Journal article
Authors list: Schulze, M; Geisler, L; Majcherczyk, A; Rühl, M
Publication year: 2019
Pages: 36-
Journal: AMB Express
Volume number: 9
ISSN: 2191-0855
Open access status: Gold
DOI Link: https://doi.org/10.1186/s13568-019-0761-1
Publisher: SpringerOpen
Abstract:
Although the model agaricomycete Coprinopsis cinerea possess 17 different laccase genes, up to now only four C. cinerea laccases have been purified and characterized to some degree. By exchanging the nucleotide sequence of the deduced signal peptide of Lcc8 it was possible to homologously express lcc8 in C.cinerea under control of the Agaricus bisporus gdpII promoter and the C.cinerea lcc1 terminator. The purified Lcc8 showed two bands in the SDS-PAGE with a molecular weight of 64kDa and 77kDa, respectively. The IEF determined pI values of 3.3 and 3.4 for both bands. The optimal pH for oxidation of the substrates ABTS, 2,6-dimethoxyphenol, guaiacol and syringaldazine was pH 4.0, pH 5.0, pH 4.5 and pH 5.0, respectively. Best pH for enzyme storage was pH 8.0. The optimal temperature for oxidation of ABTS was 63 degrees C, while Lcc8 showed activity of at least 50% over 300min at 50 degrees C. The comparable high stability of Lcc8 at alkaline pH and higher temperatures can be of interest for biotechnical applications.
Citation Styles
Harvard Citation style: Schulze, M., Geisler, L., Majcherczyk, A. and Rühl, M. (2019) Signal peptide replacement resulted in recombinant homologous expression of laccase Lcc8 in Coprinopsis cinerea, AMB Express, 9, p. 36. https://doi.org/10.1186/s13568-019-0761-1
APA Citation style: Schulze, M., Geisler, L., Majcherczyk, A., & Rühl, M. (2019). Signal peptide replacement resulted in recombinant homologous expression of laccase Lcc8 in Coprinopsis cinerea. AMB Express. 9, 36. https://doi.org/10.1186/s13568-019-0761-1