The ant Lasius niger is a new source of bacterial enzymes with biotechnological potential for bleaching dye

0518725 - MBÚ 2020 RIV GB eng J - Journal Article
Diez-Mendez, A. - García Fraile, Paula - Solano, F. - Rivas, R.
The ant Lasius niger is a new source of bacterial enzymes with biotechnological potential for bleaching dye.
Scientific Reports. Roč. 9, OCT 23 2019 (2019), č. článku 15217. ISSN 2045-2322. E-ISSN 2045-2322
R&D Projects: GA ČR(CZ) GJ16-15293Y
Institutional support: RVO:61388971
Keywords : synthetic dyes * microbial decolorization * laccase activity
OECD category: Microbiology
Impact factor: 3.998, year: 2019
Method of publishing: Open access
https://www.nature.com/articles/s41598-019-51669-w

Industrial synthetic dyes cause health and environmental problems. This work describes the isolation of 84 bacterial strains from the midgut of the Lasius niger ant and the evaluation of their potential application in dye bioremediation. Strains were identified and classified as judged by rRNA 16S. The most abundant isolates were found to belong to Actinobacteria (49%) and Firmicutes (47.2%). We analyzed the content in laccase, azoreductase and peroxidase activities and their ability to degrade three known dyes (azo, thiazine and anthraquinone) with different chemical structures. Strain Ln26 (identified as Brevibacterium permense) strongly decolorized the three dyes tested at different conditions. Strain Ln78 (Streptomyces ambofaciens) exhibited a high level of activity in the presence of Toluidine Blue (TB). It was determined that 8.5 was the optimal pH for these two strains, the optimal temperature conditions ranged between 22 and 37 degrees C, and acidic pHs and temperatures around 50 degrees C caused enzyme inactivation. Finally, the genome of the most promising candidate (Ln26, approximately 4.2 Mb in size) was sequenced. Genes coding for two DyP-type peroxidases, one laccase and one azoreductase were identified and account for the ability of this strain to effectively oxidize a variety of dyes with different chemical structures.
Permanent Link: http://hdl.handle.net/11104/0303788