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Distinct laccase expression and activity profiles of Trametes versicolor facilitate degradation of benzo[a]pyrene

A Trametes versicolor isolate from the Changbai Mountain showed promising activity in degrading benzo[a]pyrene (BaP), which is a high molecular weight (HMW) polycyclic aromatic hydrocarbon (PAH) compound. It was hypothesized that the T. versicolor isolate encode BaP-degrading enzymes, among which la...

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Autores principales: Sun, Yueming, Li, Ying, Liang, Hong, Li, Ming, Liu, Ye, Wang, Litao, Lai, Weijian, Tang, Teng, Diao, Yongzhao, Bai, Yuhong, Jørgensen, Christian Isak, Xu, Wanghui, Gao, Dawen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10551628/
https://www.ncbi.nlm.nih.gov/pubmed/37811380
http://dx.doi.org/10.3389/fbioe.2023.1264135
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author Sun, Yueming
Li, Ying
Liang, Hong
Li, Ming
Liu, Ye
Wang, Litao
Lai, Weijian
Tang, Teng
Diao, Yongzhao
Bai, Yuhong
Jørgensen, Christian Isak
Xu, Wanghui
Gao, Dawen
author_facet Sun, Yueming
Li, Ying
Liang, Hong
Li, Ming
Liu, Ye
Wang, Litao
Lai, Weijian
Tang, Teng
Diao, Yongzhao
Bai, Yuhong
Jørgensen, Christian Isak
Xu, Wanghui
Gao, Dawen
author_sort Sun, Yueming
collection PubMed
description A Trametes versicolor isolate from the Changbai Mountain showed promising activity in degrading benzo[a]pyrene (BaP), which is a high molecular weight (HMW) polycyclic aromatic hydrocarbon (PAH) compound. It was hypothesized that the T. versicolor isolate encode BaP-degrading enzymes, among which laccase is mostly sought after due to significant commercial potential. Genome of the T. versicolor isolate was sequenced and assembled, and seven laccase homologues were identified (TvLac1-7) as candidate genes potentially contributing to BaP degradation. In order to further identify the BaP responsive laccases, time-course transcriptomic and proteomic analyses were conducted in parallel on the T. versicolor isolate upon BaP treatment. Homologous laccases showed distinct expression patterns. Most strikingly, TvLac5 was rapidly induced in the secreted proteomes (secretomes), while TvLac2 was repressed. Recombinant laccase expression and biochemical characterization further showed corresponding enzymatic activity profiles, where TvLac5 was 21-fold more effective in BaP degradation compared to TvLac2. Moreover, TvLac5 also showed 3.6-fold higher BaP degrading activity compared to a commercial laccase product of T. versicolor origin. Therefore, TvLac5 was concluded to be a BaP-responsive enzyme from T. versicolor showing effective BaP degradation activity.
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spelling pubmed-105516282023-10-06 Distinct laccase expression and activity profiles of Trametes versicolor facilitate degradation of benzo[a]pyrene Sun, Yueming Li, Ying Liang, Hong Li, Ming Liu, Ye Wang, Litao Lai, Weijian Tang, Teng Diao, Yongzhao Bai, Yuhong Jørgensen, Christian Isak Xu, Wanghui Gao, Dawen Front Bioeng Biotechnol Bioengineering and Biotechnology A Trametes versicolor isolate from the Changbai Mountain showed promising activity in degrading benzo[a]pyrene (BaP), which is a high molecular weight (HMW) polycyclic aromatic hydrocarbon (PAH) compound. It was hypothesized that the T. versicolor isolate encode BaP-degrading enzymes, among which laccase is mostly sought after due to significant commercial potential. Genome of the T. versicolor isolate was sequenced and assembled, and seven laccase homologues were identified (TvLac1-7) as candidate genes potentially contributing to BaP degradation. In order to further identify the BaP responsive laccases, time-course transcriptomic and proteomic analyses were conducted in parallel on the T. versicolor isolate upon BaP treatment. Homologous laccases showed distinct expression patterns. Most strikingly, TvLac5 was rapidly induced in the secreted proteomes (secretomes), while TvLac2 was repressed. Recombinant laccase expression and biochemical characterization further showed corresponding enzymatic activity profiles, where TvLac5 was 21-fold more effective in BaP degradation compared to TvLac2. Moreover, TvLac5 also showed 3.6-fold higher BaP degrading activity compared to a commercial laccase product of T. versicolor origin. Therefore, TvLac5 was concluded to be a BaP-responsive enzyme from T. versicolor showing effective BaP degradation activity. Frontiers Media S.A. 2023-09-21 /pmc/articles/PMC10551628/ /pubmed/37811380 http://dx.doi.org/10.3389/fbioe.2023.1264135 Text en Copyright © 2023 Sun, Li, Liang, Li, Liu, Wang, Lai, Tang, Diao, Bai, Jørgensen, Xu and Gao. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Bioengineering and Biotechnology
Sun, Yueming
Li, Ying
Liang, Hong
Li, Ming
Liu, Ye
Wang, Litao
Lai, Weijian
Tang, Teng
Diao, Yongzhao
Bai, Yuhong
Jørgensen, Christian Isak
Xu, Wanghui
Gao, Dawen
Distinct laccase expression and activity profiles of Trametes versicolor facilitate degradation of benzo[a]pyrene
title Distinct laccase expression and activity profiles of Trametes versicolor facilitate degradation of benzo[a]pyrene
title_full Distinct laccase expression and activity profiles of Trametes versicolor facilitate degradation of benzo[a]pyrene
title_fullStr Distinct laccase expression and activity profiles of Trametes versicolor facilitate degradation of benzo[a]pyrene
title_full_unstemmed Distinct laccase expression and activity profiles of Trametes versicolor facilitate degradation of benzo[a]pyrene
title_short Distinct laccase expression and activity profiles of Trametes versicolor facilitate degradation of benzo[a]pyrene
title_sort distinct laccase expression and activity profiles of trametes versicolor facilitate degradation of benzo[a]pyrene
topic Bioengineering and Biotechnology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10551628/
https://www.ncbi.nlm.nih.gov/pubmed/37811380
http://dx.doi.org/10.3389/fbioe.2023.1264135
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