skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Screening and Characterization of Novel Polyesterases from Environmental Metagenomes with High Hydrolytic Activity against Synthetic Polyesters

Abstract

The continuous growth of global plastics production, including polyesters, has resulted in increasing plastic pollution and subsequent negative environmental impacts. Therefore, enzyme-catalyzed depolymerization of synthetic polyesters as a plastics recycling approach has become a focus of research. In this study, we screened over 200 purified uncharacterized hydrolases from environmental metagenomes and sequenced microbial genomes and identified at least 10 proteins with high hydrolytic activity against synthetic polyesters. These include the metagenomic esterases MGS0156 and GEN0105, which hydrolyzed polylactic acid (PLA), polycaprolactone, as well as bis-(benzoyloxyethyl)-terephthalate. With solid PLA as a substrate, both enzymes produced a mixture of lactic acid monomers, dimers, and higher oligomers as products. The crystal structure of MGS0156 was determined at 1.95 angstrom resolution and revealed a modified alpha/beta hydrolase fold, with a lid domain and highly hydrophobic active site. Mutational studies of MGS0156 identified the residues critical for hydrolytic activity against both polyester and monoester substrates, with two-times higher polyesterase activity in the MGS0156 L169A mutant protein. Thus, our work identified novel, highly active polyesterases in environmental metagenomes and provided molecular insights into their activity, thereby augmenting our understanding of enzymatic polyester hydrolysis.

Authors:
; ; ; ; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
Genome Canada; Ontario Research Fund; Natural Sciences and Engineering Research Council of Canada (NSERC); USDOE Office of Science - Office of Biological and Environmental Research; European Regional Development Fund (ERDF); Biotechnology and Biological Sciences Research Council (BBSRC)
OSTI Identifier:
1514888
DOE Contract Number:  
AC02-06CH11357
Resource Type:
Journal Article
Journal Name:
Environmental Science and Technology
Additional Journal Information:
Journal Volume: 52; Journal Issue: 21
Country of Publication:
United States
Language:
English

Citation Formats

Hajighasemi, Mahbod, Tchigvintsev, Anatoly, Nocek, Boguslaw, Flick, Robert, Popovic, Ana, Hai, Tran, khusnutdinova, Anna, Brown, Greg, Xu, Xiaohui, Cui, Hong, Anstett, Julia, Joachimiak, Andrzej, and Yakunin, Alexander. Screening and Characterization of Novel Polyesterases from Environmental Metagenomes with High Hydrolytic Activity against Synthetic Polyesters. United States: N. p., 2018. Web. doi:10.1021/acs.est.8b04252.
Hajighasemi, Mahbod, Tchigvintsev, Anatoly, Nocek, Boguslaw, Flick, Robert, Popovic, Ana, Hai, Tran, khusnutdinova, Anna, Brown, Greg, Xu, Xiaohui, Cui, Hong, Anstett, Julia, Joachimiak, Andrzej, & Yakunin, Alexander. Screening and Characterization of Novel Polyesterases from Environmental Metagenomes with High Hydrolytic Activity against Synthetic Polyesters. United States. doi:10.1021/acs.est.8b04252.
Hajighasemi, Mahbod, Tchigvintsev, Anatoly, Nocek, Boguslaw, Flick, Robert, Popovic, Ana, Hai, Tran, khusnutdinova, Anna, Brown, Greg, Xu, Xiaohui, Cui, Hong, Anstett, Julia, Joachimiak, Andrzej, and Yakunin, Alexander. Tue . "Screening and Characterization of Novel Polyesterases from Environmental Metagenomes with High Hydrolytic Activity against Synthetic Polyesters". United States. doi:10.1021/acs.est.8b04252.
@article{osti_1514888,
title = {Screening and Characterization of Novel Polyesterases from Environmental Metagenomes with High Hydrolytic Activity against Synthetic Polyesters},
author = {Hajighasemi, Mahbod and Tchigvintsev, Anatoly and Nocek, Boguslaw and Flick, Robert and Popovic, Ana and Hai, Tran and khusnutdinova, Anna and Brown, Greg and Xu, Xiaohui and Cui, Hong and Anstett, Julia and Joachimiak, Andrzej and Yakunin, Alexander},
abstractNote = {The continuous growth of global plastics production, including polyesters, has resulted in increasing plastic pollution and subsequent negative environmental impacts. Therefore, enzyme-catalyzed depolymerization of synthetic polyesters as a plastics recycling approach has become a focus of research. In this study, we screened over 200 purified uncharacterized hydrolases from environmental metagenomes and sequenced microbial genomes and identified at least 10 proteins with high hydrolytic activity against synthetic polyesters. These include the metagenomic esterases MGS0156 and GEN0105, which hydrolyzed polylactic acid (PLA), polycaprolactone, as well as bis-(benzoyloxyethyl)-terephthalate. With solid PLA as a substrate, both enzymes produced a mixture of lactic acid monomers, dimers, and higher oligomers as products. The crystal structure of MGS0156 was determined at 1.95 angstrom resolution and revealed a modified alpha/beta hydrolase fold, with a lid domain and highly hydrophobic active site. Mutational studies of MGS0156 identified the residues critical for hydrolytic activity against both polyester and monoester substrates, with two-times higher polyesterase activity in the MGS0156 L169A mutant protein. Thus, our work identified novel, highly active polyesterases in environmental metagenomes and provided molecular insights into their activity, thereby augmenting our understanding of enzymatic polyester hydrolysis.},
doi = {10.1021/acs.est.8b04252},
journal = {Environmental Science and Technology},
number = 21,
volume = 52,
place = {United States},
year = {2018},
month = {11}
}