.0 Yersinia enterocolitica 100 45 °C, pH 9.0, 24 h 100% (BT) [31]
25.0 Trametes versicolor 40 35 °C, pH 4.0, 6 h 72% (n.s.) [32]
Ketoprofen 25.0 40 35 °C, pH 4.0, 6 h 70% (n.s.)
Ibuprofen 515.7 29 40 °C, pH 7.0, 8 h 76% (BT) [39]
* BT—biotransformation, n.s.—not specified.
Table 2. Characterization of laccases used for the removal of pharmaceutical products.
Producer Redox Potential
(V vs. NHE)		 Biochemical Properties Ref.
pH Temperature (°C) Kinetic Parameters
Bacillus subtilis [B] 0.440 7.0 55 Km = 2070 μM [40][41]
Vmax = 6500 U/mL
(SYR)
Bacillus amyloliquefaciens [B] n.d. 4.0 65 Km = 436.8 μM [42][43]
(ABTS)
Yersinia enterocolitica a [B] 0.27–0.432 9.0 70 Km = 2070 μM [31][44]
Vmax = 6500 U/mL
(guaiacol)
Sclerotinia sclerotiorum [F] n.d. 4.0 60–70 Km = 85.8 μM [45]
Vmax = 18.64 U/mL
(ABTS)
Myceliophthora
Thermophila b [F]		 0.460 4.0 50 Km = 52.151 μM [46][47][48][49]
Vmax = 11.493 mU
(ABTS)
Paraconiothyrium variabile [F] n.d. 4.8 50 Km = 203 μM [50]
Vmax = 40 U/mg
[ABTS]
Moniliophthora roreri c [F] 0.58 4.0 n.d. Km = 24.13 μM [51]
(ABTS)
Echinodontium taxodii [F] n.d. 3.0 60 Km = 41.4 μM [52]
Vmax = 5.9 U/mL
(ABTS)
Trametes versicolor [F] 0.990 4.0 40 Km = 297 μM [53][54]
Vmax = 26.96 U/mg
(ABTS)
Recombinant laccase expressed in a Escherichia coli, b Aspergillus sp. or c Pichia pastoris. ABTS—2,2′-azino-di(3-ethyl-benzothiazoline sulfonic acid), B—bacteria, n.d.—not determined, F—fungi, NHE—normal hydrogen electrode, SYR—syringaldehyde.

3. Antibiotics

Antibiotics constitute one of the most widely prescribed and used drug categories globally. Due to their extensive usage and limited metabolism within the human body (with up to 70% excretion in an unchanged form), their release into the environment is steadily increasing, leading to elevated concentrations in water, soil, and sediments [55]. In raw wastewater (including hospital effluents) and treated wastewater, antibiotic concentrations exhibit a wide range, from a few ng/L to several tens of mg/L [56]. The rise of antibiotic resistance in clinically significant bacterial species poses a global public health challenge, necessitating the essential monitoring of antibiotic contamination in the environment.
Laccase efficacy has been extensively examined for various antibiotic classes, including sulfonamides, penicillins, fluoroquinolones, tetracyclines and others like trimethoprim. Antibiotics have been the focus of intensive studies concerning laccase, resulting in several reviews on this topic [57][58]. These studies encompass evaluations with crude laccase extracts or the cultivation of laccase-producing organisms in media containing antibiotics. In a study conducted by Becker et al. [59], the degradation of 38 antibiotics by laccase from T. versicolor (Sigma-Aldrich) was investigated, and their concentrations were assessed after the enzymatic reaction using HPLC. The efficiency of biotransformation varied based on the structural characteristics of the compounds. Notably, penicillins, such as amoxicillin (96.6%) and ampicillin (88.6%), fluoroquinolones (e.g., ofloxacin, ciprofloxacin, enrofloxacin, danofloxacin, and marbofloxacin) with removal rates ranging from 50.1 to 59.4%, and tetracyclines (oxytetracycline, chlortetracycline, doxycycline, and tetracycline) with removal rates ranging from 26.0 to 48.4%, were efficiently removed. The presence of the laccase mediator system (LMS) using syringaldehyde (SYR) increased the percentage of removal of most antibiotics to over 90%. However, the application of this mediator heightened the ecotoxicity of degradation products after the enzyme-mediated reaction, as indicated by a growth inhibition test with antibiotic-sensitive Bacillus subtilis and the Microtox test with Vibrio fischeri. It is noteworthy that laccase alone in a solution with antibiotics did not induce a similar increase in ecotoxicity. SYR likely forms derivatives in the presence of laccase, negatively impacting test organisms [59].
