{Reference Type}: Journal Article
{Author}: Goudopoulou, A.; Krimitzas, A.; Typas, M. A.
{Year}: 2010
{Title}: Differential gene expression of ligninolytic enzymes in Pleurotus ostreatus grown on olive oil mill wastewater
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=20607227&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Appl Microbiol Biotechnol
{Volume}: 88
{Issue}: 2
{Pages}: 541-51
{DOI}: 10.1007/s00253-010-2750-9
{Date Displayed}: 2010 Sep
{Date}: 2010-09-01
{Type of Work}: Journal Article; Research Support, Non-U.S. Gov't
{Accession Number}: 20607227
{Keywords}: Culture Media; Gene Expression Profiling; *Gene Expression Regulation, Enzymologic; *Gene Expression Regulation, Fungal; *Industrial Waste; Laccase/*genetics; Lignin/*metabolism; Peroxidases/*genetics; Plant Oils/*metabolism; Pleurotus/*enzymology/genetics/*growth & development; *Waste Disposal, Fluid
{Abstract}: The expression of laccase and manganese peroxidase genes of a selected strain of   Pleurotus ostreatus were studied in olive oil mill wastewater (OMW). The fungal strain decolourized 50% OMW in a linear way for 21 days and, at the same time, degraded the phenol compounds by 85%. Transcripts of laccase genes poxa1b, pox2,   poxa3, and sspoxa3a, sspoxa3b coding for the small subunits of POXA3, were estimated by qRT-PCR, at different time intervals, together with beta-tubulin gene used as internal control, from fungal cultures grown in a chemically-defined complete medium (CM), a supplemented CM with the addition of Cu(+2) and Mn(+2) (CM-plus) and 50% OMW in distilled water. The most abundant transcripts in both OMW and CM-plus were those of the poxa3, whereas pox2 transcripts were induced only in OMW and those of poxa1b at a strict time-window (14 days) in both OMW and CM-plus. Interestingly enough, the transcripts of genes sspoxa3a and sspoxa3b were up-regulated between 14-21 days, at a time at which the large subunit of the enzyme coded by poxa3 was down-regulated. The manganese peroxidase gene mnp2 exhibited a strong and specific transcriptional induction in OMW after 12 and 14   days, followed by a drastic drop after 18 days and a complete cease of expression at day 21, whereas mnp3 transcripts were at maximum level in OMW at day 10 but where thereafter reduced.
{Author Address}: Department of Genetics and Biotechnology, University of Athens, Panepistemiopolis, Greece.
{Language}: eng

{Reference Type}: Journal Article
{Author}: Vajna, B.; Nagy, A.; Sajben, E.; Manczinger, L.; Szijarto, N.; Kadar, Z.; Bordas, D.; Marialigeti, K.
{Year}: 2010
{Title}: Microbial community structure changes during oyster mushroom substrate preparation
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19967354&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Appl Microbiol Biotechnol
{Volume}: 86
{Issue}: 1
{Pages}: 367-75
{DOI}: 10.1007/s00253-009-2371-3
{Date Displayed}: 2010 Mar
{Date}: 2010-03-01
{Type of Work}: Journal Article; Research Support, Non-U.S. Gov't
{Accession Number}: 19967354
{Keywords}: *Bacteria/classification/genetics/growth & development; Biotechnology/*methods; DNA Fingerprinting/methods; DNA, Ribosomal/analysis/genetics; *Ecosystem; *Fungi/classification/genetics/growth & development; Medicago/*metabolism; *Pleurotus/growth & development/metabolism; Polymorphism, Restriction Fragment Length; RNA, Ribosomal, 16S/genetics; Triticum/*metabolism
{Abstract}: Although oyster mushroom (Pleurotus spp.) is a valuable food, cultivated worldwide on an industrial scale, still very little is known about the microbial   dynamics during oyster mushroom substrate preparation. Therefore, the characterization of the microbial dynamics by chemical and biological tools was the objective of this study. During substrate preparation, enzymatic digestibility of the substrate improved by 77%, whereas the cellulose and hemicellulose to lignin ratios decreased by 9% and 19%, respectively. Fluorescein diacetate hydrolysis reached its minimum value at the temperature maximum of the   process during the composting phase and exceeded the initial level at the end of   the process. Fungal species played part in the initial mesophilic phase of the substrate preparation process, but they disappeared after pasteurization in tunnels at constant elevated temperatures. Changes in the microbiota showed a marked bacterial community succession during substrate preparation investigated by 16S ribosomal deoxyribonucleic acid-based terminal restriction fragment length polymorphism (T-RFLP). Mature samples represented the least variance, which indicated the effect of the standardized preparation protocol. The relation between mushroom yield and the bacterial community T-RFLP fingerprints was investigated, but the uniformity of mushroom yields did not support any significant correlation.
{Author Address}: Department of Microbiology, Eotvos Lorand University, Pazmany Peter setany 1/C, 1117 Budapest, Hungary. vbalanus@gmail.com
{Language}: eng

