Laccase Isoenzymes of Trametes hirsuta LE-BIN072: Degradation of Industrial Dyes and Secretion under the Different Induction Conditions
- Authors: Moiseenko K.V.1, Savinova O.S.1, Vasina D.V.1, Kononikhin A.S.2,3, Tyazhelova T.V.4, Fedorova T.V.1
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Affiliations:
- A.N. Bach Institute of Biochemistry, Research Center of Biotechnology, Russian Academy of Sciences
- Emanuel Institute of Biochemical Physics, Russian Academy of Sciences
- V.L. Talrose Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences
- N.I. Vavilov Institute of General Genetics, Russian Academy of Sciences
- Issue: Vol 54, No 9 (2018)
- Pages: 834-841
- Section: Producing Organisms, Biology, Selection, and Genetic Engineering
- URL: https://journals.rcsi.science/0003-6838/article/view/152738
- DOI: https://doi.org/10.1134/S0003683818090090
- ID: 152738
Cite item
Abstract
It is well-known that various oxidative enzymes of wood-degrading fungi are widely demanded in various fields of biotechnology. Laccases attract particular attention, since they have different substrate specificities and can be used not only in pulp and paper industry, but also for the degradation of various xenobiotics, including decolorization of dyes. In this work, a comparative analysis of the native major (LacA) and the recombinant minor (rLacC, rLacD, rLacF) Trametes hirsuta 072 laccase isoenzymes applicability for bleaching of four widely used recalcitrant dyes was conducted. It was shown that all isoenzymes decolorized dyes to different extent, and the minor isoenzymes rLacD and rLacF are the most promising for decolorization of congo red and phenol red dyes. Moreover, we provide detailed exoproteome analysis of T. hirsuta 072 growing on the media supplemented with compounds that were previously shown to increase transcription levels of the minor laccase isoenzymes.
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About the authors
K. V. Moiseenko
A.N. Bach Institute of Biochemistry, Research Center of Biotechnology, Russian Academy of Sciences
Author for correspondence.
Email: mr.moiseenko@gmail.com
Russian Federation, Moscow, 119071
O. S. Savinova
A.N. Bach Institute of Biochemistry, Research Center of Biotechnology, Russian Academy of Sciences
Email: mr.moiseenko@gmail.com
Russian Federation, Moscow, 119071
D. V. Vasina
A.N. Bach Institute of Biochemistry, Research Center of Biotechnology, Russian Academy of Sciences
Email: mr.moiseenko@gmail.com
Russian Federation, Moscow, 119071
A. S. Kononikhin
Emanuel Institute of Biochemical Physics, Russian Academy of Sciences; V.L. Talrose Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences
Email: mr.moiseenko@gmail.com
Russian Federation, Moscow, 119334; Moscow, 119334
T. V. Tyazhelova
N.I. Vavilov Institute of General Genetics, Russian Academy of Sciences
Email: mr.moiseenko@gmail.com
Russian Federation, Moscow, 119333
T. V. Fedorova
A.N. Bach Institute of Biochemistry, Research Center of Biotechnology, Russian Academy of Sciences
Email: mr.moiseenko@gmail.com
Russian Federation, Moscow, 119071
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