Structural highlights
Publication Abstract from PubMed
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 IsPETase(S93M), IsPETase(W159F), and IsPETase(N241F) mutants can hydrolyze naphthyl esters. IsPETase engineering can direct researchers to use this alpha/beta-hydrolase protein scaffold to design enzymes that can hydrolyze a variety of polyesters.
Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis.,Liu C, Shi C, Zhu S, Wei R, Yin CC Biochem Biophys Res Commun. 2019 Jan 1;508(1):289-294. doi:, 10.1016/j.bbrc.2018.11.148. Epub 2018 Nov 27. PMID:30502092[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu C, Shi C, Zhu S, Wei R, Yin CC. Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis. Biochem Biophys Res Commun. 2019 Jan 1;508(1):289-294. doi:, 10.1016/j.bbrc.2018.11.148. Epub 2018 Nov 27. PMID:30502092 doi:http://dx.doi.org/10.1016/j.bbrc.2018.11.148
