{Reference Type}: Journal Article
{Author}: Sheedy, E. M.; Van de Wouw, A. P.; Howlett, B.; May, T. W.
{Year}: 2013
{Title}: Multi-gene sequence data reveal morphologically cryptic phylogenetic species within the genus Laccaria in southern Australia
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=23396157&query_hl=1
{Tag}: 5
{Star}: 0
{Journal}: Mycologia
{DOI}: 10.3852/12-266
{Date Displayed}: 2013 Feb 8
{Date}: 2013-02-08
{Type of Work}: JOURNAL ARTICLE
{Accession Number}: 23396157
{Abstract}: Laccaria (Hydnangiaceae, Agaricales, Basidiomycota) is one of the more intensively studied ectomycorrhizal genera; however, species boundaries within Laccaria and the closely related Hydnangium and Podohydnangium in Australia have   not yet been examined with molecular sequence data. Based on morphological characters, eight native species of Laccaria are currently recognized in Australia, as well as three Hydnangium species and the monotypic Podohydnangium australe. Sequences of the internal transcribed spacer region of nuclear rDNA (ITS), RNA polymerase beta subunit II (rpb2) and translation elongation factor 1   alpha (tef-1alpha) were generated from 77 collections of Laccaria, Hydnangium and Podohydnangium from Australia. Ten phylogenetic species and a further 11 potential species (represented by singletons) of Laccaria in Australia are delimited from sequence analyses. Most of the morphological species contained cryptic phylogenetic species, but these species were always nested entirely within a given morphological species, although not always as sister taxa. The rpb2 locus performed best as a species barcode with pairwise and patristic distance measures. The ITS sequence region returned the least resolved gene tree   of the three regions examined and was the least useful as a barcode region. Based on the phylogenetic topology, there appears to have been multiple gains and/or losses of the ectomycorrhizal association of some species with the myrtle beech,   Nothofagus cunninghamii as well as of sequestrate basidiocarps and two-spored basidia.
{Author Address}: School of Botany, The University of Melbourne, Parkville, Victoria, 3010, Australia.
{Language}: ENG

{Reference Type}: Journal Article
{Author}: Sathishkumar, Palanivel; Palvannan, Thayumanavan; Murugesan, Kumarasamy; Kamala-Kannan, Seralathan
{Year}: 2013
{Title}: Detoxification of malachite green by Pleurotus florida laccase produced under solid-state fermentation using agricultural residues
{Tag}: 0
{Star}: 0
{Journal}: ENVIRONMENTAL TECHNOLOGY
{Volume}: 34
{Issue}: 2
{Pages}: 139-147
{ISBN/ISSN}: 0959-3330
{Keywords}: SAJOR-CAJU; TRAMETES-VERSICOLOR; PHENOLIC-COMPOUNDS; PICHIA-PASTORIS; WASTE-WATER; DECOLORIZATION; GENE; EXPRESSION; DYES; PURIFICATION; decolorization; laccase; malachite green; N-demethylation; Pleurotus florida; response surface methodology
{Abstract}: Laccase was produced from Pleurotus florida under solid-state fermentation, and the production was optimized by response surface methodology. The predicted maximum laccase production of 8.81 U g -1 was obtained by the optimum concentration of malt extract, banana peel, wheat bran and CuSO 4, which was found to be 0.69 g, 10.61 g, 10.68 g and 77.15 ppm, respectively. The validation results suggested that the laccase production was 7.96 U g -1 in the optimized medium, which was close to the predicted value. Decolorization efficiency of P. florida laccase was evaluated against malachite green (MG). Rapid decolorization of MG dye was observed, and a dark-coloured precipitate was formed in the reaction mixture. HPLC analysis indicated that the laccase enzyme degraded MG by the demethylation process. The toxicity of MG was reduced to 67% after the treatment with laccase, which was confirmed by a phytotoxicity study.
{Author Address}: Chonbuk Natl Univ, Bioremediat Lab, Adv Inst Environm & Biosci, Div Biotechnol,Coll Environm & Bioresource Sci, Iksan 570752, South Korea; Periyar Univ, Dept Biochem, Lab Bioproc & Engn, Salem 636011, Tamil Nadu, India; Periyar Univ, Dept Biochem, Lab Bioproc & Engn, Salem 636011, Tamil Nadu, India; Pohang Univ Sci & Technol, Sch Environm Sci & Engn, Pohang 790784, South Korea; Chonbuk Natl Univ, Bioremediat Lab, Adv Inst Environm & Biosci, Div Biotechnol,Coll Environm & Bioresource Sci, Iksan 570752, South Korea
{Database Provider}: Web of Science SCI
{Language}: English
{Country}: India; South Korea; South Korea

