191
Views
6
CrossRef citations to date
0
Altmetric
Articles

Effect of copper ions on the ligninolytic enzyme complex and the antioxidant enzyme activity in the white-rot fungus Trametes trogii 46

, , , , , & show all
Pages 1128-1133 | Received 11 Jul 2017, Accepted 14 Dec 2017, Published online: 04 Jan 2018
 

Abstract

White-rot fungi of the Phylum Basidiomycota are quite promising in ligninolytic enzyme production and the optimization of their synthesis is of particular significance. The aim of this study was to investigate the effect of enhanced concentration of copper (Cu) ions (25–1000 μg/ml) on the activity of the ligninolytic enzyme complex (laccase, Lac; lignin peroxidase, LiP; Mn-peroxidase, MnP) in Trametes trogii 46, as well as the changes in the antioxidant cell response. All concentrations tested reduced significantly in growth and glucose consumption. Cu ions affected the ligninolytic enzyme activity in a dose dependent manner. Concentrations in the range of 25–100 μg/ml strongly stimulated Lac production (a 5–6-fold increase compared to the control). LiP activity was also induced by Cu, with the peak value being recorded following exposure to 50 μg/ml metal ions. In contrast, the addition of Cu ions had a positive effect on MnP activity at a concentration higher than 100 μg/ml. The maximum enzyme level was achieved at 1000 μg/ml. The results obtained on superoxide dismutase and catalase activities indicated that exposure of T. trogii 46 mycelia to Cu ions promoted oxidative stress. Both enzyme activities were co-ordinately produced with Lac and LiP but not co-ordinately with MnP.

View correction statement:
Corrigendum

Acknowledgments

The authors express their appreciation for the financial support to the Program for support of young scientists in Bulgaria, granted by the Bulgarian Academy of Sciences (grant number DFNP-57/27.04.2016).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.