Two Manganese Peroxidases and a Laccase of Trametes polyzona KU-RNW027 with Novel Properties for Dye and Pharmaceutical Product Degradation in Redox Mediator-Free System
10.1080/12298093.2019.1589900
- Author:
Piyangkun LUEANGJAROENKIT
1
;
Churapa TEERAPATSAKUL
;
Kazuo SAKKA
;
Makiko SAKKA
;
Tetsuya KIMURA
;
Emi KUNITAKE
;
Lerluck CHITRADON
Author Information
1. Department of Microbiology, Faculty of Science, Kasetsart University, Bangkok, Thailand. lerluckc@yahoo.com
- Publication Type:Original Article
- Keywords:
Manganese peroxidase;
Trametes polyzona;
dye decolorization;
pharmaceutical product degradation;
redox mediator-free system
- MeSH:
Amoxicillin;
Biodegradation, Environmental;
Ciprofloxacin;
Doxycycline;
Hydrogen-Ion Concentration;
Ions;
Laccase;
Manganese;
Oxidation-Reduction;
Peroxidases;
Pharmaceutical Preparations;
Solvents;
Tetracycline;
Trametes
- From:Mycobiology
2019;47(2):217-229
- CountryRepublic of Korea
- Language:English
-
Abstract:
Two manganese peroxidases (MnPs), MnP1 and MnP2, and a laccase, Lac1, were purified from Trametes polyzona KU-RNW027. Both MnPs showed high stability in organic solvents which triggered their activities. Metal ions activated both MnPs at certain concentrations. The two MnPs and Lac1, played important roles in dye degradation and pharmaceutical products deactivation in a redox mediator-free system. They completely degraded Remazol brilliant blue (25 mg/L) in 10–30 min and showed high degradation activities to Remazol navy blue and Remazol brilliant yellow, while Lac1 could remove 75% of Remazol red. These three purified enzymes effectively deactivated tetracycline, doxycycline, amoxicillin, and ciprofloxacin. Optimal reaction conditions were 50 °C and pH 4.5. The two MnPs were activated by organic solvents and metal ions, indicating the efficacy of using T. polyzona KU-RNW027 for bioremediation of aromatic compounds in environments polluted with organic solvents and metal ions with no need for redox mediator supplements.
