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...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2023-09-01
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| Series: | Frontiers in Bioengineering and Biotechnology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fbioe.2023.1264135/full |
| _version_ | 1797678106704609280 |
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| author | Yueming Sun Ying Li Ying Li Hong Liang Hong Liang Ming Li Ye Liu Litao Wang Litao Wang Weijian Lai Teng Tang Teng Tang Yongzhao Diao Yuhong Bai Yuhong Bai Christian Isak Jørgensen Wanghui Xu Dawen Gao Dawen Gao |
| author_facet | Yueming Sun Ying Li Ying Li Hong Liang Hong Liang Ming Li Ye Liu Litao Wang Litao Wang Weijian Lai Teng Tang Teng Tang Yongzhao Diao Yuhong Bai Yuhong Bai Christian Isak Jørgensen Wanghui Xu Dawen Gao Dawen Gao |
| author_sort | Yueming Sun |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-11T22:54:52Z |
| format | Article |
| id | doaj.art-a2c27490ec91426683d917229c079255 |
| institution | Directory Open Access Journal |
| issn | 2296-4185 |
| language | English |
| last_indexed | 2024-03-11T22:54:52Z |
| publishDate | 2023-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Bioengineering and Biotechnology |
| spelling | doaj.art-a2c27490ec91426683d917229c0792552023-09-21T17:28:12ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852023-09-011110.3389/fbioe.2023.12641351264135Distinct laccase expression and activity profiles of Trametes versicolor facilitate degradation of benzo[a]pyreneYueming Sun0Ying Li1Ying Li2Hong Liang3Hong Liang4Ming Li5Ye Liu6Litao Wang7Litao Wang8Weijian Lai9Teng Tang10Teng Tang11Yongzhao Diao12Yuhong Bai13Yuhong Bai14Christian Isak Jørgensen15Wanghui Xu16Dawen Gao17Dawen Gao18Novozymes (China) Investment Co., Ltd., Beijing, ChinaCentre for Urban Environmental Remediation, Beijing University of Civil Engineering and Architecture, Beijing, ChinaBeijing Energy Conservation and Sustainable Urban and Rural Development Provincial and Ministry Co-construction Collaboration Innovation Center, Beijing University of Civil Engineering and Architecture, Beijing, ChinaCentre for Urban Environmental Remediation, Beijing University of Civil Engineering and Architecture, Beijing, ChinaBeijing Energy Conservation and Sustainable Urban and Rural Development Provincial and Ministry Co-construction Collaboration Innovation Center, Beijing University of Civil Engineering and Architecture, Beijing, ChinaNovozymes (China) Investment Co., Ltd., Beijing, ChinaNovozymes (China) Investment Co., Ltd., Beijing, ChinaCentre for Urban Environmental Remediation, Beijing University of Civil Engineering and Architecture, Beijing, ChinaBeijing Energy Conservation and Sustainable Urban and Rural Development Provincial and Ministry Co-construction Collaboration Innovation Center, Beijing University of Civil Engineering and Architecture, Beijing, ChinaNovozymes (China) Investment Co., Ltd., Beijing, ChinaCentre for Urban Environmental Remediation, Beijing University of Civil Engineering and Architecture, Beijing, ChinaBeijing Energy Conservation and Sustainable Urban and Rural Development Provincial and Ministry Co-construction Collaboration Innovation Center, Beijing University of Civil Engineering and Architecture, Beijing, ChinaNovozymes (China) Investment Co., Ltd., Beijing, ChinaCentre for Urban Environmental Remediation, Beijing University of Civil Engineering and Architecture, Beijing, ChinaBeijing Energy Conservation and Sustainable Urban and Rural Development Provincial and Ministry Co-construction Collaboration Innovation Center, Beijing University of Civil Engineering and Architecture, Beijing, ChinaNovozymes A/S, Lyngby, DenmarkNovozymes (China) Investment Co., Ltd., Beijing, ChinaCentre for Urban Environmental Remediation, Beijing University of Civil Engineering and Architecture, Beijing, ChinaBeijing Energy Conservation and Sustainable Urban and Rural Development Provincial and Ministry Co-construction Collaboration Innovation Center, Beijing University of Civil Engineering and Architecture, Beijing, ChinaA 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.https://www.frontiersin.org/articles/10.3389/fbioe.2023.1264135/fullpolycyclic aromatic hydrocarbon (PAH)benzo[a]pyrene (BaP)Trametes versicolorlaccasemulti-omicssoil remediation |
| spellingShingle | Yueming Sun Ying Li Ying Li Hong Liang Hong Liang Ming Li Ye Liu Litao Wang Litao Wang Weijian Lai Teng Tang Teng Tang Yongzhao Diao Yuhong Bai Yuhong Bai Christian Isak Jørgensen Wanghui Xu Dawen Gao Dawen Gao Distinct laccase expression and activity profiles of Trametes versicolor facilitate degradation of benzo[a]pyrene Frontiers in Bioengineering and Biotechnology polycyclic aromatic hydrocarbon (PAH) benzo[a]pyrene (BaP) Trametes versicolor laccase multi-omics soil remediation |
| 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 | polycyclic aromatic hydrocarbon (PAH) benzo[a]pyrene (BaP) Trametes versicolor laccase multi-omics soil remediation |
| url | https://www.frontiersin.org/articles/10.3389/fbioe.2023.1264135/full |
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