Fungal Laccases and Their Potential in Bioremediation Applications

2020 ◽  
pp. 1-25
Author(s):  
Miia R. Mäkelä ◽  
Marja Tuomela ◽  
Annele Hatakka ◽  
Kristiina Hildén
Keyword(s):  
Fungal Laccases

Fungal laccases as green catalysts for dye synthesis

2012 ◽  
Vol 47 (9) ◽  
pp. 1295-1307 ◽  
Author(s):  
Jolanta Polak ◽  
Anna Jarosz-Wilkolazka
Keyword(s):  
Fungal Laccases

Interaction of fungal laccases and laccase-mediator systems with lignin

2006 ◽  
Vol 39 (4) ◽  
pp. 841-847 ◽  
Author(s):  
Sergey Shleev ◽  
Per Persson ◽  
Galina Shumakovich ◽  
Yulia Mazhugo ◽  
Alexander Yaropolov ◽  
...  
Keyword(s):  
Fungal Laccases ◽  
Mediator Systems

Reactivity of bacterial and fungal laccases with lignin under alkaline conditions

2011 ◽  
Vol 102 (21) ◽  
pp. 10006-10012 ◽  
Author(s):  
Raquel Moya ◽  
Päivi Saastamoinen ◽  
Manuel Hernández ◽  
Anna Suurnäkki ◽  
Enriqueta Arias ◽  
...  
Keyword(s):  
Fungal Laccases ◽  
Alkaline Conditions

Effect of Ethanol on Enzymatic Activity of Fungal Laccases

1999 ◽  
Vol 19 (6) ◽  
pp. 589-600 ◽  
Author(s):  
J. Rodakiewicz-Nowak ◽  
J. Haber ◽  
N. Pozdnyakova ◽  
A. Leontievsky ◽  
L. A. Golovleva
Keyword(s):  
Enzymatic Activity ◽  
Coriolus Versicolor ◽  
Acetate Buffer ◽  
Fungal Laccases ◽  
Mixed Inhibition ◽  
Inhibition Model ◽  
Buffer Solutions ◽  
Panus Tigrinus ◽  
Yellow Laccase

Blue laccase from Coriolus versicolor and blue and yellow laccases from Panus tigrinus were isolated, purified and studied in acetate buffer solutions, with and without addition of various amounts of ethanol, using syringaldazine and 2,6-dimethoxyphenol as substrates. Effect of ethanol on blue laccases could be successfully described using the mixed inhibition model, over the range of 0–2.5 M ethanol concentrations. Yellow laccase from P. tigrinus behaves differently, which may be explained by the presence of some extra molecules in its structure, which possibly stabilize the enzyme and might be exchanged in ethanol solutions.

scholarly journals Directed Evolution of Fungal Laccases

2011 ◽  
Vol 12 (2) ◽  
pp. 113-122 ◽  
Author(s):  
Diana Mate ◽  
Eva Garcia-Ruiz ◽  
Susana Camarero ◽  
Miguel Alcalde
Keyword(s):  
Directed Evolution ◽  
Fungal Laccases

scholarly journals LAC2 Encoding a Secreted Laccase Is Involved in Appressorial Melanization and Conidial Pigmentation in Colletotrichum orbiculare

2012 ◽  
Vol 25 (12) ◽  
pp. 1552-1561 ◽  
Author(s):  
Shao Yu Lin ◽  
Shiho Okuda ◽  
Kyoko Ikeda ◽  
Tetsuro Okuno ◽  
Yoshitaka Takano
Keyword(s):  
Cell Wall ◽  
Signal Peptide ◽  
Oxidative Activity ◽  
Invasion Assay ◽  
High Homology ◽  
Laccase Gene ◽  
Wild Type ◽  
Colletotrichum Orbiculare ◽  
Fungal Laccases ◽  
Fungal Pathogenicity

Both Colletotrichum and Magnaporthe spp. develop appressoria pigmented with melanin, which is essential for fungal pathogenicity. 1,8-Dihydroxynaphthalene (1,8-DHN) is believed to be polymerized to yield melanin around the appresorial cell wall through the oxidative activity of laccases. However, no 1,8-DHN laccase has yet been identified in either Colletotrichum or Magnaporthe spp. Here, we report a laccase gene, LAC2, that is involved in the appressorial melanization of Colletotrichum orbiculare, which causes cucumber anthracnose. LAC2 encodes a protein with a signal peptide and has high homology to fungal laccases. The conidial color of lac2 mutants is distinct from that of the C. orbiculare wild type, and the mutants are nonpathogenic. Notably, the mutant appressoria are defective in melanization, and a host invasion assay showed that the appressoria are nonfunctional. LAC2 was induced during appressorial melanization. These results suggest that LAC2 oxidizes 1,8-DHN in the appressoria. The LAC2 homologues of other fungi located in the same phylogenetic clade as LAC2 fully complemented the lac2 mutants. Interestingly, a LAC2 homologue, located in a different clade, complemented the conidial pigmentation but not appressorial melanization of the mutants, suggesting that the LAC2 function in appressorial melanization might only be conserved in laccases of the LAC2 clade.

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