{Reference Type}: Journal Article
{Author}: Largeteau, M. L.; Latapy, C.; Minvielle, N.; Regnault-Roger, C.; Savoie, J. M.
{Year}: 2010
{Title}: Expression of phenol oxidase and heat-shock genes during the development of Agaricus bisporus fruiting bodies, healthy and infected by Lecanicillium fungicola
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19711071&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Appl Microbiol Biotechnol
{Volume}: 85
{Issue}: 5
{Pages}: 1499-507
{DOI}: 10.1007/s00253-009-2186-2
{Date Displayed}: 2010 Feb
{Date}: 2010-02-01
{Type of Work}: Journal Article
{Accession Number}: 19711071
{Keywords}: Agaricus/enzymology/*genetics/growth & development/metabolism; DNA, Fungal/genetics/metabolism; Fruiting Bodies, Fungal/genetics/*growth & development/metabolism; Fungal Proteins/genetics/metabolism; Gene Expression Regulation, Fungal; Heat-Shock Proteins/*genetics/metabolism; Host-Pathogen Interactions; Hypocreales/growth & development/*pathogenicity; Laccase/genetics/metabolism; Monophenol Monooxygenase/*genetics/metabolism; Mycelium/genetics/growth & development/metabolism; Polymerase Chain Reaction; Verticillium/growth & development/*pathogenicity
{Abstract}: The fungal pathogen Lecanicillium fungicola (formerly Verticillium fungicola) is   responsible for severe losses worldwide in the mushroom (Agaricus bisporus) industry. Infected crops are characterised by masses of undifferentiated tissue (bubbles) growing in place of sporophores. The expression of three laccase genes   (lcc1, lcc2 and lcc3), two tyrosinase genes (AbPPO1 and AbPPO2) and the hspA gene encoding a heat-shock protein known to be potentially associated with host-pathogen interaction was investigated in mycelial aggregates and during the   development of healthy sporophores and bubbles of a susceptible cultivar. The lcc3, AbPPO2 and hspA genes were each expressed at different levels at the different stages of sporophore morphogenesis, whilst they showed a stable expression throughout bubble development. The transcript levels were similar in bubbles and at the first developmental stage of healthy fruiting bodies, both showing no tissue differentiation. These observations suggest that lcc3, AbPPO2 and hspA are associated with A. bisporus morphogenesis. Comparing the expression   of the hspA gene in three susceptible and three tolerant strains showed that the   latter displayed a higher level of transcript in the primordium, which is the stage receptive to the pathogen. The six strains exhibited a comparable expression in the vegetative mycelium, non-receptive to L. fungicola.
{Author Address}: UR1264, Mycologie et Securite des Aliments, INRA, BP81, 33883 Villenave d'Ornon,   France. largeteau@bordeaux.inra.fr
{Language}: eng

{Reference Type}: Journal Article
{Author}: Pisanelli, I.; Kujawa, M.; Gschnitzer, D.; Spadiut, O.; Seiboth, B.; Peterbauer, C.
{Year}: 2010
{Title}: Heterologous expression of an Agaricus meleagris pyranose dehydrogenase-encoding   gene in Aspergillus spp. and characterization of the recombinant enzyme
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19888575&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Appl Microbiol Biotechnol
{Volume}: 86
{Issue}: 2
{Pages}: 599-606
{DOI}: 10.1007/s00253-009-2308-x
{Date Displayed}: 2010 Mar
{Date}: 2010-03-01
{Type of Work}: Journal Article; Research Support, Non-U.S. Gov't
{Accession Number}: 19888575
{Keywords}: Agaricus/*enzymology; Aspergillus nidulans/genetics; Aspergillus niger/genetics; Carbohydrate Dehydrogenases/*genetics/*metabolism; Fungal Proteins/*genetics/*metabolism; Pyrans/*metabolism; Recombinant Proteins/genetics/metabolism; Substrate Specificity
{Abstract}: Pyranose dehydrogenase (PDH) is a flavin-dependant sugar oxidoreductase found in   the family Agaricaceae, basidiomycetes that degrade lignocellulose-rich forest litter, and is catalytically related to the fungal enzymes pyranose 2-oxidase and cellobiose dehydrogenase. It has broad substrate specificity and displays similar activities with most sugar constituents of lignocellulose including disaccharides and oligosaccharides, a number of (substituted) quinones, and metal ions are suitable electron acceptors rather than molecular oxygen. In contrast to pyranose 2-oxidase and cellobiose dehydrogenase, which oxidize regioselectively at C-2 and C-1, respectively, PDH is capable of oxidation on C-1 to C-4 as well as double oxidations, depending on the nature of the substrate. This makes it a very interesting enzyme for biocatalytic applications, as many of the reaction products are otherwise unaccessible by chemical or enzymatic means. PDH was characterized in detail in a limited number of fungi, and the first encoding genes were isolated only recently. We report here, for the first time, the heterologous expression of one of these genes, encoding the major PDH protein in   Agaricus meleagris, in the filamentous fungi Aspergillus nidulans, and Aspergillus niger.
{Author Address}: Department of Food Sciences and Technology, University of Natural Resources and Applied Life Sciences (BOKU), Vienna, Austria.
{Language}: eng