Laccases: The Biocatalyst with Industrial and Biotechnological Applications

Thakur, Shilpi; Patel, Hasmukh S.; Gupte, Shilpa; Gupte, Akshaya

doi:10.1007/978-94-007-2214-9_16

Cited by 7 publications

(13 citation statements)

References 174 publications

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“…Laccases (EC 1.10.3.2) are a promising group of oxidoreductases that have high activity in oxidizing phenolic compounds and arylamine, including phenols, polyphenols, methoxy‐substituted phenols, aromatic and aliphatic amines, by using molecular oxygen as the electron acceptor without the need for cofactors (Strong & Claus, ; Thakur, Patel, Gupte, & Gupte, ). Prior studies have demonstrated the use of laccases for effective degradation of emerging contaminants, such as endocrine disruptors (bisphenol A [Zdarta, Antecka et al, ] and triclosan [Le et al, ]), pharmaceuticals (sulfamethoxazole [Margot, Copin, von Gunten, Barry, & Holliger, ] and naproxen [Tran, Urase, & Kusakabe, ]), and pesticides (bromofenoxim [Torres‐Duarte, Roman, Tinoco, & Vazquez‐Duhalt, ] and carbofuran [Wang, Liu, Yao, Zhang, & Bao, ]).…”

Section: Introductionmentioning

confidence: 99%

Biocatalytic properties of cell surface display laccase for degradation of emerging contaminant acetaminophen in water reclamation

Chen

Wei

2019

Biotech & Bioengineering

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The surface display laccase (SDL) biocatalyst, where the enzyme laccase is displayed on the surface of biological cells through synthetic biology, provides a new opportunity to develop sustainable technologies for removal of emerging contaminants from wastewater. This study vigorously characterized biocatalytic properties of the SDL in comparison to free laccase in removing emerging contaminant acetaminophen (APAP), with the aim to understand the effect of surface display on enzyme functionality and identify the strategy to overcome the potential limitation. The SDL could effectively remove APAP. Adding redox mediators substantially improved the removal efficiency. The Michaelis–Menten kinetic analysis showed that the redox mediator 2,2‐azinobis‐3‐ethylbenzothiazoline‐6‐sulfonate could overcome the limitation of APAP accessing the active site of laccase in the SDL biocatalyst. The APAP removal rate catalyzed by the SDL in real secondary wastewater effluent was higher than that in acetate buffer; comprehensive enzyme kinetic analysis provided clear evidence that there were redox mediating compounds in the wastewater. Analysis of transformation products revealed that surface display did not change laccase functionality in terms of APAP transformation mechanism. In addition, the SDL retained 88% of the initial activity after six repeated APAP biotransformation reactions. Results from this study provide a scientific basis for developing and implementing SDL as an innovative biocatalytic material for contaminant treatment applications.

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Section: Introductionmentioning

confidence: 99%

Biocatalytic properties of cell surface display laccase for degradation of emerging contaminant acetaminophen in water reclamation

Chen

Wei

2019

Biotech & Bioengineering

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“…Laccases (benzenediol: oxygen oxidoreductases, EC 1.10.3.2) are blue multi-copper oxidases that are involved in the oxidation of numerous aromatic substrates together with the reduction in molecular oxygen to water [ 1 ]. Laccases are distributed in a wide range of organisms [ 2 ], including plants, fungi, insects and bacteria and have been associated with diverse biological processes. Generally, laccases are classified into three categories according to the source, its physiological conditions and functions: (1) polymerization of monomers; (2) degradation of polymers; and (3) aromatic ring cleavage [ 3 ].…”

Section: Introductionmentioning

confidence: 99%

Importance of a Laccase Gene (Lcc1) in the Development of Ganoderma tsugae

Jin

Feng

You

et al. 2018

IJMS

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In this study, a novel laccase gene (Lcc1) from Ganoderma tsugae was isolated and its functions were characterized in detail. The results showed that Lcc1 has the highest expression activity during mycelium development and fruit body maturation based on the analysis of Lcc1 RNA transcripts at different developmental stages of G. tsugae. To investigate the exact contribution of Lcc1 to mycelium and fruit body development in G. tsugae, Lcc1 transgenic strains were constructed by targeted gene replacement and over-expression approaches. The results showed that the lignin degradation rate in Lcc1 deletion mutant was much lower than the degradation efficiency of the wild-type (WT), over-expression and rescue strains. The lignin degradation activity of G. tsugae is dependent on Lcc1 and the deletion of Lcc1 exerted detrimental influences on the development of mycelium branch. Furthermore, the study uncovered that Lcc1 deletion mutants generated much shorter pale grey fruit bodies, suggesting that Lcc1 contributes directly to pigmentation and stipe elongation during fruit body development in G. tsugae. The information obtained in this study provides a novel and mechanistic insight into the specific role of Lcc1 during growth and development of G. tsugae.