Sulfonamide antibiotics are widely used to treat livestock diseases and account for a high proportion of total antibiotic consumption worldwide. Laccase itself was not effective in the removal of sulfonamide antibiotics [52][59][60]. Sulfadimethoxine and sulfamonomethoxine were efficiently removed by the LMS using laccase from the white-rot fungus Perenniporia strain TFRI 707 and 2,2′-azino-di (3-ethyl-benzothiazoline sulfonic acid) (ABTS) or violuric acid (VA) as a redox mediator. Laccase from T. versicolor (Sigma-Aldrich) efficiently degraded 12 sulfonamide antibiotics with SYR (1 mM) [59]. In a study conducted by Alharbi et al. [61], the ability of T. versicolor laccase (Sigma-Aldrich) to degrade sulfamethoxazole at a concentration of 5 mg/L was tested, observing only 48% removal within 48 h. Shi et al. [52] observed 100% removal of the sulfonamide antibiotics sulfadiazine, sulfamethazine, and sulfamethoxazole by the LMS with SYR (1 mM) but no removal with laccase from Echinodontium taxodii itself. Weng et al. [60] found that deaniline and oxidative coupling are two detectable pathways for the conversion of sulfonamide antibiotics by the LMS. The coupling reaction of sulfonamide antibiotics with redox mediators was also determined via LC-MS in a study conducted by Shi et al. [52]. They observed the formation of 2,6-dimethoxybenzoquinone (2,6-DMBQ) with the tested sulfonamide antibiotics, where 2,6-DMBQ was formed after the oxidation of the natural mediators acetosyringone, SYR or syringic acid (SA) by E. taxodii laccase. A toxicity evaluation of the degradation products after treatment with T. versicolor laccase using the bioluminescent Photobacterium leiognathi (BLT-Screen) showed no toxic effect [61]. Furthermore, the degradation products of sulfonamide antibiotics did not have a negative effect on the growth of Staphylococcus aureus and E. coli [52], confirming the biotransformation of the antibiotic to a form without the original antibiotic effect.
Penicillins represent one of the most extensively used classes of antibiotics, primarily owing to their broad spectrum of clinical applications. Depending on their structure, penicillins can serve as substrates for laccase produced by both bacteria [62] and fungi [59]. The laccase from T. versicolor (Sigma-Aldrich) demonstrated efficient removal of amoxicillin and ampicillin (96.6 and 88.6%, respectively). Additionally, penicillin G, penicillin V, cloxacillin, and oxacillin were degraded using the LMS with SYR as a mediator at a concentration of 1 mM, resulting in removal rates ranging from 53.5 to 93.9% [59]. Moreover, laccase from B. subtilis, expressed in E. coli, exhibited the complete removal of ampicillin within two hours, as confirmed via HPLC analysis [62]. The researchers subsequently proposed a degradation mechanism featuring two putative pathways, wherein the cleavage of the β-lactate ring occurs during ampicillin degradation by laccase, leading to the subsequent loss of antibiotic activity. The degradation mechanism was corroborated by ecotoxicity assays utilizing B. subtilis and E. coli.
Fluoroquinolones represent a substantial group of broad-spectrum bactericidal agents, characterized by a common bicyclic nuclear structure related to 4-quinolone and are employed in the treatment of bacterial infections. In a study conducted by Zou et al. [63], the efficacy of laccase from T. versicolor (Sigma-Aldrich) in degrading fluoroquinolones, specifically norfloxacin, enrofloxacin, and moxifloxacin, was investigated. The laccase was immobilized in a magnetically modified biochore, primarily facilitating antibiotic removal through sorption—a common phenomenon observed with immobilized laccases [64][65]. While the presence of laccase slightly increased the removal percentage (by 0.7–2.6%), the addition of ABTS as a redox mediator further enhanced removal by 11.0–16.8%. Additionally, the removal of ciprofloxacin by laccase from T. versicolor (Sigma-Aldrich) was found to be effective in the presence of a redox mediator, either p-coumaric acid (p-CA) (57%) or HBT (81%). It is noteworthy that a higher percentage of removal was observed in the phosphate buffer compared to the wastewater sample (approximately 1.6 times less) [64]. The proposed putative biotransformation mechanism for fluoroquinolones by laccase was elucidated through LC-MS analysis.
