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Identification, heterologous expression and characterization of a dye-decolorizing peroxidase of Pleurotus sapidus

Lauber, Christiane ; Schwarz, Tatiana ; Nguyen, Quoc Khanh ; Lorenz, Patrick ; Lochnit, Guenter ; Zorn, Holger


Originalveröffentlichung: (2017) AMB Express 7:164 doi: 10.1186/s13568-017-0463-5
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URN: urn:nbn:de:hebis:26-opus-138308
URL: http://geb.uni-giessen.de/geb/volltexte/2018/13830/

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Sammlung: Open Access - Publikationsfonds
Universität Justus-Liebig-Universität Gießen
Institut: Institute of Food Chemistry and Food Biotechnology
Fachgebiet: Biochemie (FB 08)
DDC-Sachgruppe: Biowissenschaften, Biologie
Dokumentart: Aufsatz
Sprache: Englisch
Erstellungsjahr: 2017
Publikationsdatum: 13.11.2018
Kurzfassung auf Englisch: The coding sequence of a peroxidase from the secretome of Pleurotus sapidus was cloned from a cDNA library. Bioinformatic analyses revealed an open reading frame of 1551 bp corresponding to a primary translation product of 516 amino acids. The DyP-type peroxidase was heterologously produced in Trichoderma reesei with an activity of 55,000 U L-1. The enzyme was purified from the culture supernatant, biochemically characterized and the kinetic parameters were determined. The enzyme has an N-terminal signal peptide composed of 62 amino acids. Analysis by Blue Native PAGE and activity staining with ABTS, as well as gel filtration chromatography showed the native dimeric state of the enzyme (115 kDa). Analysis of the substrate range revealed that the recombinant enzyme catalyzes, in addition to the conversion of some classic peroxidase substrates such as 2,2-azino-bis(3-ethylthiazoline-6-sulfonate) and substituted phenols like 2,6–dimethoxyphenol, also the decolorization of the anthraquinonic dye Reactive Blue 5. The enzyme also catalyzes bleaching of natural colorants such as ß-carotene and annatto. Surprisingly, ß-carotene was transformed in the presence and absence of H2O2 by rPsaDyP, however enzyme activity was increased by the addition of H2O2. This indicates that the rPsaDyP has an oxidase function in addition to a peroxidase activity. As a consequence of the high affinity to the characteristic substrate Reactive Blue 5 the rPsaDyP belongs functionally to the dyp-type peroxidase family.
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