Enzymatic treatment of estrogens and estrogen glucuronide

Tanaka, Takaaki; Tamura, Toshiyuki; Ishizaki, Yuuichi; Kawasaki, Akito; Kawase, Tomokazu; Teraguchi, Masahiro; Taniguchi, Masayuki

doi:10.1016/s1001-0742(08)62332-3

Cited by 21 publications

(18 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Indeed, the oxidation of the oestrogens estrone, 17β‐estradiol and 17α‐ethynylestradiol by a fungal laccase from Trametes sp. Ha1 has been described (Tanaka et al ., ). Besides, a treatment system was developed that comprised the laccase and a β‐D‐glucuronidase to degrade the 17β‐estradiol 3‐(β‐ d ‐glucuronide), efficiently eliminating this compound and its intermediate 17β‐estradiol.…”

Section: Laccases In the Cutting Edge Of Biotechnologymentioning

confidence: 97%

Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology

Maté

Alcalde

2016

Microbial Biotechnology

439

228

View full text Add to dashboard Cite

SummaryLaccases are multicopper containing enzymes capable of performing one electron oxidation of a broad range of substrates. Using molecular oxygen as the final electron acceptor, they release only water as a by‐product, and as such, laccases are eco‐friendly, versatile biocatalysts that have generated an enormous biotechnological interest. Indeed, this group of enzymes has been used in different industrial fields for very diverse purposes, from food additive and beverage processing to biomedical diagnosis, and as cross‐linking agents for furniture construction or in the production of biofuels. Laccases have also been studied intensely in nanobiotechnology for the development of implantable biosensors and biofuel cells. Moreover, their capacity to transform complex xenobiotics makes them useful biocatalysts in enzymatic bioremediation. This review summarizes the most significant recent advances in the use of laccases and their future perspectives in biotechnology.

show abstract

Section: Laccases In the Cutting Edge Of Biotechnologymentioning

confidence: 97%

Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology

Maté

Alcalde

2016

Microbial Biotechnology

439

228

View full text Add to dashboard Cite

show abstract

“…Indeed, several previous researchers have studied the transformation of E1, E2, and EE2 by ligninolytic enzymes, being laccase (EC 1.10.3.2, benzenodiol/oxygen oxidoreductase) the most widely applied biocatalyst due to its potential ability to degrade recalcitrant compounds and its simple catalytic mechanism using oxygen as final electron acceptor . Previous works reported significant removal yields of both the target compounds and their estrogenic activities. ,,,− Nevertheless, most of those experiments were conducted at relatively high concentrations in synthetic media, whereas only a few investigations assessed the removal of estrogens in real wastewaters . Furthermore, research has been focused in the operation in batch mode, whereas relative low effort has been devoted for its implementation in a continuous process.…”

Section: Introductionmentioning

confidence: 99%

Removal of Estrogenic Compounds from Filtered Secondary Wastewater Effluent in a Continuous Enzymatic Membrane Reactor. Identification of Biotransformation Products

Lloret

Eibes

Moreira

et al. 2013

Environ. Sci. Technol.

102

View full text Add to dashboard Cite

In the present study, a novel and efficient technology based on the use of an oxidative enzyme was developed to perform the continuous removal of estrogenic compounds from polluted wastewaters. A 2 L enzymatic membrane reactor (EMR) was successfully operated for 100 h with minimal requirements of laccase for the transformation of estrone (E1), 17β-estradiol (E2), and 17α-ethinylestradiol (EE2)from both buffer solution and real wastewater (filtered secondary effluent). When the experiments were performed at high and low concentrations of the target compounds, 4 mg/L and 100 μg/L, not only high removal yields (80-100%) but also outstanding reduction of estrogenicity (about 84-95%) were attained. When the EMR was applied for the treatment of municipal wastewaters with real environmental concentrations of the different compounds (0.29-1.52 ng/L), excellent results were also achieved indicating the high efficiency and potential of the enzymatic reactor system. A second goal of this study relied on the identification of the transformation products to elucidate the catalytic mechanism of estrogens' transformation by laccase. The formation of dimers and trimers of E1, E2, and EE2, as well as the decomposition of E2 into E1 by laccase-catalyzed treatment, has been demonstrated by liquid chromatography atmospheric pressure chemical ionization (LC-APCI) analysis and confirmed by determination of accurate masses through liquid chromatography electrospray time-of-flight mass spectrometry (LC-ESI-TOF). Dimeric products of E2 and EE2 were found even when operating at environmental concentrations. Moreover, the reaction pathways of laccase-catalyzed transformation of E2 were proposed.

show abstract

“…Laccase oxidizes phenolic moieties; however, this phenolic site at the C-3 position in E2-3G molecule is blocked by the conjugate moiety preventing its oxidation. 39 Abiotic oxidation of an estrogen in soils is a surface process mediated by manganese oxides, 34 which ranged from 154 to 255 μg g −1 for the soils of this study.…”

Section: ■ Results and Discussionmentioning

confidence: 88%

Fate and Transformation of an Estrogen Conjugate and Its Metabolites in Agricultural Soils

Shrestha

Casey

Hakk³

et al. 2012

Environ. Sci. Technol.

View full text Add to dashboard Cite

In the environment, conjugated estrogens are nontoxic but may hydrolyze to their potent unconjugated, 'free' forms. Compared to free estrogens, conjugated estrogens would be more mobile in the environment because of their higher water solubility. To identify the fate of a conjugated estrogen in natural agricultural soils, batch experiments were conducted with a (14)C labeled prototype conjugate, 17β-estradiol-3-glucuronide (E2-3G). Initially, aqueous dissipation was dominated by biological hydrolysis of E2-3G and its oxidized metabolite, estrone glucuronide (E1-3G), both of which were transformed into the free estrogens, 17β-estradiol (E2) and estrone (E1), respectively. Following hydrolysis, hydrophobic sorption interactions of E2 and E1 dominated. Depending on soil organic matter contents, dissolved E2-3G persisted from 1-14 d, which was much longer than what others reported for free estrogens (generally <24 h). Biodegradation rate constants of E2-3G were smaller in the subsoil (0.01-0.02 h(-1)) compared to topsoil (0.2-0.4 h(-1)). Field observations supported our laboratory findings where significant concentrations (425 ng L(-1)) of intact E2-3G were detected in groundwater (6.5-8.1 m deep) near a swine (Sus scrofa domesticus) farm. This study provides evidence that conjugate estrogens may be a significant source of free estrogens to surface water and groundwater.

show abstract

Enzymatic treatment of estrogens and estrogen glucuronide

Cited by 21 publications

References 18 publications

Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology

Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology

Removal of Estrogenic Compounds from Filtered Secondary Wastewater Effluent in a Continuous Enzymatic Membrane Reactor. Identification of Biotransformation Products

Fate and Transformation of an Estrogen Conjugate and Its Metabolites in Agricultural Soils

Contact Info

Product

Resources

About