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“…Enzyme biocatalysis can be a promising alternative to current advanced treatment processes for removing organic contaminants from wastewater streams with advantages of high activity under ambient conditions of temperature and pressure, low energy requirements, low toxicity, and simple process control and maintenance. , Laccases (EC 1.10.3.2) from the white-rot fungi of the phylum Basidiomycota have received increasing attention for their high biochemical activity in catalyzing degradation of recalcitrant organic compounds . Fungal laccases were first identified as lignin degrading enzymes and subsequently shown to couple the reduction of molecular oxygen with the oxidation of a broad range of organic substrates, including phenols, polyphenols, methoxy-substituted phenols, and aromatic and aliphatic amines. , Prior studies have demonstrated the activity of fungal laccases in degrading various emerging contaminants, such as bisphenol A (BPA), , estrogens, (e.g., estrone (E1) , 17β-estradiol (E2), 17α-ethinylestradiol (EE2), atrazine, sulfamethoxazole, and other persistent organic contaminants . While biocatalysis by laccases holds great potential for organic compound transformation, use of laccase biocatalysis for water and wastewater treatment , is underexplored compared to its use for industrial applications such as textile-dye or pulp bleaching, food improvement, polymer synthesis, and the development of biosensors …”

Section: Introductionmentioning

confidence: 99%

“…15 Fungal laccases were first identified as lignin degrading enzymes 16 and subsequently shown to couple the reduction of molecular oxygen with the oxidation of a broad range of organic substrates, including phenols, polyphenols, methoxy-substituted phenols, and aromatic and aliphatic amines. 17,18 Prior studies have demonstrated the activity of fungal laccases in degrading various emerging contaminants, such as bisphenol A (BPA), 19,20 estrogens, (e.g., estrone (E1) 21,22 17β-estradiol (E2), 21 17α-ethinylestradiol (EE2), 23 atrazine, 24 sulfamethoxazole, 25 and other persistent organic contaminants. 26 While biocatalysis by laccases holds great potential for organic compound transformation, use of laccase biocatalysis for water and wastewater treatment 23,27 is underexplored compared to its use for industrial applications such as textile-dye or pulp bleaching, food improvement, polymer synthesis, and the development of biosensors.…”

Section: ■ Introductionmentioning

confidence: 99%

Cell Surface Display Fungal Laccase as a Renewable Biocatalyst for Degradation of Persistent Micropollutants Bisphenol A and Sulfamethoxazole

Chen

Stemple

Kumar

et al. 2016

Environ. Sci. Technol.

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Fungal laccases have high activity in degrading various persistent organic pollutants. However, using enzymes in solution for water treatment has limitations of nonreusability, short enzyme lifetimes, and high cost of single use. In this study, we developed a new type of biocatalyst by immobilizing fungal laccase on the surface of yeast cells using synthetic biology techniques. The biocatalyst, referred to as surface display laccase (SDL), had an enzyme activity of 104 ± 3 mU/g dry cell (with 2,2-azinobis-3-ethylbenzothiazoline-6-sulfonate (ABTS)). The SDL retained over 90% of the initial enzyme activity after 25 days storage at room temperature, while, in contrast, activity of free laccase declined to 60% of its initial activity. The SDL could be reused with high stability as it retained 74% of initial activity after eight repeated batch reactions. Proof-of-concept evaluations of the effectiveness of SDL in treating contaminants of emerging concern were performed with bisphenol A and sulfamethoxazole. Results from contaminant degradation kinetics and the effects of redox mediator amendment provided insights into the factors affecting the efficacy of the SDL system. This study reports, for the first time, the development of a surface display enzyme biocatalyst as an effective and renewable alternative for treating recalcitrant organic micropollutants.

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Laccases: The Biocatalyst with Industrial and Biotechnological Applications

Cited by 7 publications

References 174 publications

Biocatalytic properties of cell surface display laccase for degradation of emerging contaminant acetaminophen in water reclamation

Biocatalytic properties of cell surface display laccase for degradation of emerging contaminant acetaminophen in water reclamation

Importance of a Laccase Gene (Lcc1) in the Development of Ganoderma tsugae

Cell Surface Display Fungal Laccase as a Renewable Biocatalyst for Degradation of Persistent Micropollutants Bisphenol A and Sulfamethoxazole

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