Heterologous expression of an Agaricus meleagris pyranose dehydrogenase-encoding gene in Aspergillus spp. and characterization of the recombinant enzyme
2010 (English)In: Applied Microbiology and Biotechnology, ISSN 0175-7598, E-ISSN 1432-0614, Vol. 86, no 2, 599-606 p.Article in journal (Refereed) Published
Pyranose dehydrogenase (PDH) is a flavin-dependant sugar oxidoreductase found in the family Agaricaceae, basidiomycetes that degrade lignocellulose-rich forest litter, and is catalytically related to the fungal enzymes pyranose 2-oxidase and cellobiose dehydrogenase. It has broad substrate specificity and displays similar activities with most sugar constituents of lignocellulose including disaccharides and oligosaccharides, a number of (substituted) quinones, and metal ions are suitable electron acceptors rather than molecular oxygen. In contrast to pyranose 2-oxidase and cellobiose dehydrogenase, which oxidize regioselectively at C-2 and C-1, respectively, PDH is capable of oxidation on C-1 to C-4 as well as double oxidations, depending on the nature of the substrate. This makes it a very interesting enzyme for biocatalytic applications, as many of the reaction products are otherwise unaccessible by chemical or enzymatic means. PDH was characterized in detail in a limited number of fungi, and the first encoding genes were isolated only recently. We report here, for the first time, the heterologous expression of one of these genes, encoding the major PDH protein in Agaricus meleagris, in the filamentous fungi Aspergillus nidulans, and Aspergillus niger.
Place, publisher, year, edition, pages
2010. Vol. 86, no 2, 599-606 p.
Agaricus, Aspergillus nidulans, Aspergillus niger, Biocatalytic applications, Cellobiose Dehydrogenase, Electron acceptor, Encoding genes, Filamentous fungi, Forest litter, Fungal enzymes, Heterologous expression, Oxidoreductases, Pyranose, Reaction products, Recombinant enzymes, Substrate specificity, Sugar constituents
IdentifiersURN: urn:nbn:se:kth:diva-149422DOI: 10.1007/s00253-009-2308-xISI: 000274707600019PubMedID: 19888575ScopusID: 2-s2.0-77249143323OAI: oai:DiVA.org:kth-149422DiVA: diva2:739399
QC 201408212014-08-212014-08-212015-06-23Bibliographically approved