Applications of ligninolytic enzymes to pollutants, wastewater, dyes, soil, coal, paper and polymers

Yadav, Meera; Yadav, Hardeo Singh

doi:10.1007/s10311-015-0516-4

Cited by 68 publications

(25 citation statements)

References 142 publications

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“…White rot fungi may degrade lignin by secreting ligninolytic enzymes, including peroxidases (PODs), multicopper oxidase (MCO), laccases, and H2O2-generating enzymes (Yadav and Yadav 2015;Manavalan et al 2015). Complete enzymatic hydrolysis and breakdown of cellulose chains require the combined activities of the β-1,4-glycosidic bond-cleaving enzymes endoglucanase (EG), cellobiohydrolase (CBH), and β-glucosidase (BGL).…”

Section: Introductionmentioning

confidence: 99%

Transcriptomic Profile of Lignocellulose Degradation from Trametes versicolor on Poplar Wood

Zhang

Wang

et al. 2017

BioResources

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The Trametes versicolor genome is predicted to encode many enzymes that effectively degrade lignin, making it a potentially useful tool for biopulping. However, the wood degradation mechanism of T. versicolor is not clear. To identify the enzymes that contribute to lignocellulose degradation, changes in the T. versicolor transcriptome during growth on poplar wood, relative to growth on glucose medium, were evaluated. Eight hundred and fifty-three genes were differentially expressed, with 360 genes up-regulated and 493 genes were down-regulated on poplar wood. Notably, most genes involved in lignin degradation were upregulated, including eight lignin peroxidase (LiP) genes. Genes encoding cellulose and hemicellulose degrading-enzymes were mostly downregulated, including six endo-β-1,4-glucanase genes and three cellobiohydrolase I genes. These results characterized transcriptomic changes related to lignocellulose degradation. This information could be used to develop T. versicolor as a tool to improve the efficiency of lignin degradation or to provide a theoretical foundation for a new paper pulp manufacturing process.

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Section: Introductionmentioning

confidence: 99%

Transcriptomic Profile of Lignocellulose Degradation from Trametes versicolor on Poplar Wood

Zhang

Wang

et al. 2017

BioResources

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“…Most of them, blue colored, catalyze the direct oxidation of a wide variety of phenolic compounds [ 3 , 4 ]. Some yellow laccases, able to oxidize both phenolic and non-phenolic compounds, have also been described [ 5 ]. Besides the ability to oxidize a multitude of substrates, the laccases do not require hydrogen peroxide for the oxidation reaction; moreover, they use molecular oxygen as an electron acceptor, generating water.…”

Section: Introductionmentioning

confidence: 99%

“…The laccases are monomeric, dimeric or tetrameric proteins that contain four copper atoms per monomer, distributed in three redox sites named T1, T2 and T3 [ 5 ]. The redox potential ( E °) of the T1 copper site is characteristic of each enzyme, ranging from 0.4 to 0.8 V vs. normal hydrogen electrode (NHE).…”

Section: Introductionmentioning

confidence: 99%

A High Redox Potential Laccase from Pycnoporus sanguineus RP15: Potential Application for Dye Decolorization

Zimbardi

Camargo

Carli

et al. 2016

IJMS

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Laccase production by Pycnoporus sanguineus RP15 grown in wheat bran and corncob under solid-state fermentation was optimized by response surface methodology using a Central Composite Rotational Design. A laccase (Lacps1) was purified and characterized and the potential of the pure Lacps1 and the crude culture extract for synthetic dye decolorization was evaluated. At optimal conditions (eight days, 26 °C, 18% (w/w) milled corncob, 0.8% (w/w) NH4Cl and 50 mmol·L−1 CuSO4, initial moisture 4.1 mL·g−1), the laccase activity reached 138.6 ± 13.2 U·g−1. Lacps1 was a monomeric glycoprotein (67 kDa, 24% carbohydrate). Optimum pH and temperature for the oxidation of 2,2’-azino-bis(3-ethylbenzthiazoline-6-sulfonate) (ABTS) were 4.4 and 74.4 °C, respectively. Lacps1 was stable at pH 3.0–8.0, and after two hours at 55–60 °C, presenting high redox potential (0.747 V vs. NHE). ABTS was oxidized with an apparent affinity constant of 147.0 ± 6.4 μmol·L−1, maximum velocity of 413.4 ± 21.2 U·mg−1 and catalytic efficiency of 3140.1 ± 149.6 L·mmol−1·s−1. The maximum decolorization percentages of bromophenol blue (BPB), remazol brilliant blue R and reactive blue 4 (RB4), at 25 or 40 °C without redox mediators, reached 90%, 80% and 60%, respectively, using either pure Lacps1 or the crude extract. This is the first study of the decolorization of BPB and RB4 by a P. sanguineus laccase. The data suggested good potential for treatment of industrial dye-containing effluents.

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“…They catalyze the redox reaction for a wide range of substrates, which leads to the classification of peroxidases as an important group of enzymes for medicinal, biochemical, immunological, biotechnological and industrial applications. They have been successfully used for biopulping and biobleaching in the paper and textile industries [16,17]. Additionally, peroxidases extracted from different sources have been used for bioremediation and decolorization reactions [18][19][20][21].…”

Section: Introductionmentioning

confidence: 99%

A Green and Simple Protocol for Extraction and Application of a Peroxidase-Rich Enzymatic Extract

Rosa

Barreto

Pinto

et al. 2020

MPs

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Recently there is a great social expectation that scientists should produce more sustainable and environmentally friendly chemical processes. Within this necessity, biocatalysis presents many attractive features because reactions are often performed in water, under mild conditions, the catalyst is biodegradable and can be obtained from renewable raw materials. In this work, we propose a simple, rapid and low-cost method for the preparation and application of an enzymatic extract from turnip root. The protocol described includes (1) the preparation of the enzymatic extract, (2) the procedure for the assessment of the more favorable working parameters (temperature, pH) and (3) the methodology for the application of the extract as the catalyst for biotransformation reactions. We anticipate that the protocol in this research will provide a simple way for obtaining an enzymatic extract which can operate efficiently under mild conditions and can effectively catalyze the biotransformation of simple phenols.

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Applications of ligninolytic enzymes to pollutants, wastewater, dyes, soil, coal, paper and polymers

Cited by 68 publications

References 142 publications

Transcriptomic Profile of Lignocellulose Degradation from Trametes versicolor on Poplar Wood

Transcriptomic Profile of Lignocellulose Degradation from Trametes versicolor on Poplar Wood

A High Redox Potential Laccase from Pycnoporus sanguineus RP15: Potential Application for Dye Decolorization

A Green and Simple Protocol for Extraction and Application of a Peroxidase-Rich Enzymatic Extract

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