Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation
文献类型:期刊论文
作者 | Jia, Yunpu1,2; Samak, Nadia A.3; Hao, Xuemi1,2; Chen, Zheng1,2; Wen, Qifeng1,2; Xing, Jianmin1,2,4 |
刊名 | FRONTIERS IN MICROBIOLOGY |
出版日期 | 2022-09-29 |
卷号 | 13页码:11 |
关键词 | PET biodegradation whole-cell catalysis extracellular protein production polyethylene terephthalate surface display PETase |
DOI | 10.3389/fmicb.2022.1005480 |
英文摘要 | Remarkably, a hydrolase from Ideonella sakaiensis 201-F6, termed PETase, exhibits great potential in polyethylene terephthalate (PET) waste management due to it can efficiently degrade PET under moderate conditions. However, its low yield and poor accessibility to bulky substrates hamper its further industrial application. Herein a multigene fusion strategy is introduced for constructing a hydrophobic cell surface display (HCSD) system in Escherichia coli as a robust, recyclable, and sustainable whole-cell catalyst. The truncated outer membrane hybrid protein FadL exposed the PETase and hydrophobic protein HFBII on the surface of E. coli with efficient PET accessibility and degradation performance. E. coli containing the HCSD system changed the surface tension of the bacterial solution, resulting in a smaller contact angle (83.9 +/- 2 degrees vs. 58.5 +/- 1 degrees) of the system on the PET surface, thus giving a better opportunity for PETase to interact with PET. Furthermore, pretreatment of PET with HCSD showed rougher surfaces with greater hydrophilicity (water contact angle of 68.4 +/- 1 degrees vs. 106.1 +/- 2 degrees) than the non-pretreated ones. Moreover, the HCSD system showed excellent sustainable degradation performance for PET bottles with a higher degradation rate than free PETase. The HCSD degradation system also had excellent stability, maintaining 73% of its initial activity after 7 days of incubation at 40 degrees C and retaining 70% activity after seven cycles. This study indicates that the HCSD system could be used as a novel catalyst for efficiently accelerating PET biodegradation. |
WOS关键词 | ANCHORING MOTIF ; LIPASE ; CUTINASE ; FUSION ; ENZYME ; RESOLUTION ; HYDROLASE ; CELLULOSE ; DOMAIN ; FADL |
资助项目 | National Natural Science Foundation of China[31961133017] ; National Natural Science Foundation of China[31961133018] ; National Natural Science Foundation of China[31961133019] ; European Union's Horizon 2020 research and innovation programme[870294] |
WOS研究方向 | Microbiology |
语种 | 英语 |
出版者 | FRONTIERS MEDIA SA |
WOS记录号 | WOS:000868568800001 |
资助机构 | National Natural Science Foundation of China ; European Union's Horizon 2020 research and innovation programme |
源URL | [http://ir.ipe.ac.cn/handle/122111/55155] |
专题 | 中国科学院过程工程研究所 |
通讯作者 | Xing, Jianmin |
作者单位 | 1.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, CAS Key Lab Green Proc & Engn, Beijing, Peoples R China 2.Univ Chinese Acad Sci, Coll Chem Engn, Beijing, Peoples R China 3.Univ Duisburg Essen, Environm Microbiol & Biotechnol, Aquat Microbiol, Essen, Germany 4.Chem & Chem Engn Guangdong Lab, Shantou, Peoples R China |
推荐引用方式 GB/T 7714 | Jia, Yunpu,Samak, Nadia A.,Hao, Xuemi,et al. Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation[J]. FRONTIERS IN MICROBIOLOGY,2022,13:11. |
APA | Jia, Yunpu,Samak, Nadia A.,Hao, Xuemi,Chen, Zheng,Wen, Qifeng,&Xing, Jianmin.(2022).Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation.FRONTIERS IN MICROBIOLOGY,13,11. |
MLA | Jia, Yunpu,et al."Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation".FRONTIERS IN MICROBIOLOGY 13(2022):11. |
入库方式: OAI收割
来源:过程工程研究所
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