The typical biotransformation mechanism of fluoroquinolones involves processes such as the loss of ethyl/ethylene, defluorination, and demethylation or decarboxylation. In a study conducted by Zou et al. [64], the laccase-mediated pretreatment of ciprofloxacin resulted in only a negligible inhibition of B. subtilis, S. aureus, and Pseudomonas aeruginosa. This observation affirms the positive impact of laccase in the biotransformation of antibiotics.
Tetracycline antibiotics as broad-spectrum antibiotics are widely used to treat human and animal diseases, making them the second most widely used antibiotics in the world [66]. Laccase produced by bacteria and expressed in E. coli, as well as laccase from Myceliophthora thermophila, expressed in Aspergillus sp., have been tested [65][67]. Laccase from Bacillus amyloliquefaciens, expressed in E. coli, was able to efficiently remove tetracycline antibiotics such as tetracycline, doxycycline, and tigecycline with the efficiency of 86.1, 96.5 and 81.0%, respectively [65]. Tetracycline was biotransformed to a level below the detection limit of the HPLC analysis after a 2-h catalyzed reaction with laccase of B. subtilis, expressed in E. coli [62]. Laccase from M. thermophila exhibited the complete removal of tetracycline using SYR as a redox mediator even in salt water [67]. The researchers proposed a putative mechanism of tetracycline biotransformation with two possible pathways, both leading to the opening of the tetracycline ring to form small acid molecules, resulting in a loss of antibiotic activity. In the case of tetracycline in the presence of laccase from B. amyloliquefaciens, the opening of the aromatic ring was observed in two of the three putative pathways, preceded by epimerization, demethylation, deamination, dehydrogenation, and hydroxylation in the second putative pathway or demethylation and dehydrogenation, dehydroxylation in the third pathway [65].
The same reactions, leading to the formation of degradation products with a smaller molecular size, have also been observed for tetracycline degraded by fungal laccase [67] and other tetracycline antibiotics such as doxycycline and tigecycline [65]. The loss of the antibiotic effect of tetracycline was also confirmed by ecotoxicity assays determined via the incubation of degradation products with B. subtilis and E. coli bacteria [62].
Trimethoprim (diaminopyrimidine) is an antibiotic used for treating and preventing urinary tract infections. In a study conducted by Alharbi et al. [61], the efficacy of laccase from T. versicolor (Sigma-Aldrich) in degrading trimethoprim at a concentration of 5 mg/L was investigated. The results demonstrated a 95% removal of this drug within 48 h. LC-MS was used in the study to identify degradation products, but none were detected in either the positive or negative scanning mode. Furthermore, testing against the bioluminescent P. leiognathi (BLT-Screen) after the enzyme-catalyzed reaction revealed no toxic effect, indicating that the laccase-catalyzed reaction did not lead to the formation of toxic products [61].
In summary, it can be concluded that bacterial or fungal laccase, without a redox mediator, exhibited efficient removal of penicillins, fluoroquinolones, and tetracyclines, with degradation involving the opening of the antibiotic’s aromatic rings. The degradation percentage varied based on the antibiotic’s structure and the presence of electron-donating or electron-withdrawing functional groups (Table 3). An enhanced degradation efficiency was observed with the use of the LMS employing SYR, HBT, or ABTS [59][60][64][67]. Sulfonamide antibiotics proved to be the most resistant to laccase-catalyzed degradation, requiring the presence of a redox mediator for a decrease in concentration. Putative degradation pathways indicated biotransformation through crosslinking with a redox mediator [52][60]. Importantly, the antibiotic effect was eliminated in all studied cases, but the choice of a mediator in the LMS is crucial to avoid the production of toxic products [62][63][65][67].
Table 3. Laccases and their use in degradation/ biotransformation of antibiotics.
Drug Concentration
[mg/L]		 Laccase Producer Laccase Activity [U/L] Concentration of Redox Mediator [mM] Enzyme Reaction Degradation/Transformation Efficiency Ref.
Sulfamonomethoxine 50 Perenniporia
TFRI 707		 600 ABTS [1.0] 30 °C, pH 4.0, 0.5 h 100% (BT) [60]
VA [1.0] 100% (BT)
0.01 Trametes versicolor n.s. - 25 °C, pH 7.0, 24 h 5.4% (n.s.) [59]
SYR [1.0] 96.1% (n.s.)
Sulfadimethoxine 50 Perenniporia
TFRI 707		 600 ABTS [1.0] 30 °C, pH 4.0, 0.5 h 100% (BT) [60]
VA [1.0] 100% (BT)
Sulfadiazine 0.01 Trametes versicolor n.s. - 25 °C, pH 7.0, 24 h 11.2% (n.s.) [59]
SYR [1.0] 99.7% (n.s.)