{Reference Type}: Journal Article
{Author}: Bleve, Gianluca; Lezzi, Chiara; Spagnolo, Stefano; Tasco, Gianluca; Tufariello, Maria; Casadio, Rita; Mita, Giovanni; Rampino, Patrizia; Grieco, Francesco
{Year}: 2013
{Title}: Role of the C-terminus of Pleurotus eryngii Ery4 laccase in determining enzyme structure, catalytic properties and stability
{Tag}: 0
{Star}: 0
{Journal}: PROTEIN ENGINEERING DESIGN & SELECTION
{Volume}: 26
{Issue}: 1
{Pages}: 1-13
{ISBN/ISSN}: 1741-0126
{Keywords}: COMBINATORIAL SATURATION MUTAGENESIS; PRELIMINARY-X-RAY; SACCHAROMYCES-CEREVISIAE; CRYSTAL-STRUCTURE; FUNGAL LACCASE; MELANOCARPUS-ALBOMYCES; MYCELIOPHTHORA THERMOPHILA; SUBCELLULAR-LOCALIZATION; HETEROLOGOUS EXPRESSION; FUNCTIONAL EXPRESSION; C-terminal domain; laccase; rational mutagenesis
{Abstract}: The ERY4 laccase gene of Pleurotus eryngii is not biologically active when expressed in yeast. To explain this finding, we analysed the role of the C-terminus of Ery4 protein by producing a number of its different mutant variants. Two different categories of ERY4 mutant genes were produced and expressed in yeast: (i) mutants carrying C-terminal deletions and (ii) mutants carrying different site-specific mutations at their C-terminus. Investigation of the catalytic properties of the recombinant enzymes indicated that each novel variant acquired different affinities and catalytic activity for various substrates. Our results highlight that C-terminal processing is fundamental for Ery4 laccase enzymatic activities allowing substrate accessibility to the enzyme catalytic core. Apparently, the last 18 amino acids in the C-terminal end of the Ery4 laccase play a critical role in enzyme activity, stability and kinetic and, in particular biochemical and structural data indicate that the K532 residue is fundamental for enzyme activation. These studies shed light on the structure/function relationships of fungal laccases and will enhance the development of biotechnological strategies for the industrial exploitation of these enzymes.
{Author Address}: CNR, ISPA, I-73100 Lecce, Italy; Univ Salento, Dipartimento Sci & Tecnol Biol & Ambientali, I-73100 Lecce, Italy; CNR, ISPA, I-73100 Lecce, Italy; Univ Bologna, Dipartimento Biol Evoluzionist Sperimentale, I-40126 Bologna, Italy; CNR, IMM, I-73100 Lecce, Italy; Univ Bologna, Dipartimento Biol Evoluzionist Sperimentale, I-40126 Bologna, Italy; CNR, ISPA, I-73100 Lecce, Italy; Univ Salento, Dipartimento Sci & Tecnol Biol & Ambientali, I-73100 Lecce, Italy; CNR, ISPA, I-73100 Lecce, Italy
{Database Provider}: Web of Science SCI
{Language}: English
{Country}: Italy; Italy; Italy; Italy

{Reference Type}: Journal Article
{Author}: Janusz, Grzegorz; Kucharzyk, Katarzyna H.; Pawlik, Anna; Staszczak, Magdalena; Paszczynski, Andrzej J.
{Year}: 2013
{Title}: Fungal laccase, manganese peroxidase and lignin peroxidase: Gene expression and regulation
{Tag}: 0
{Star}: 0
{Journal}: ENZYME AND MICROBIAL TECHNOLOGY
{Volume}: 52
{Issue}: 1
{Pages}: 1-12
{ISBN/ISSN}: 0141-0229
{Keywords}: BASIDIOMYCETE PHANEROCHAETE-CHRYSOSPORIUM; WHITE-ROT BASIDIOMYCETE; UBIQUITIN-PROTEASOME SYSTEM; PLEUROTUS-SAJOR-CAJU; DEGRADING BASIDIOMYCETE; TRAMETES-VERSICOLOR; CERIPORIOPSIS-SUBVERMISPORA; MOLECULAR CHARACTERIZATION; DIFFERENTIAL REGULATION; DEPENDENT PEROXIDASE; Laccase; Manganese peroxidase; MnP; Lignin peroxidase; LiP; Genetics
{Abstract}: Extensive research efforts have been dedicated to characterizing expression of laccases and peroxidases and their regulation in numerous fungal species. Much attention has been brought to these enzymes broad substrate specificity resulting in oxidation of a variety of organic compounds which brings about possibilities of their utilization in biotechnological and environmental applications. Research attempts have resulted in increased production of both laccases and peroxidases by the aid of heterologous and homologous expression. Through analysis of promoter regions, protein expression patterns and culture conditions manipulations it was possible to compare and identify common pathways of these enzymes' production and secretion. Although laccase and peroxidase proteins have been crystallized and thoroughly analyzed, there are still a lot of questions remaining about their evolutionary origin and the physiological functions. This review describes the present understanding of promoter sequences and correlation between the observed regulatory effects on laccase, manganese peroxidase and lignin peroxidase genes transcript levels and the presence of specific response elements. (C) 2012 Elsevier Inc. All rights reserved.
{Author Address}: Marie Curie Sklodowska Univ, Dept Biochem, PL-20033 Lublin, Poland; Duke Univ, Dept Civil & Environm Engn, Durham, NC 27708 USA; Marie Curie Sklodowska Univ, Dept Biochem, PL-20033 Lublin, Poland; Marie Curie Sklodowska Univ, Dept Biochem, PL-20033 Lublin, Poland; Univ Idaho, Food Res Ctr, Sch Food Sci, Moscow, ID 83844 USA
{Database Provider}: Web of Science SCI
{Language}: English
{Country}: Poland; USA; USA