Cargando…
Computational design of highly efficient thermostable MHET hydrolases and dual enzyme system for PET recycling
Recently developed enzymes for the depolymerization of polyethylene terephthalate (PET) such as FAST-PETase and LCC-ICCG are inhibited by the intermediate PET product mono(2-hydroxyethyl) terephthalate (MHET). Consequently, the conversion of PET enzymatically into its constituent monomers terephthal...
Autores principales: | Zhang, Jun, Wang, Hongzhao, Luo, Zhaorong, Yang, Zhenwu, Zhang, Zixuan, Wang, Pengyu, Li, Mengyu, Zhang, Yi, Feng, Yue, Lu, Diannan, Zhu, Yushan |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10636135/ https://www.ncbi.nlm.nih.gov/pubmed/37945666 http://dx.doi.org/10.1038/s42003-023-05523-5 |
Ejemplares similares
-
Molecular docking analysis of PET with MHET
por: D Gowda, Omkar, et al.
Publicado: (2023) -
DeepTM: A deep learning algorithm for prediction of melting temperature of thermophilic proteins directly from sequences
por: Li, Mengyu, et al.
Publicado: (2023) -
Development of a yeast whole-cell biocatalyst for MHET conversion into terephthalic acid and ethylene glycol
por: Loll-Krippleber, Raphael, et al.
Publicado: (2022) -
Discovery and mechanism-guided engineering of BHET hydrolases for improved PET recycling and upcycling
por: Li, Anni, et al.
Publicado: (2023) -
Structural Insight Into Chitin Degradation and Thermostability of a Novel Endochitinase From the Glycoside Hydrolase Family 18
por: Wang, Yan-Jun, et al.
Publicado: (2019)