@article{XueChenRongetal.2021,
  author    = {Rui Xue and Yinping Chen and Huan Rong and Ren Wei and Zhongli Cui and Jie Zhou and Weiliang Dong and Min Jiang},
  title     = {Fusion of Chitin-Binding Domain From Chitinolyticbacter meiyuanensis SYBC-H1 to the Leaf-Branch Compost Cutinase for Enhanced PET Hydrolysis},
  series   = {Frontiers in Bioengineering and Biotechnology},
  volume    = {9},
  publisher = {Frontiers Media S.A.},
  address   = {Lausanne},
  issn      = {2296-4185},
  doi       = {10.3389/fbioe.2021.762854},
  url       = {https://nbn-resolving.org/urn:nbn:de:gbv:9-opus-58255},
  year      = {2021},
  abstract  = {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.},
  language  = {en}
}