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High-yield production of aromatic peroxygenase by the agaric fungus Marasmius rotula.
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High-yield production of aromatic peroxygenase by the agaric fungus Marasmius rotula.

Author: G Gröbe Affiliation: Department of Biology, Chemistry and Process Technology, Lausitz University of Applied Sciences, Großenhainer Straße 57, 01968 Senftenberg, Germany. ggroebe@hs-lausitz.de.R UllrichMJ PecynaD KapturskaS FriedrichAll authors
Edition/Format: Article Article : English
Publication:AMB Express, 2011 Oct 11; 1(1): 31
Summary:
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  Read more...
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Document Type: Article
All Authors / Contributors: G Gröbe Affiliation: Department of Biology, Chemistry and Process Technology, Lausitz University of Applied Sciences, Großenhainer Straße 57, 01968 Senftenberg, Germany. ggroebe@hs-lausitz.de.; R Ullrich; MJ Pecyna; D Kapturska; S Friedrich; M Hofrichter; K Scheibner
Language Note: English
Unique Identifier: 761091964
Awards:

Abstract:

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.

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