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Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis.

Authors
  • Liu, Congcong1
  • Shi, Chao2
  • Zhu, Sujie3
  • Wei, Risheng4
  • Yin, Chang-Cheng5
  • 1 Department of Biophysics, The Health Science Center, Peking University, Beijing, 100191, China. Electronic address: [email protected] , (China)
  • 2 Department of Biophysics, The Health Science Center, Peking University, Beijing, 100191, China. Electronic address: [email protected] , (China)
  • 3 Department of Biophysics, The Health Science Center, Peking University, Beijing, 100191, China. Electronic address: [email protected] , (China)
  • 4 Department of Biophysics, The Health Science Center, Peking University, Beijing, 100191, China. Electronic address: [email protected] , (China)
  • 5 Department of Biophysics, The Health Science Center, Peking University, Beijing, 100191, China; Electron Microscopy Analysis Laboratory, The Health Science Center, Peking University, Beijing, 100191, China; Center for Protein Science, Peking University, Beijing, 100871, China. Electronic address: [email protected] , (China)
Type
Published Article
Journal
Biochemical and Biophysical Research Communications
Publisher
Elsevier
Publication Date
Jan 01, 2019
Volume
508
Issue
1
Pages
289–294
Identifiers
DOI: 10.1016/j.bbrc.2018.11.148
PMID: 30502092
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Polyethylene terephthalate (PET) hydrolase from Ideonella sakaiensis (IsPETase) can be used to degrade PET. In order to use IsPETase in industry, we studied the enzymatic activity of IsPETase in different conditions containing environmental and physicochemical factors commonly found in nature. We observed that salts and glycerol enhanced the enzymatic activity, while detergents and organic solvents reduced the enzymatic activity. IsPETase hydrolyzed p-nitrophenyl (p-NP) esters instead of naphthyl esters. To make IsPETase an enzyme capable of hydrolyzing naphthyl esters, site-directed mutagenesis was carried out based on the structural information provided by the crystal structure. We found that the IsPETaseS93M, IsPETaseW159F, and IsPETaseN241F mutants can hydrolyze naphthyl esters. IsPETase engineering can direct researchers to use this α/β-hydrolase protein scaffold to design enzymes that can hydrolyze a variety of polyesters. Copyright © 2018 Elsevier Inc. All rights reserved.

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