50 Echinodontium taxodii 200 SA [1.0] 30 °C, pH 5.0, 0.5 h 100% (BT) [52]
Sulfamethoxazole 50 Echinodontium taxodii 200 SA [1.0] 30 °C, pH 5.0, 0.5 h 100% (BT) [52]
5.0 Trametes versicolor 430–460 - 25 °C, pH 6.8–6.9, 8 h 56% (n.s.) [61]
0.01 Trametes versicolor n.s. - 25 °C, pH 7.0, 24 h 14.2% (n.s.) [59]
SYR [1.0] 97.2% (n.s.)
Tetracycline 0.01 Trametes versicolor n.s. - 25 °C, pH 7.0, 24 h 26.0% (n.s.) [59]
SYR [0.01] 85.2% (n.s.)
100 Bacillus subtilis 34.3 - 25 °C, pH 5.5, 2 h 100% (D) [62]
100 Bacillus amyloliquefaciens 2000 - 30 °C, pH 7.0, 2 h 86.1% (D) [65]
0.002 Myceliophthora thermophila 200 SA [0.001] 15 °C, pH 8.0, 2 h 100% (D) [67]
Doxycycline 100 Bacillus amyloliquefaciens 500 - 30 °C, pH 7.0, 2 h 96.5% (D) [65]
0.01 Trametes versicolor n.s. - 25 °C, pH 7.0, 24 h 30.4% (n.s.) [59]
SYR [0.01] 89.1% (n.s.)
Tigecycline 100 Bacillus amyloliquefaciens 500 - 30 °C, pH 7.0, 2 h 81.0% (D) [65]
Norfloxacin 0.01 Trametes versicolor n.s. - 25 °C, pH 7.0, 24 h 58.1% (n.s.) [59]
SYR [1.0] 82.4% (n.s.)
Enrofloxacin 0.01 Trametes versicolor n.s. - 25 °C, pH 7.0, 24 h 50.1% (n.s.) [59]
SYR [1.0] 76.6% (n.s.)
Ciprofloxacin 10 Trametes versicolor n.s. p-CA [3.0] 45 °C, pH 6.8, 6 h 57% (n.s.) [64]
HBT [3.0] 81% (n.s.)
Amoxicillin 0.01 Trametes versicolor n.s. - 25 °C, pH 7.0, 24 h 96.6% (n.s.) [59]
SYR [1.0] 94.7% (n.s.)
Ampicillin 0.01 Trametes versicolor n.s. - 25 °C, pH 7.0, 24 h 88.6% (n.s.) [59]
SYR [1.0] 99.9% (n.s.)
100 Bacillus subtilis 34.3 - 25 °C, pH 5.5, 2 h 100% (D) [62]
Trimethoprim 5.0 Trametes versicolor 430–460 - 25 °C, pH 6.8–6.9, 24 h 95% (n.s.) [61]
0.01 n.s. - 25 °C, pH 7.0, 24 h 26.6% (n.s.) [59]
SYR [1.0] 66.8% (n.s.)
ATBS—2,2′-azino-di[3-ethyl-benzothiazoline sulfonic acid], BT—biotransformation, D—degradation, HBT—1-hydroxybenzotriazole, VA—violuric acid, p-CA—p-coumaric acid, SYR—syringaldehyde, SA—syringic acid, n.s.—not specified.

References

  1. Statista. Available online: https://www.statista.com/statistics/263102/pharmaceutical-market-worldwide-revenue-since-2001/ (accessed on 22 December 2023).
  2. Product Stewardship Council. Webinar. Global Best Practices for Drug Take-Back Programs—Product Stewardship Institute. Available online: https://www.productstewardship.us/page/20180607_GBPFDTBP (accessed on 22 December 2023).
  3. López-Serna, R.; Petrović, M.; Barceló, D. Occurrence and distribution of multi-class pharmaceuticals and their active metabolites and transformation products in the Ebro River basin (NE Spain). Sci. Total Environ. 2012, 440, 280–289.
  4. Mons, M.N.; van Genderen, J.; van Dijk-Looijaard, A.M. Inventory on the Presence of Pharmaceuticals in Dutch Water; KIWA: Nieuwegein, The Netherlands, 2000; Available online: https://www.riwa-rijn.org/wp-content/uploads/2015/06/Inventory_presence_pharmas_dutchwaters.pdf (accessed on 22 December 2023).
  5. Miao, X.S.; Yang, J.J.; Metcalfe, C.D. Carbamazepine and its metabolites in a municipal wastewater treatment plant. Environ. Sci. Technol. 2005, 39, 7469–7475.
