{Reference Type}: Journal Article
{Author}: Pezzella, Cinzia; Lettera, Vincenzo; Piscitelli, Alessandra; Giardina, Paola; Sannia, Giovanni
{Year}: 2013
{Title}: Transcriptional analysis of Pleurotus ostreatus laccase genes
{Tag}: 0
{Star}: 0
{Journal}: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
{Volume}: 97
{Issue}: 2
{Pages}: 705-717
{ISBN/ISSN}: 0175-7598
{Keywords}: FRUIT BODY DEVELOPMENT; HETEROLOGOUS EXPRESSION; CRYPTOCOCCUS-NEOFORMANS; DIFFERENTIAL REGULATION; FUNGUS; CLONING; BIOREMEDIATION; ISOENZYMES; INDUCTION; EFFLUENTS; Laccase transcriptional regulation; Laccase physiological role; Heterodimeric laccase; Fungal developmental stage; Quantitative RT-PCR; Laccase gene family
{Abstract}: Fungal laccases (p-diphenol:oxygen oxidoreductase; EC 1.10.3.2) are multi-copper-containing oxidases that catalyse the oxidation of a great variety of phenolic compounds and aromatic amines through simultaneous reduction of molecular oxygen to water. Fungi generally produce several laccase isoenzymes encoded by complex multi-gene families. The Pleurotus ostreatus genome encodes 11 putative laccase coding genes, and only six different laccase isoenzymes have been isolated and characterised so far. Laccase expression was found to be regulated by culture conditions and developmental stages even if the redundancy of these genes still raises the question about their respective functions in vivo. In this context, laccase transcript profiling analysis has been used to unravel the physiological role played by the different isoforms produced by P. ostreatus. Even if reported results depict a complex picture of the transcriptional responses exhibited by the analysed laccase genes, they were allowed to speculate on the isoform role in vivo. Among the produced laccases, LACC10 (POXC) seems to play a major role during vegetative growth, since its transcription is downregulated when the fungus starts the fructification process. Furthermore, a new tessera has been added to the puzzling mosaic of the heterodimeric laccase LACC2 (POXA3). LACC2 small subunit seems to play an additional physiological role during fructification, beside that of LACC2 complex activation/stabilisation.
{Author Address}: Univ Naples Federico II, Dept Organ Chem & Biochem, I-80126 Naples, Italy; Biopox Srl, I-80129 Naples, Italy; Univ Naples Federico II, Dept Organ Chem & Biochem, I-80126 Naples, Italy; Biopox Srl, I-80129 Naples, Italy; Univ Naples Federico II, Dept Organ Chem & Biochem, I-80126 Naples, Italy; Biopox Srl, I-80129 Naples, Italy; Univ Naples Federico II, Dept Organ Chem & Biochem, I-80126 Naples, Italy; Univ Naples Federico II, Dept Organ Chem & Biochem, I-80126 Naples, Italy; Biopox Srl, I-80129 Naples, Italy
{Database Provider}: Web of Science SCI
{Language}: English
{Country}: Italy; Italy

{Reference Type}: Journal Article
{Author}: Quevedo-Hidalgo, Balkys; Monsalve-Marin, Felipe; Cesar Narvaez-Rincon, Paulo; Marina Pedroza-Rodriguez, Aura; Enrique Velasquez-Lozano, Mario
{Year}: 2013
{Title}: Ethanol production by Saccharomyces cerevisiae using lignocellulosic hydrolysate from Chrysanthemum waste degradation
{Tag}: 0
{Star}: 0
{Journal}: WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY
{Volume}: 29
{Issue}: 3
{Pages}: 459-466
{ISBN/ISSN}: 0959-3993
{Keywords}: SOLID-STATE FERMENTATION; PLEUROTUS-OSTREATUS; ENZYMATIC-HYDROLYSIS; WHEAT-STRAW; PHANEROCHAETE-CHRYSOSPORIUM; LIGNINOLYTIC ENZYMES; TRAMETES-VERSICOLOR; REDUCING SUGAR; BIODEGRADATION; DETOXIFICATION; Ethanol; Saccharomyces cerevisiae; Chrysanthemum; Lignocellulose
{Abstract}: Ethanol production derived from Saccharomyces cerevisiae fermentation of a hydrolysate from floriculture waste degradation was studied. The hydrolysate was produced from Chrysanthemum (Dendranthema grandiflora) waste degradation by Pleurotus ostreatus and characterized to determine the presence of compounds that may inhibit fermentation. The products of hydrolysis confirmed by HPLC were cellobiose, glucose, xylose and mannose. The hydrolysate was fermented by S. cerevisiae, and concentrations of biomass, ethanol, and glucose were determined as a function of time. Results were compared to YGC modified medium (yeast extract, glucose and chloramphenicol) fermentation. Ethanol yield was 0.45 g g(-1), 88 % of the maximal theoretical value. Crysanthemum waste hydrolysate was suitable for ethanol production, containing glucose and mannose with adequate nutrients for S. cerevisiae fermentation and low fermentation inhibitor levels.
{Author Address}: Pontificia Univ Javeriana, Dept Microbiol, Lab Biotecnol Aplicada, GBAI, Bogota, Colombia; Pontificia Univ Javeriana, Bogota, Colombia; Univ Nacl Colombia Sede Bogota, Grp Proc Quim & Bioquim, Lab Ingn Quim, Dept Ingn Quim & Ambiental, Bogota, Colombia; Pontificia Univ Javeriana, Dept Microbiol, Lab Microbiol Ambiental, GBAI, Bogota, Colombia; Univ Nacl Colombia Sede Bogota, Grp Proc Quim & Bioquim, Lab Ingn Quim, Dept Ingn Quim & Ambiental, Bogota, Colombia
{Database Provider}: Web of Science SCI
{Language}: English
{Country}: Colombia; Colombia; Colombia; Colombia

