Journal
FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY
Volume 9, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fbioe.2021.762854
Keywords
chitin-binding domain; polyethylene terephthalate; hydrolysis; leaf-branch compost; hydrophobicity
Funding
- National Key R and D Program of China [2019YFA0905500]
- National Natural Science Foundation of China [31961133017, 21978129, 21908102]
- Jiangsu Association for Science and Technology Young Scientific and Technological Talents Support Project [TJ-2021-092]
- NSFC
- European Union [870294]
- EU
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A new method has been developed to fuse a chitin-binding domain from Chitinolyticbacter meiyuanensis SYBC-H1 to a cutinase, improving its adsorption to PET substrates and enhancing degradation performance by up to 19.6% compared to the precursor enzyme. This approach shows promising potential in stimulating the enzymatic hydrolysis of PET by fusing a polymer-binding module to the enzyme.
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.
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