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来自细菌的可降解塑料聚酯酶jmPE13和jmPE14的特性及工程改造

Characterization and engineering of plastic-degrading polyesterases jmPE13 and jmPE14 from bacterium.

作者信息

Zhou Xiaoli, Zhou Xianmin, Xu Zhiqiang, Zhang Mingxia, Zhu Honghui

机构信息

Key Laboratory of Agricultural Microbiomics and Precision Application (MARA), Key Laboratory of Agricultural Microbiome (MARA), Guangdong Provincial Key Laboratory of Microbial Culture Collection and Application, State Key Laboratory of Applied Microbiology Southern China, Institute of Microbiology, Guangdong Academy of Sciences, Guangzhou, China.

出版信息

Front Bioeng Biotechnol. 2024 Feb 14;12:1349010. doi: 10.3389/fbioe.2024.1349010. eCollection 2024.

Abstract

Polyester plastics are widely used in daily life, but also cause a large amount of waste. Degradation by microbial enzymes is the most promising way for the biobased upcycling of the wastes. However, there is still a shortage of high-performance enzymes, and more efficient polyester hydrolases need to be developed. Here we identified two polyester hydrolases, jmPE13 and jmPE14, from a previously isolated strain sp. JM16B3. The proteins were recombinantly expressed and purified in , and their enzymatic properties were characterized. JmPE13 and jmPE14 showed hydrolytic activity towards polyethylene terephthalate (PET) and Poly (butylene adipate-co-terephthalate) (PBAT) at medium temperatures. The enzyme activity and stability of jmPE13 were further improved to 3- and 1.5-fold, respectively, by rational design. The results of our research can be helpful for further engineering of more efficient polyester plastic hydrolases and their industrial applications.

摘要

聚酯塑料在日常生活中广泛使用,但也会产生大量废弃物。通过微生物酶进行降解是这些废弃物生物基升级再造最具前景的途径。然而,高性能酶仍然短缺,需要开发更高效的聚酯水解酶。在此,我们从先前分离的菌株sp. JM16B3中鉴定出两种聚酯水解酶,jmPE13和jmPE14。这些蛋白质在大肠杆菌中进行重组表达和纯化,并对其酶学性质进行了表征。JmPE13和jmPE14在中等温度下对聚对苯二甲酸乙二酯(PET)和聚己二酸丁二醇酯-对苯二甲酸丁二醇酯共聚物(PBAT)表现出水解活性。通过合理设计,jmPE13的酶活性和稳定性分别进一步提高了3倍和1.5倍。我们的研究结果有助于进一步设计更高效的聚酯塑料水解酶及其工业应用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d7ce/10904013/2581f8908082/fbioe-12-1349010-g001.jpg

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