{Reference Type}: Journal Article
{Author}: Sathian, S.; Radha, G.; Shanmugapriya, V.; Rajasimman, M.; Karthikeyan, C.
{Year}: 2013
{Title}: Optimization and kinetic studies on treatment of textile dye wastewater using Pleurotus floridanus
{Tag}: 0
{Star}: 0
{Place Published}: Tiergartenstrasse 17, Heidelberg, D-69121, Germany
{Journal}: Applied Water Science
{Volume}: 3
{Issue}: 1
{Pages}: 41-48
{Date Displayed}: 2013
{ISBN/ISSN}: 21905495
{Original Publication}: Springer Verlag
{Keywords}: Textile finishing; Batch reactors; Enzyme kinetics; Kinetics; Optimization; Textiles; Wastewater treatment
{Abstract}: Treatment of textile dye wastewater was carried using Pleurotus floridanus in a batch reactor. Response surface methodology (RSM) was used to optimize the process parameters like pH, temperature, agitation speed and dye wastewater concentration for the decolorization of textile dye wastewater. The optimum conditions for the maximum decolorization was: pH 6. 6, temperature 28. 8 C, agitation speed 183 rpm and dye wastewater concentration 1:2. From the results it was found that, the linear effect of agitation speed and initial textile dye wastewater concentration were more significant than other factors for the textile dye wastewater treatment. At these optimized conditions, the maximum decolorization and COD reduction was found to be 71. 2 and 80. 5 %, respectively. Kinetics of textile dye degradation process was studied by various models like first order, diffusional and Singh model. From the results it was found that the degradation follows first order model with R2 value of 0. 9550.   2012 The Author(s).
{Notes}: Compilation and indexing terms, Copyright 2013 Elsevier Inc.
20131016083663
Agitation speed
COD reduction
Decolorization
Dye wastewaters
First order
First-order models
Kinetic study
Optimized conditions
Optimum conditions
Pleurotus
Process parameters
Response surface methodology
RSM
Textile dyes
{Author Address}: Department of Chemical Engineering, Environmental Engineering Laboratory, Annamalai University, Annamalai Nagar, 608 002 Tamil Nadu, India

{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}: Roleof the C-terminusof Pleurotus eryngii Ery4 laccase in determining enzyme structure, catalytic properties and stability
{Tag}: 0
{Star}: 0
{Place Published}: Great Clarendon Street, Oxford, OX2 6DP, United Kingdom
{Journal}: Protein Engineering, Design and Selection
{Volume}: 26
{Issue}: 1
{Pages}: 1-13
{Date Displayed}: 2013
{ISBN/ISSN}: 17410126
{Original Publication}: Oxford University Press
{Keywords}: Enzymes; Amino acids; Genes; Substrates; Yeast
{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.   2012 The Author. Published by oxford University Press. All rights reserved.
{Notes}: Compilation and indexing terms, Copyright 2013 Elsevier Inc.
20125115825477
C-terminal domains
C-terminus
Catalytic core
Catalytic properties
Enzymatic activities
Enzyme activation
Enzyme structures
Fungal laccases
Laccase gene
Laccases
Mutant genes
Pleurotus eryngii
Recombinant enzymes
Site-specific
Structural data
Structure/function relationships
Various substrates
{Author Address}: CNR-Istituto di Scienze Delle Produzioni Alimentari (ISPA), via Monteroni, 73100 Lecce, Italy