期刊
FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY
卷 11, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fbioe.2023.1264135
关键词
polycyclic aromatic hydrocarbon (PAH); benzo[a]pyrene (BaP); Trametes versicolor; laccase; multi-omics; soil remediation
A Trametes versicolor isolate from the Changbai Mountain showed effective degradation activity for benzo[a]pyrene (BaP), a high molecular weight polycyclic aromatic hydrocarbon (PAH) compound. Through genomic analysis and transcriptomic/proteomic studies, a BaP-responsive laccase, TvLac5, was identified and found to have a 21-fold higher degradation activity for BaP compared to other homologous laccases, as well as a 3.6-fold higher activity than a commercial laccase product derived from T. versicolor.
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据