  6. Morasch, B.; Bonvin, F.; Reiser, H.; Grandjean, D.; De Alencastro, L.F.; Perazzolo, C.; Chevre, N.; Kohn, T. Occurrence and fate of micropollutants in the Vidy Bay of Lake Geneva, Switzerland. Part II: Micropollutant removal between wastewater and raw drinking water. Environ. Toxicol. Chem. 2010, 29, 1658–1668.
  7. Martín, J.; Camacho-Muñoz, D.; Santos, J.L.; Aparicio, I.; Alonso, E. Occurrence and ecotoxicological risk assessment of 14 cytostatic drugs in wastewater. Water Air Soil Pollut. 2014, 225, 1896.
  8. Santana-Viera, S.; Hernández-Arencibia, P.; Sosa-Ferrera, Z.; Santana-Rodríguez, J.J. Simultaneous and systematic analysis of cytostatic drugs in wastewater samples by ultra-high performance liquid chromatography tandem mass spectrometry. J. Chromatogr. B 2019, 1110–1111, 124–132.
  9. Alharbi, S.K.; Price, W.E.; Kang, J.; Fujioka, T.; Nghiem, L.D. Ozonation of carbamazepine, diclofenac, sulfamethoxazole and trimethoprim and formation of major oxidation products. Desalination Water Treat. 2016, 57, 29340–29351.
  10. Alharbi, S.K.; Kang, J.; Nghiem, L.D.; van de Merwe, J.P.; Leusch, F.D.L.; Price, W.E. Photolysis and UV/H2O2 of diclofenac, sulfamethoxazole, carbamazepine, and trimethoprim: Identification of their major degradation products by ESI–LC–MS and assessment of the toxicity of reaction mixtures. Process Saf. Environ. Protect. 2017, 112, 222–234.
  11. Kudlek, E. Decomposition of contaminants of emerging concern in advanced oxidation processes. Water 2018, 10, 955.
  12. Oluwole, A.O.; Omotola, E.O.; Olatunji, O.S. Pharmaceuticals and personal care products in water and wastewater: A review of treatment processes and use of photocatalyst immobilized on functionalized carbon in AOP degradation. BMC Chem. 2020, 14, 62.
  13. Yehya, T.; Favier, L.; Audonnet, F.; Fayad, N.; Bahry, H.; Bahrim, G.E.; Vial, C. Towards a better understanding of the removal of carbamazepine by Ankistrodesmus braunii: Investigation of some key parameters. Appl. Sci. 2020, 10, 8034.
  14. Ji, C.; Hou, J.; Wang, K.; Zhang, Y.; Chen, V. Biocatalytic degradation of carbamazepine with immobilized laccase-mediator membrane hybrid reactor. J. Membr. Sci. 2016, 502, 11–20.
  15. Bhattacharya, S.; Banerjee, P.; Das, P.; Bhowal, A.; Majumder, S.K.; Ghosh, P. Erratum: Removal of aqueous carbamazepine using graphene oxide nanoplatelets: Process modelling and optimization. Sustain. Environ. Res. 2020, 30, 25.
  16. Al-Mashaqbeh, O.A.; Snow, D.D.; Alsafadi, D.A.; Alsalhi, L.Z.; Bartelt-Hunt, S.L. Removal of carbamazepine onto modified zeolitic tuff in different water matrices: Batch and continuous flow experiments. Water 2021, 13, 1084.
  17. Pereira, C.S.; Kelbert, M.; Daronch, N.A.; Michels, C.; de Oliveira, D.; Soares, H.M. Potential of enzymatic process as an innovative technology to remove anticancer drugs in wastewater. Appl. Microbiol. Biotechnol. 2020, 104, 23–31.
  18. Morsi, R.; Bilal, M.; Iqbal, H.M.N.; Ashraf, S.S. Laccases and peroxidases: The smart, greener and futuristic biocatalytic tools to mitigate recalcitrant emerging pollutants. Sci. Total Environ. 2020, 714, 136572.
  19. Chmelová, D.; Ondrejovič, M. Effect of metal ions on triphenylmethane dye decolorization by laccase from Trametes versicolor. Nova Biotechnol. Chim. 2015, 14, 191–200.
  20. Legerská, B.; Chmelová, D.; Ondrejovič, M. Degradation of synthetic dyes by laccases—A mini-review. Nova Biotechnol. Chim. 2016, 15, 90–106.
