Enhancing the biodegradation of bis(2-hydroxyethyl) terephthalate by an IsPETasePA and MHETase dual-enzyme system

IF 2.8 4区 生物学 Q3 BIOTECHNOLOGY & APPLIED MICROBIOLOGY Journal of chemical technology and biotechnology Pub Date : 2024-06-03 DOI:10.1002/jctb.7688
Yingtong Gao, Yunxin Zheng, Zixin Qi, Yufan Pan, Yu Zhou, Shengping You, Rongxin Su, Wei Qi, Mengfan Wang
{"title":"Enhancing the biodegradation of bis(2-hydroxyethyl) terephthalate by an IsPETasePA and MHETase dual-enzyme system","authors":"Yingtong Gao,&nbsp;Yunxin Zheng,&nbsp;Zixin Qi,&nbsp;Yufan Pan,&nbsp;Yu Zhou,&nbsp;Shengping You,&nbsp;Rongxin Su,&nbsp;Wei Qi,&nbsp;Mengfan Wang","doi":"10.1002/jctb.7688","DOIUrl":null,"url":null,"abstract":"<div>\n \n \n <section>\n \n <h3> BACKGROUND</h3>\n \n <p>Environmental and ecological hazards caused by the accumulation of polyethylene terephthalate (PET) are becoming a global concern. The use of enzymes to address the plastic crisis has achieved many successes, but the difficulty in degrading high-crystallinity PET has limited its application. Numerous studies have investigated the degradation of PET with arbitrary crystallinity to bis-2-(2-hydroxyethyl) terephthalate (BHET) using chemical pre-treatment methods such as glycolysis, but few have tested its biocompatibility with enzymatic alliances.</p>\n </section>\n \n <section>\n \n <h3> RESULTS</h3>\n \n <p>Herein, we report the enzymatic characterization and subsequent engineering of the state-of-the-art <i>Is</i>PETase<sup>PA</sup> and MHETase (where MHET is mono(2-hydroxyethyl) terephthalate), a dual-enzyme system which can be used for the degradation from BHET to a single-product terephthalate (TPA). Modulators, including surfactants, organic solvents and metal ions, enhanced the enzyme activity of <i>Is</i>PETase<sup>PA</sup> and MHETase by up to 1.1-fold and 2.3-fold, respectively. 100% TPA yield (BHET of 25 g L<sup>−1</sup>) was achieved within 5 h. We also analyzed the mechanism of optimal ion modulator modification by dynamics simulation, and it synergistically achieved enhancement of MHET degradation ability by improving stability and binding energy.</p>\n </section>\n \n <section>\n \n <h3> CONCLUSION</h3>\n \n <p>The introduction of modulators improves the efficiency of the dual-enzyme system in degrading BHET. This work provides a valuable strategy for the complete degradation of BHET to TPA, laying the groundwork for the realization of PET recycling. © 2024 Society of Chemical Industry (SCI).</p>\n </section>\n </div>","PeriodicalId":15335,"journal":{"name":"Journal of chemical technology and biotechnology","volume":null,"pages":null},"PeriodicalIF":2.8000,"publicationDate":"2024-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of chemical technology and biotechnology","FirstCategoryId":"5","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/jctb.7688","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

BACKGROUND

Environmental and ecological hazards caused by the accumulation of polyethylene terephthalate (PET) are becoming a global concern. The use of enzymes to address the plastic crisis has achieved many successes, but the difficulty in degrading high-crystallinity PET has limited its application. Numerous studies have investigated the degradation of PET with arbitrary crystallinity to bis-2-(2-hydroxyethyl) terephthalate (BHET) using chemical pre-treatment methods such as glycolysis, but few have tested its biocompatibility with enzymatic alliances.

RESULTS

Herein, we report the enzymatic characterization and subsequent engineering of the state-of-the-art IsPETasePA and MHETase (where MHET is mono(2-hydroxyethyl) terephthalate), a dual-enzyme system which can be used for the degradation from BHET to a single-product terephthalate (TPA). Modulators, including surfactants, organic solvents and metal ions, enhanced the enzyme activity of IsPETasePA and MHETase by up to 1.1-fold and 2.3-fold, respectively. 100% TPA yield (BHET of 25 g L−1) was achieved within 5 h. We also analyzed the mechanism of optimal ion modulator modification by dynamics simulation, and it synergistically achieved enhancement of MHET degradation ability by improving stability and binding energy.

CONCLUSION

The introduction of modulators improves the efficiency of the dual-enzyme system in degrading BHET. This work provides a valuable strategy for the complete degradation of BHET to TPA, laying the groundwork for the realization of PET recycling. © 2024 Society of Chemical Industry (SCI).

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
IsPETasePA 和 MHETase 双酶系统促进对苯二甲酸二(2-羟乙基)酯的生物降解
聚对苯二甲酸乙二醇酯(PET)的累积对环境和生态造成的危害正成为全球关注的问题。使用酶来解决塑料危机已经取得了许多成功,但降解高结晶度 PET 的困难限制了酶的应用。已有大量研究利用化学预处理方法(如糖酵解)将任意结晶度的 PET 降解为对苯二甲酸二-2-(2-羟乙基)酯(BHET),但很少有研究利用酶联盟测试其生物相容性。在此,我们报告了最先进的 IsPETasePA 和 MHETase(其中 MHET 为对苯二甲酸单(2-羟乙基)酯)的酶学特性和后续工程设计,这是一种双酶系统,可用于将 BHET 降解为单产物对苯二甲酸(TPA)。包括表面活性剂、有机溶剂和金属离子在内的调节剂可分别将 IsPETasePA 和 MHETase 的酶活性提高 1.1 倍和 2.3 倍。我们还通过动力学模拟分析了最佳离子调节剂的作用机理,它通过提高稳定性和结合能协同增强了 MHET 的降解能力。这项工作为将 BHET 完全降解为 TPA 提供了一种有价值的策略,为实现 PET 回收奠定了基础。© 2024 化学工业学会(SCI)。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
CiteScore
7.00
自引率
5.90%
发文量
268
审稿时长
1.7 months
期刊介绍: Journal of Chemical Technology and Biotechnology(JCTB) is an international, inter-disciplinary peer-reviewed journal concerned with the application of scientific discoveries and advancements in chemical and biological technology that aim towards economically and environmentally sustainable industrial processes.
期刊最新文献
Issue Information Adsorption behavior of graphite‐like walnut shell biochar modified with ammonia for ciprofloxacin in aqueous solution Eco‐friendly approaches for synthesis of indolyl 1H‐pyrroles using rice‐husk‐derived carbonaceous sulfonation as the green catalyst Impact of neutrophil‐activating protein conservation on diagnostic tests and vaccine design Issue Information
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1