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  <title>Unitus DSpace</title>
  <link rel="alternate" href="http://http://dspace.unitus.it:80" />
  <subtitle>The DSpace digital repository system captures, stores, indexes, preserves, and distributes digital research material.</subtitle>
  <id>http://http://dspace.unitus.it:80</id>
  <updated>2013-05-21T11:48:40Z</updated>
  <dc:date>2013-05-21T11:48:40Z</dc:date>
  <entry>
    <title>In vivo and in vitro degradation of aromatic contaminants by white rot fungi. A case study: Panus tigrinus CBS 577.79</title>
    <link rel="alternate" href="http://hdl.handle.net/2067/1200" />
    <author>
      <name>Covino, Stefano</name>
    </author>
    <id>http://hdl.handle.net/2067/1200</id>
    <updated>2011-02-25T01:30:47Z</updated>
    <published>2010-02-17T23:00:00Z</published>
    <summary type="text">Title: In vivo and in vitro degradation of aromatic contaminants by white rot fungi. A case study: Panus tigrinus CBS 577.79
Authors: Covino, Stefano
Description: Dottorato di ricerca in Evoluzione biologica e biochimica</summary>
    <dc:date>2010-02-17T23:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Effect of mobilizing agents on mycoremediation and impact on the indigenous microbiota</title>
    <link rel="alternate" href="http://hdl.handle.net/2067/1408" />
    <author>
      <name>Giubilei, Maria Angela</name>
    </author>
    <author>
      <name>Leonardi, Vanessa</name>
    </author>
    <author>
      <name>Federici, Ermanno</name>
    </author>
    <author>
      <name>Covino, Stefano</name>
    </author>
    <author>
      <name>Sasek, Vaclav</name>
    </author>
    <author>
      <name>Novotny, Cenek</name>
    </author>
    <author>
      <name>Federici, Federico</name>
    </author>
    <author>
      <name>D'Annibale, Alessandro</name>
    </author>
    <author>
      <name>Petruccioli, Maurizio</name>
    </author>
    <id>http://hdl.handle.net/2067/1408</id>
    <updated>2011-06-29T15:15:47Z</updated>
    <published>2008-12-31T23:00:00Z</published>
    <summary type="text">Title: Effect of mobilizing agents on mycoremediation and impact on the indigenous microbiota
Authors: Giubilei, Maria Angela; Leonardi, Vanessa; Federici, Ermanno; Covino, Stefano; Sasek, Vaclav; Novotny, Cenek; Federici, Federico; D'Annibale, Alessandro; Petruccioli, Maurizio
Abstract: BACKGROUND: Mobilizing agents (MAs) have been suggested to improve the fungal degradation of polycyclic aromatic&#xD;
hydrocarbons (PAHs) in soil. Three different MAs (Tween 20, Tween 80 and soybean oil) were investigated for their ability to&#xD;
stimulate contaminant degradation by either Phlebia sp. DABAC 9 or Allescheriella sp. DABAC1 in a soil spiked with amixture of&#xD;
PAHs.&#xD;
RESULTS: Phlebia sp. and Allescheriella sp. markedly differed in their growth capabilities under non-sterile conditions and&#xD;
withoutMAs (3.0 versus 0.1 μg ergosterol g−1 soil, respectively). However, soybean oil led to a 35-fold increase of Allescheriella&#xD;
sp. growth. Contaminant degradations by Phlebia sp. DABAC 9 and Allescheriella sp. DABAC 1 were best supported by soybean&#xD;
oil and Tween 20, respectively. Enumeration of cultivable bacteria and denaturing gradient gel electrophoresis (DGGE) analysis&#xD;
of PCR-amplified 16S rRNA showed that microbial density and biodiversity were positively affected by the mycoremediation&#xD;
especially with Allescheriella sp., the use of which led to an evident detoxification.&#xD;
CONCLUSIONS: Allescheriella sp. DABAC 1 appears to be a promising strain in the remediation of PAH-contaminated soils. The&#xD;
different response of the two fungi to MAs addition confirms the stringent need for a preliminary lab-scale assessment of&#xD;
fungus/MA combinations prior to application.
Description: L'articolo è disponibile sul sito dell'editore: http://www.onlinelibrary.wiley.com</summary>
    <dc:date>2008-12-31T23:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Kinetic and redox properties of MnP II, a major manganese peroxidase isoenzyme from Panus tigrinus CBS 577.79.</title>
    <link rel="alternate" href="http://hdl.handle.net/2067/1411" />
    <author>
      <name>Petruccioli, Maurizio</name>
    </author>
    <author>
      <name>Frascono, Marco</name>
    </author>
    <author>
      <name>Quaratino, Daniele</name>
    </author>
    <author>
      <name>Covino, Stefano</name>
    </author>
    <author>
      <name>Favero, Gabriele</name>
    </author>
    <author>
      <name>Mazzei, Franco</name>
    </author>
    <author>
      <name>Federici, Federico</name>
    </author>
    <author>
      <name>D'Annibale, Alessandro</name>
    </author>
    <id>http://hdl.handle.net/2067/1411</id>
    <updated>2011-06-30T12:42:40Z</updated>
    <published>2008-12-31T23:00:00Z</published>
    <summary type="text">Title: Kinetic and redox properties of MnP II, a major manganese peroxidase isoenzyme from Panus tigrinus CBS 577.79.
Authors: Petruccioli, Maurizio; Frascono, Marco; Quaratino, Daniele; Covino, Stefano; Favero, Gabriele; Mazzei, Franco; Federici, Federico; D'Annibale, Alessandro
Abstract: A manganese peroxidase (MnP) isoenzyme&#xD;
from Panus tigrinus CBS 577.79 was produced in a benchtop stirred-tank reactor and purified to apparent homogeneity. The purification scheme involving ultrafiltration, affinity chromatography on concanavalin–A Sepharose, and gel filtration led to a purified MnP, termed ‘‘MnP II,’’ with a specific activity of 288 IU mg-1 protein and a final yield of 22%. The enzyme turned out to be a monomeric protein with molecular mass of 50.5 kDa, pI of 4.07, and an extent of N-glycosylation of about 5.3% of the high-mannose type. The temperature and pH optima for the formation of malonate manganic chelates were 45°C and 5.5, respectively. MnP II proved to be poorly thermostable at 50 and 60°C, with half-lives of 11 min and 105 s, respectively. Km values for H2O2 and Mn2+ were 16 and&#xD;
124 lM, respectively. Although MnP II was able to oxidize veratryl alcohol and to catalyze the Mn2+ -independent&#xD;
oxidation of several phenols, it cannot be assigned to the versatile peroxidase family. As opposed to versatile peroxidase&#xD;
oxidation, veratryl alcohol oxidation required the simultaneous presence of H2O2 and Mn2+; in addition, low turnover numbers and Km values higher than 300 lM&#xD;
characterized the Mn2+ -independent oxidation of substituted phenols. Kinetic properties and the substrate specificity&#xD;
of the enzyme markedly differed from those reported for MnP isoenzymes produced by the reference strain P. tigrinus 8/18. To our knowledge, this study reports for the first time a thorough electrochemical  characterization of a MnP from this fungus.
Description: L'articolo è disponibile sul sito dell'editore: http://www.springerlink.com</summary>
    <dc:date>2008-12-31T23:00:00Z</dc:date>
  </entry>
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