  21. Legerská, B.; Chmelová, D.; Ondrejovič, M. Azonaphthalene dyes decolorization and detoxification by laccase from Trametes versicolor. Nova Biotechnol. Chim. 2018, 17, 172–180.
  22. Legerská, B.; Chmelová, D.; Ondrejovič, M. Decolourization and detoxification of monoazo dyes by laccase from the white-rot fungus Trametes versicolor. J. Biotechnol. 2018, 285, 84–90.
  23. Varga, B.; Somogyi, V.; Meiczinger, M.; Kováts, N.; Domokos, E. Enzymatic treatment and subsequent toxicity of organic micropollutants using oxidoreductases—A review. J. Clean. Prod. 2019, 221, 306–322.
  24. Chmelová, D.; Ondrejovič, M. Purification and characterization of extracellular laccase produced by Ceriporiopsis subvermispora and decolorization of triphenylmethane dyes. J. Basic Microbiol. 2016, 56, 1173–1182.
  25. Hazuchová, M.; Chmelová, D.; Ondrejovič, M. The optimization of propagation medium for the increase of laccase production by the white-rot fungus Pleurotus ostreatus. Nova Biotechnol. Chim. 2017, 16, 113–123.
  26. Pecková, V.; Legerská, B.; Chmelová, D.; Horník, M.; Ondrejovič, M. Comparison of efficiency for monoazo dye removal by different species of white-rot fungi. Int. J. Environ. Sci. Technol. 2020, 18, 21–30.
  27. Chmelová, D.; Legerská, B.; Kunstová, J.; Ondrejovič, M.; Miertuš, S. The production of laccases by white-rot fungi under solid-state fermentation conditions. World J. Microbiol. Biotechnol. 2022, 38, 21.
  28. Spina, F.; Cordero, C.; Sgorbini, B.; Schilirò, T.; Gilli, G.; Bicchi, C.; Varese, G.C. Endocrine disrupting chemicals in municipal wastewaters: Effective degradation and detoxification by fungal laccases. Chem. Eng. Trans. 2013, 32, 391–396.
  29. Praveenkumarreddy, Y.; Vimalkumar, K.; Ramaswamy, B.R.; Kumar, V.; Singhal, R.K.; Basu, H.; Gopal, C.M.; Vandana, K.E.; Bhat, K.; Udayashankar, H.N.; et al. Assessment of nonsteroidal anti-inflammatory drugs from selected wastewater treatment plants of Southwestern India. Emerg. Contam. 2021, 7, 43–51.
  30. Nakada, N.; Tanishima, T.; Shinohara, H.; Kiri, K.; Takada, H. Pharmaceutical chemicals and endocrine disrupters in municipal wastewater in Tokyo and their removal during activated sludge treatment. Water Res. 2006, 40, 3297–3303.
  31. Singh, D.; Rawat, S.; Waseem, M.; Gupta, S.; Lynn, A.; Nitin, M.; Ramchiary, N.; Sharma, K.K. Molecular modeling and simulation studies of recombinant laccase from Yersinia enterocolitica suggests significant role in the biotransformation of non-steroidal anti-inflammatory drugs. Biochem. Biophys. Res. Commun. 2016, 469, 306–312.
  32. Al-sareji, O.J.; Meiczniger, M.; Salman, J.M.; Al-Juboori, R.A.; Hashim, K.S.; Somogyi, V.; Jakab, M. Ketoprofen and aspirin removal by laccase immobilized on date stones. Chemosphere 2023, 311, 137133.
  33. Papagiannaki, D.; Morgillo, S.; Bocina, G.; Calza, P.; Binetti, R. Occurrence and human health risk assessment of pharmaceuticals and hormones in drinking water sources in the metropolitan area of Turin in Italy. Toxics 2021, 9, 88.
  34. Tyumina, E.; Subbotina, M.; Polygalov, M.; Tyan, S.; Ivshina, I. Ketoprofen as an emerging contaminant: Occurrence, ecotoxicity and removal. Front. Microbiol. 2023, 14, 1200108.
  35. Marchlewicz, A.; Guzik, U.; Wojcieszyńska, D. Over-the-counter monocyclic non-steroidal anti-inflammatory drugs in environment–sources, risks, biodegradation. Water Air Soil Pollut. 2015, 226, 355.
  36. Huppert, N.; Würtele, M.; Hahn, H.H. Determination of the plasticizer N-butylbenzenesulfonamide and the pharmaceutical Ibuprofen in wastewater using solid phase microextraction . Fresenius’ J. Anal. Chem. 1998, 362, 529–536.
