<?xml version="1.0" encoding="utf-8"?>
<export-example>
  <doc>
    <id>11638</id>
    <completedYear/>
    <publishedYear>2011</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst/>
    <pageLast/>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume/>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2014-08-19</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">High-yield production of aromatic peroxygenase by the agaric fungus Marasmius rotula</title>
    <abstract language="eng">An extracellular peroxygenase from Marasmius rotula was produced in liquid culture, chromatographically purified and partially characterized. This is the third aromatic peroxygenase (APO) that has been characterized in detail and the first one that can be produced in high yields. The highest enzyme levels of about 41,000 U l-1 (corresponding to appr. 445 mg l-1 APO protein) exceeded the hitherto reported levels more than 40-fold and were detected in carbon- and nitrogen-rich complex media. The enzyme was purified by FPLC to apparent homogeneity (SDS-PAGE) with a molecular mass of 32 kDa (27 kDa after deglycosylation) and isoelectric points between 4.97 and 5.27. The UV-visible spectrum of the native enzyme showed a characteristic maximum (Soret band) at 418 nm that shifted after reduction with sodium dithionite and flushing with carbon monoxide to 443 nm. The pH optimum of the M. rotula enzyme was found to vary between pH 5 and 6 for most reactions studied. The apparent Km-values for 2,6-dimethoxyphenol, benzyl alcohol, veratryl alcohol, naphthalene and H2O2 were 0.133, 0.118, 0.279, 0.791 and 3.14 mM, respectively. M. rotula APO was found to be highly stable in a pH range from 5 to 10 as well as in the presence of organic solvents (50% vol/vol) such as methanol, acetonitrile and N,N-dimethylformamide. Unlike other APOs, the peroxygenase of M. rotula showed neither brominating nor chlorinating activities.</abstract>
    <parentTitle language="eng">AMB Express</parentTitle>
    <identifier type="url">http://www.amb-express.com/content/1/1/31</identifier>
    <identifier type="issn">2191-0855</identifier>
    <enrichment key="BTU">nicht an der BTU erstellt / not created at BTU</enrichment>
    <author>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </author>
    <submitter>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </submitter>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Marek J.</firstName>
      <lastName>Pecyna</lastName>
    </author>
    <author>
      <firstName>Danuta</firstName>
      <lastName>Kapturska</lastName>
    </author>
    <author>
      <firstName>Stephanie</firstName>
      <lastName>Friedrich</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxidase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Basidiomycota</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Cytochrome P450</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Bioreactor</value>
    </subject>
    <collection role="old_institute" number="06010">Prof. Enzymtechnologie</collection>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>11640</id>
    <completedYear/>
    <publishedYear>2014</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>36</pageFirst>
    <pageLast>40</pageLast>
    <pageNumber/>
    <edition/>
    <issue>103</issue>
    <volume/>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2014-08-21</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Optimization of a biocatalytic process to gain (R)-1-phenylethanol by applying the software tool Sabento for ecological assessment during the early stages of development</title>
    <abstract language="eng">Ecological assessment using the software tool Sabento was conducted to compare different processes to gain the fine chemical (R)-1-phenylethanol from ethylbenzene. The software was applied during the biocatalytic process development using the unspecific peroxygenase (EC .11.2.1) of the fungus Agrocybe aegerita. The process could be systematically improved with respect to the ecological performance during process development. Compared to a modern chemical process and a further biotechnological process, it now reaches the best environmental key indicator. The software tool Sabento proved to be well suited to work out the most important factors determining the ecological burdens in the early stages of process&#13;
development.</abstract>
    <parentTitle language="eng">Journal of Molecular Catalysis : B, Enzymatic</parentTitle>
    <identifier type="doi">10.1016/j.molcatb.2013.10.002</identifier>
    <identifier type="url">http://www.sciencedirect.com/science/article/pii/S1381117713002774</identifier>
    <identifier type="issn">1381-1177</identifier>
    <enrichment key="BTU">an der BTU erstellt / created at BTU</enrichment>
    <author>
      <firstName>Stephanie</firstName>
      <lastName>Friedrich</lastName>
    </author>
    <submitter>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </submitter>
    <author>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Kluge</lastName>
    </author>
    <author>
      <firstName>Tobias</firstName>
      <lastName>Brinkmann</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Ecological assessment</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Biocatalytic process for (R)-1-phenylethanol</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Unspecific peroxygenase (EC 1.11.2.1)</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Agrocybe aegerita</value>
    </subject>
    <collection role="old_institute" number="06010">Prof. Enzymtechnologie</collection>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
</export-example>
