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Fusion of Chitin-Binding Domain From Chitinolyticbacter meiyuanensis SYBC-H1 to the Leaf-Branch Compost Cutinase for Enhanced PET Hydrolysis
- Polyethylene terephthalate (PET) is a mass-produced petroleum-based non-biodegradable plastic that contributes to the global plastic pollution. Recently, biocatalytic degradation has emerged as a viable recycling approach for PET waste, especially with thermophilic polyester hydrolases such as a cutinase (LCC) isolated from a leaf-branch compost metagenome and its variants. To improve the enzymatic PET hydrolysis performance, we fused a chitin-binding domain (ChBD) from Chitinolyticbacter meiyuanensis SYBC-H1 to the C-terminus of the previously reported LCCICCG variant, demonstrating higher adsorption to PET substrates and, as a result, improved degradation performance by up to 19.6% compared to with its precursor enzyme without the binding module. For compare hydrolysis with different binding module, the catalytic activity of LCCICCG-ChBD, LCCICCG-CBM, LCCICCG-PBM and LCCICCG-HFB4 were further investigated with PET substrates of various crystallinity and it showed measurable activity on high crystalline PET with 40% crystallinity. These results indicated that fusing a polymer-binding module to LCCICCG is a promising method stimulating the enzymatic hydrolysis of PET.
Author: | Rui Xue, Yinping Chen, Huan Rong, Ren Wei, Zhongli Cui, Jie Zhou, Weiliang Dong, Min Jiang |
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URN: | urn:nbn:de:gbv:9-opus-58255 |
DOI: | https://doi.org/10.3389/fbioe.2021.762854 |
ISSN: | 2296-4185 |
Parent Title (English): | Frontiers in Bioengineering and Biotechnology |
Publisher: | Frontiers Media S.A. |
Place of publication: | Lausanne |
Document Type: | Article |
Language: | English |
Date of first Publication: | 2021/12/15 |
Release Date: | 2022/07/06 |
Tag: | chitin-binding domain; hydrolysis; hydrophobicity; leaf-branch compost; polyethylene terephthalate |
GND Keyword: | - |
Volume: | 9 |
Article Number: | 762854 |
Page Number: | 9 |
Faculties: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie |
Licence (German): | Creative Commons - Namensnennung |