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海洋真菌来源的角质酶在温和温度下高效生物降解聚己二酸丁二醇酯对苯二甲酸酯。

Efficient biodegradation of poly(butylene adipate-co-terephthalate) in mild temperature by cutinases derived from a marine fungus.

机构信息

CAS and Shandong Province Key Laboratory of Experimental Marine Biology & Center of Deep Sea Research, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266404, China; Laboratory for Marine Biology and Biotechnology, Qingdao Marine Science and Technology Center, Qingdao 266237, China; College of Earth Science, University of Chinese Academy of Sciences, Beijing 101408, China.

CAS and Shandong Province Key Laboratory of Experimental Marine Biology & Center of Deep Sea Research, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266404, China; Laboratory for Marine Biology and Biotechnology, Qingdao Marine Science and Technology Center, Qingdao 266237, China.

出版信息

J Hazard Mater. 2024 Dec 5;480:136008. doi: 10.1016/j.jhazmat.2024.136008. Epub 2024 Oct 2.

DOI:10.1016/j.jhazmat.2024.136008
PMID:39368353
Abstract

Poly(butylene adipate-co-terephthalate) (PBAT) waste gradually accumulates in the environment, posing ecological risks. Enzymatic hydrolysis holds great potential in the end-of-life management of PBAT, but reported enzymes require high reaction temperatures, limiting their practical industrial applications. In this study, we discovered that the marine fungus Alternaria alternata FB1 can efficiently degrade PBAT at 28 °C. Two cutinases designated as AaCut4 and AaCut10, were identified and verified as key enzymes responsible for this degradation process. Notably, the recombinant AaCut10 was able to depolymerize 82.14 % PBAT within 24 h and fully decompose it within 48 h at 37 °C. Through protein engineering, the yield of terephthalic acid monomer was increased to 96.01 %, highlighting its potential for facilitating PBAT upcycling. Furthermore, based on the investigation of the distribution patterns of PBAT hydrolases, novel degradative agents have been identified within unique ecological niches, leading to the establishment of a comprehensive screening repository of PBAT hydrolases. Overall, our study provides new candidates for enzymatic PBAT recycling with low energy consumption and offers insights into the PBAT degradation manner in ecosystems.

摘要

聚己二酸/对苯二甲酸丁二酯(PBAT)废弃物逐渐在环境中积累,对生态系统构成风险。酶解法在 PBAT 的末端管理方面具有很大的潜力,但报道的酶需要较高的反应温度,限制了其实际工业应用。在这项研究中,我们发现海洋真菌交替单端孢霉 FB1 可以在 28°C 下有效降解 PBAT。鉴定并验证了两种被命名为 AaCut4 和 AaCut10 的角质酶是负责这一降解过程的关键酶。值得注意的是,重组的 AaCut10 能够在 37°C 下在 24 小时内将 82.14%的 PBAT 解聚,48 小时内完全分解。通过蛋白质工程,提高了对苯二甲酸单体的产量,达到 96.01%,突出了其促进 PBAT 升级回收的潜力。此外,基于对 PBAT 水解酶分布模式的研究,在独特的生态位中发现了新型降解剂,从而建立了一个全面的 PBAT 水解酶筛选库。总的来说,我们的研究为低能耗的 PBAT 酶法回收提供了新的候选酶,并深入了解了 PBAT 在生态系统中的降解方式。

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引用本文的文献

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Highly efficient degradation of polybutylene succinate (PBS) and polycaprolactone (PCL) by a recombinant marine fungal cutinase.重组海洋真菌角质酶对聚丁二酸丁二醇酯(PBS)和聚己内酯(PCL)的高效降解
Appl Environ Microbiol. 2025 Aug 14:e0083325. doi: 10.1128/aem.00833-25.