Journalartikel

Jahr der Veröffentlichung: 2016

Seiten: 8021-8030

Zeitschrift: Applied Microbiology and Biotechnology

Bandnummer: 100

Heftnummer: 18

ISSN: 0175-7598

DOI Link: https://doi.org/10.1007/s00253-016-7567-8

Verlag: Springer

Abstract: 
Aryl-alcohol oxidases (AAOs) are enzymes supporting the degradation of lignin by fungal derived class II peroxidases produced by white-rot fungi. AAOs are able to generate H2O2 as a by-product via oxidation of an aryl-alcohol into its correspondent aldehyde. In this study, an AAO was heterologously expressed in a basidiomycete host for the first time. The gene for an AAO of the white-rot fungus Pleurotus sapidus, a close relative to the oyster mushroom Pleurotus ostreatus, was cloned into an expression vector and put under control of the promotor of the glyceraldehyde-3-phosphate dehydrogenase gene 2 (gpdII) of the button mushroom Agaricus bisporus. The expression vector was transformed into the model basidiomycete Coprinopsis cinerea, and several positive transformants were obtained. The best producing transformants were grown in shake-flasks and in a stirred tank reactor reaching enzymatic activities of up to 125 U L-1 using veratryl alcohol as a substrate. The purified AAO was biochemically characterized and compared to the previously described native and recombinant AAOs from other Pleurotus species. In addition, a two-enzyme system comprising a dye-decolorizing peroxidase (DyP) from Mycetinis scorodonius and the P. sapidus AAO was successfully employed to bleach the anthraquinone dye Reactive Blue 5.

Harvard-Zitierstil: Galperin, I., Javeed, A., Luig, H., Lochnit, G. and Rühl, M. (2016) An aryl-alcohol oxidase of Pleurotus sapidus: heterologous expression, characterization, and application in a 2-enzyme system, Applied Microbiology and Biotechnology, 100(18), pp. 8021-8030. https://doi.org/10.1007/s00253-016-7567-8

APA-Zitierstil: Galperin, I., Javeed, A., Luig, H., Lochnit, G., & Rühl, M. (2016). An aryl-alcohol oxidase of Pleurotus sapidus: heterologous expression, characterization, and application in a 2-enzyme system. Applied Microbiology and Biotechnology. 100(18), 8021-8030. https://doi.org/10.1007/s00253-016-7567-8