  37. Fang, T.-H.; Nan, F.-H.; Chin, T.-S.; Feng, H.-M. The occurrence and distribution of pharmaceutical compounds in the effluents of a major sewage treatment plant in Northern Taiwan and the receiving coastal waters. Mar. Pollut. Bull. 2012, 64, 1435–1444.
  38. Chopra, S.; Kumar, D. Ibuprofen as an emerging organic contaminant in environment, distribution and remediation. Heliyon 2020, 6, 04087.
  39. Zhang, J.; Cai, Q.; Chen, J.; Lu, Y.; Ren, X.; Lio, Q.; Wen, L.; Mateen, M. Enhanced removal of ibuprofen in water using dynamic dialysis of laccase catalysis. J. Water Process Eng. 2022, 47, 102791.
  40. Cambria, M.T.; Minniti, Z.; Librando, V.; Cambria, A. Degradation of polycyclic aromatic hydrocarbons by Rigidoporus lignosus and its laccase in the presence of redox mediators. Appl. Biochem. Biotechnol. 2018, 149, 1–8.
  41. Basheer, S.; Rashid, N.; Akram, M.S.; Akhtar, M. A highly stable laccase from Bacillus subtilis strain R5: Gene cloning and characterization. Biosci. Biotechnol. Biochem. 2019, 83, 436–445.
  42. Lončar, N.; Božić, N.; Lopez-Santin, J.; Vujčić, Z. Bacillus amyloliquefaciens laccase—From soil bacteria to recombinant enzyme for wastewater decolorization. Bioresour. Technol. 2013, 147, 177–183.
  43. Wang, J.; Yu, S.; Li, X.; Feng, F.; Lu, L. High-level expression of Bacillus amyloliquefaciens laccase and construction of its chimeric variant with improved stability by domain substitution. Bioprocess Biosyst. Eng. 2020, 43, 403–411.
  44. Kumar, A.; Ahlawat, S.; Mohan, H.; Sharma, K.K. Stabilization–destabilization and redox properties of laccases from medicinal mushroom Ganoderma lucidum and human pathogen Yersinia enterocolitica. Int. J. Biol. Macromol. 2021, 167, 369–381.
  45. Mot, A.C.; Parvu, M.; Damian, G.; Irimie, F.D.; Darula, Z.; Medzihradszky, L.F.; Brem, B.; Silaghi-Dumitrescu, R. A “yellow” laccase with “blue” spectroscopic features, from Sclerotinia sclerotiorum. Process Biochem. 2012, 47, 968–975.
  46. Hollmann, F.; Gumulya, Y.; Tölle, C.; Liese, A.; Thum, O. Evaluation of the laccase from Myceliophthora thermophila as industrial biocatalyst for polymerization reactions. Macromolecules 2008, 41, 8520–8524.
  47. Lloret, L.; Eibes, G.; Lú-Chau, T.A.; Moreira, M.T.; Feijoo, G.; Lema, J.M. Laccase-catalyzed degradation of anti-inflammatories and estrogens. Biochem. Eng. J. 2010, 51, 124–131.
  48. Lucas, M.F.; Monza, E.; Jorgensen, L.J.; Ernst, H.A.; Piontek, K.; Bjerrum, M.J.; Martinez, A.T.; Camarero, S.; Guallar, V. Simulating substrate recognition and oxidation in laccases: From description to design. J. Chem. Theory Comput. 2017, 13, 1462–1467.
  49. Chan, C.J.; Zhang, B.; Martinez, M.; Kuruba, B.; Brozik, J.; Kang, C.; Zhang, X. Structural studies of Myceliophthora thermophila laccase in the presence of deep eutectic solvents. Enzym. Microb. Technol. 2021, 150, 109890.
  50. Forootanfar, H.; Faramarzi, M.A.; Shahverdi, A.R.; Yazdi, M.T. Purification and biochemical characterization of extracellular laccase from the ascomycete Paraconiothyrium variabile. Bioresour. Technol. 2011, 102, 1808–1814.
  51. Bronikowski, A.; Hagedoorn, P.L.; Koschorreck, K.; Urlacher, V.B. Expression of a new laccase from Moniliophthora roreri at high levels in Pichia pastoris and its potential application in micropollutant degradation. AMB Express 2017, 7, 73.
  52. Shi, L.; Ma, F.; Han, Y.; Zhang, X.; Yu, H. Removal of sulfonamide antibiotics by oriented immobilized laccase on Fe3O4 nanoparticles with natural mediators. J. Hazard. Mater. 2014, 279, 203–211.
