Journal Article10.1007/S00018-009-0169-1
Laccases: a never-ending story.
Paola Giardina,Vincenza Faraco,Cinzia Pezzella,Alessandra Piscitelli,Sophie Vanhulle,Giovanni Sannia +5 more
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TL;DR: In this review, the most recent studies on laccase structural features and catalytic mechanisms along with analyses of their expression are reported and examined with the aim of contributing to the discussion on their structure–function relationships.
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Abstract: Laccases (benzenediol:oxygen oxidoreductases, EC 1.10.3.2) are blue multicopper oxidases that catalyze the oxidation of an array of aromatic substrates concomitantly with the reduction of molecular oxygen to water. In fungi, laccases carry out a variety of physiological roles during their life cycle. These enzymes are being increasingly evaluated for a variety of biotechnological applications due to their broad substrate range. In this review, the most recent studies on laccase structural features and catalytic mechanisms along with analyses of their expression are reported and examined with the aim of contributing to the discussion on their structure-function relationships. Attention has also been paid to the properties of enzymes endowed with unique characteristics and to fungal laccase multigene families and their organization.
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Citations
Using CuMgFe layered double oxide to replace laccase as a catalyst for abiotic humification.
Vu Khac Hoang Bui,Xuan Cuong Nguyen,Hai Bang Truong,Jin Hur +3 more
TL;DR: CuMgFe layered double oxide catalysts replace laccase, enhancing abiotic humification of polyphenols, with MgO stabilizing pH and Cu-Fe synergy driving rapid reaction, outperforming laccase and MgFe LDH in efficiency and humic-like substance formation.
1
Producción de laccasa y ligno-degradación de cascarilla de cebada en cultivo sumergido y agitado, por Pleurotus smithii y Pleurotus ostreatus
Alejandro Canale-Guerrero,Alan J. Reynolds +1 more
- 31 May 2014
TL;DR: This article shows a relationship between a significant (P<0.05) degradation of lignin, from brewery spent grain in submerged and shaken basic culture medium without carbon source, and laccase activity by Pleurotus smithii Guzman after the first 7 days of incubation.
1
Biochemical Characterization of Three Heterologous Lactic Acid Bacteria Laccases from Pediococcus, Lactobacillus, and Lactococcus Genus and Their Potential to Degrade Biogenic Amines Using ABTS and Epicatechin as Mediators
Isaac Monroy,I. Olmeda,Sergi Ferrer,I. Pardo +3 more
TL;DR: This study presents a comparison of the laccases’ biogenic amine-degrading efficiency using different mediators, the first time such a comparison has been made.
1
Challenges and Progress in Evaluating Apple Root Resistance Responses to <i>Pythium ultimum</i> Infection
Yanmin Zhu,Zhe Zhou +1 more
TL;DR: This study evaluates apple root resistance to Pythium ultimum infection, overcoming challenges through micropropagation and identifying elite rootstock germplasm with distinct resistance levels, shedding light on potential mechanisms and genetic elements underlying resistance traits.
1
References
Electron transfers in chemistry and biology
Rudolph A. Marcus,Norman Sutin +1 more
TL;DR: In this paper, the electron transfer reactions between ions and molecules in solution have been the subject of considerable experimental study during the past three decades, including charge transfer, photoelectric emission spectra, chemiluminescent electron transfer, and electron transfer through frozen media.
7.9K
Multicopper Oxidases and Oxygenases
TL;DR: Copper sites have historically been divided into three classes based on their spectroscopic features, which reflect the geometric and electronic structure of the active site: type 1 or blue copper, type 2 (T2) or normal copper, and type 3 (T3) or coupled binuclear copper centers.
3.5K
Oxidation of non-phenolic substrates. An expanded role for laccase in lignin biodegradation.
TL;DR: Laccase is capable of oxidizing both phenolic and non‐phenolic moieties of lignin but that the latter is dependent on the co‐presence of primary laccase substrates.
1.3K
Potential applications of oxidative enzymes and phenoloxidase-like compounds in wastewater and soil treatment: a review
Nelson Durán,Elisa Esposito +1 more
TL;DR: Immobilization of oxidative enzymes on porous ceramic supports or resins did not adversely affect their stability and showed a good potential for degradation of environment persistent aromatics.
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