Identification and Characterization of New Laccase Biocatalysts from Pseudomonas Species Suitable for Degradation of Synthetic Textile Dyes

Document identifier: oai:DiVA.org:ltu-75724
Access full text here:10.3390/catal9070629
Keyword: Engineering and Technology, Industrial Biotechnology, Bioprocess Technology, Teknik och teknologier, Industriell bioteknik, Bioprocessteknik, Laccase, Genome-mining, Heterologous expression, Biocatalysis, Pseudomonas, Biokemisk processteknik, Biochemical Process Engineering
Publication year: 2019
Relevant Sustainable Development Goals (SDGs):
SDG 9 Industry, innovation and infrastructure
The SDG label(s) above have been assigned by OSDG.ai

Abstract:

Laccases are multicopper-oxidases with variety of biotechnological applications. While predominantly used, fungal laccases have limitations such as narrow pH and temperature range and their production via heterologous protein expression is more complex due to posttranslational modifications. In comparison, bacterial enzymes, including laccases, usually possess higher thermal and pH stability, and are more suitable for expression and genetic manipulations in bacterial expression hosts. Therefore, the aim of this study was to identify, recombinantly express, and characterize novel laccases from Pseudomonas spp. A combination of approaches including DNA sequence analysis, N-terminal protein sequencing, and genome sequencing data analysis for laccase amplification, cloning, and overexpression have been used. Four active recombinant laccases were obtained, one each from P. putida KT2440 and P. putida CA-3, and two from P. putida F6. The new laccases exhibited broad temperature and pH range and high thermal stability, as well as the potential to degrade selection of synthetic textile dyes. The best performing laccase was CopA from P. putida F6 which degraded five out of seven tested dyes, including Amido Black 10B, Brom Cresol Purple, Evans Blue, Reactive Black 5, and Remazol Brilliant Blue. This work highlighted species of Pseudomonas genus as still being good sources of biocatalytically relevant enzymes.

Authors

Mina Mandic

Institute of Molecular Genetics and Genetic Engineering, University of Belgrade, Belgrade, Serbia
Other publications >>

Lidija Djokic

Institute of Molecular Genetics and Genetic Engineering, University of Belgrade, Belgrade, Serbia
Other publications >>

Efstratios Nikolaivits

School of Chemical Engineering, National Technical University of Athens, Athens, Greece
Other publications >>

Radivoje Prodanovic

Faculty of Chemistry, University of Belgrade, Belgrade, Serbia
Other publications >>

Kevin O’Connor

BEACON SFI Bioeconomy Research Centre and School of Biomolecular and Biomedical Science, University College Dublin, Belfield, Dublin, Ireland
Other publications >>

Sanja Jeremic

Institute of Molecular Genetics and Genetic Engineering, University of Belgrade, Belgrade, Serbia
Other publications >>

Evangelos Topakas

Luleå tekniska universitet; Kemiteknik; School of Chemical Engineering, National Technical University of Athens, Athens, Greece
Other publications >>

Jasmina Nikodinovic-Runic

Institute of Molecular Genetics and Genetic Engineering, University of Belgrade, Belgrade, Serbia
Other publications >>

Record metadata

Click to view metadata