  53. Ivnitski, D.; Atanassov, P. Electrochemical studies of intramolecular electron transfer in laccase from Trametes versicolor. Electroanalysis 2007, 19, 2307–2313.
  54. Aydemir, T.; Güler, S. Characterization and immobilization of Trametes versicolor laccase on magnetic chitosan–clay composite beads for phenol removal. Artif. Cells Nanomed. Biotechnol. 2015, 43, 425–432.
  55. Kümmerer, K. Antibiotics in the aquatic environment—A review—Part I. Chemosphere 2009, 75, 417–434.
  56. Mutuku, C.; Gazdag, Z.; Melegh, S. Occurrence of antibiotics and bacterial resistance genes in wastewater: Resistance mechanisms and antimicrobial resistance control approaches. World J. Microbiol. Biotechnol. 2022, 38, 152.
  57. Yang, J.; Li, W.; Ng, T.B.; Deng, X.; Lin, J.; Ye, X. Laccases: Production, expression regulation, and applications in pharmaceutical biodegradation. Front. Microbiol. 2017, 8, 832.
  58. Sahay, R. Fungal laccase mediator and its biocatalytic potential applications: A review. Biotechnol. Apl. 2020, 38, 1101–1109.
  59. Becker, D.; Giustina, S.V.D.; Rodriquez-Mozaz, S.; Schoevaart, R.; Barceló, D.; de Cazes, M.; Belleville, M.-P.; Sanchez-Marcano, J.; de Gunzburg, J.; Couillerot, O.; et al. Removal of antibiotics in wastewater by enzymatic treatment with fungal laccase—Degradation of compounds does not always eliminate toxicity. Bioresour. Technol. 2016, 219, 500–509.
  60. Weng, S.S.; Ku, K.-L.; Lai, H.-T. The implication of mediators for enhancement of laccase oxidation of sulfonamide antibiotics. Bioresour. Technol. 2012, 113, 259–264.
  61. Alharbi, S.K.; Nghiem, L.D.; van de Merwe, J.P.; Leusch, F.D.L.; Asif, M.B.; Hai, F.I.; Price, W.E. Degradation of diclofenac, trimethoprim, carbamazepine, and sulfamethoxazole by laccase from Trametes versicolor: Transformation products and toxicity of treated effluent. Biocatal. Biotransformation 2019, 37, 399–408.
  62. Zhang, C.; You, S.; Zhang, J.; Qi, W.; Su, R.; He, Z. An effective in-situ method for laccase immobilization: Excellent activity, effective antibiotic removal rate and low potential ecological risk for degradation products. Bioresour. Technol. 2020, 308, 123271.
  63. Zou, M.; Tian, W.; Chu, M.; Lu, Z.; Liu, B.; Xu, D. Magnetically separable laccase-biochar composite enable highly efficient adsorption-degradation of quinolone antibiotics: Immobilization, removal, performance and mechanisms. Sci. Total Environ. 2023, 879, 163057.
  64. Jafari-Nodoushan, H.; Fazeli, M.R.; Faramarzi, M.A.; Samadi, N. Hierarchically-structured laccase@Ni32 hybrid nanoflowers for antibiotic degradation: Application in real wastewater effluent and toxicity evaluation. Int. J. Biol. Macromol. 2023, 234, 123574.
  65. Han, Z.; Wang, H.; Zheng, J.; Wang, S.; Yu, S.; Lu, L. Ultrafast synthesis of laccase-copper phosphate hybrid nanoflowers for efficient degradation of tetracycline antibiotics. Environ. Res. 2023, 216, 114690.
  66. Scaria, J.; Anupama, K.V.; Nidheesh, P.V. Tetracyclines in the environment: An overview on the occurrence, fate, toxicity, detection, removal methods, and sludge management. Sci. Total Environ. 2021, 771, 145291.
  67. Wang, X.; Meng, F.; Zhang, B. Elimination of tetracyclines in seawater by laccase-mediator system. Chemosphere 2023, 333, 138916.
More
© Text is available under the terms and conditions of the Creative Commons Attribution (CC BY) license; additional terms may apply. By using this site, you agree to the Terms and Conditions and Privacy Policy.
Upload a video for this entry
Information
Subjects: Biochemistry & Molecular Biology
Contributors MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register :
Daniela Chmelová
,
Miroslav Ondrejovič
,
Stanislav Miertuš
View Times: 138
Revisions: 2 times (View History)
Update Date: 28 Feb 2024
Table of Contents
    1000/1000
    Hot Most Recent
    Video Production Service
    Feedback