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Expression, characterization, and immobilization of a novel SGNH esterase Est882 and its potential for pyrethroid degradation
The widely-used pyrethroid pesticides have attracted public attention because of their potentials to cause environmental pollution and toxic effects on non-target organisms. Esterase is a kind of hydrolytic enzyme that can catalyze the cleavage or formation of ester bonds. it plays a pivotal role in...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9810817/ https://www.ncbi.nlm.nih.gov/pubmed/36620037 http://dx.doi.org/10.3389/fmicb.2022.1069754 |
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author | Zong, Wei Su, Wenfeng Xie, Qingfen Gu, Quliang Deng, Xinyi Ren, Yifei Li, He |
author_facet | Zong, Wei Su, Wenfeng Xie, Qingfen Gu, Quliang Deng, Xinyi Ren, Yifei Li, He |
author_sort | Zong, Wei |
collection | PubMed |
description | The widely-used pyrethroid pesticides have attracted public attention because of their potentials to cause environmental pollution and toxic effects on non-target organisms. Esterase is a kind of hydrolytic enzyme that can catalyze the cleavage or formation of ester bonds. it plays a pivotal role in the decomposition of pyrethroids and esters containing industrial pollutants through the hydrolysis of ester bonds. Here, a new esterase gene est882 was successfully screened, which encodes Est882, a SGNH family esterase composed of 294 amino acids. It was heterogeneously expressed, identified and immobilized. Multiple sequence alignment showed that Est882 had a typical GDS(X) conserved motif and a catalytic triad composed of Ser79, Asp269 and His275. Phylogenetic analysis showed that Est882 shall belong to a new esterase family. Biochemical characterization demonstrated that the optimum condition was 40°C and pH 9.0. Est882 immobilization was studied with mesoporous silica SBA-15 as the carrier and found to significantly improve the tolerance and stability of Est882. Its optimum pH increased to 10.0 and stabilized within pH 8.0–11.0. Free Est882 can effectively degrade various pyrethroids within 30 min, with a degradation rate above 80%. The immobilized Est882 yet degraded more than 70% of pyrethroids within 30 min. The present study indicated that Est882 has outstanding potential in bioremediation of a pyrethroid-polluted environment. These characteristics endow Est882 with potential values in various industrial applications and hydrolysis of pyrethroid residues. |
format | Online Article Text |
id | pubmed-9810817 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-98108172023-01-05 Expression, characterization, and immobilization of a novel SGNH esterase Est882 and its potential for pyrethroid degradation Zong, Wei Su, Wenfeng Xie, Qingfen Gu, Quliang Deng, Xinyi Ren, Yifei Li, He Front Microbiol Microbiology The widely-used pyrethroid pesticides have attracted public attention because of their potentials to cause environmental pollution and toxic effects on non-target organisms. Esterase is a kind of hydrolytic enzyme that can catalyze the cleavage or formation of ester bonds. it plays a pivotal role in the decomposition of pyrethroids and esters containing industrial pollutants through the hydrolysis of ester bonds. Here, a new esterase gene est882 was successfully screened, which encodes Est882, a SGNH family esterase composed of 294 amino acids. It was heterogeneously expressed, identified and immobilized. Multiple sequence alignment showed that Est882 had a typical GDS(X) conserved motif and a catalytic triad composed of Ser79, Asp269 and His275. Phylogenetic analysis showed that Est882 shall belong to a new esterase family. Biochemical characterization demonstrated that the optimum condition was 40°C and pH 9.0. Est882 immobilization was studied with mesoporous silica SBA-15 as the carrier and found to significantly improve the tolerance and stability of Est882. Its optimum pH increased to 10.0 and stabilized within pH 8.0–11.0. Free Est882 can effectively degrade various pyrethroids within 30 min, with a degradation rate above 80%. The immobilized Est882 yet degraded more than 70% of pyrethroids within 30 min. The present study indicated that Est882 has outstanding potential in bioremediation of a pyrethroid-polluted environment. These characteristics endow Est882 with potential values in various industrial applications and hydrolysis of pyrethroid residues. Frontiers Media S.A. 2022-12-21 /pmc/articles/PMC9810817/ /pubmed/36620037 http://dx.doi.org/10.3389/fmicb.2022.1069754 Text en Copyright © 2022 Zong, Su, Xie, Gu, Deng, Ren and Li. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Zong, Wei Su, Wenfeng Xie, Qingfen Gu, Quliang Deng, Xinyi Ren, Yifei Li, He Expression, characterization, and immobilization of a novel SGNH esterase Est882 and its potential for pyrethroid degradation |
title | Expression, characterization, and immobilization of a novel SGNH esterase Est882 and its potential for pyrethroid degradation |
title_full | Expression, characterization, and immobilization of a novel SGNH esterase Est882 and its potential for pyrethroid degradation |
title_fullStr | Expression, characterization, and immobilization of a novel SGNH esterase Est882 and its potential for pyrethroid degradation |
title_full_unstemmed | Expression, characterization, and immobilization of a novel SGNH esterase Est882 and its potential for pyrethroid degradation |
title_short | Expression, characterization, and immobilization of a novel SGNH esterase Est882 and its potential for pyrethroid degradation |
title_sort | expression, characterization, and immobilization of a novel sgnh esterase est882 and its potential for pyrethroid degradation |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9810817/ https://www.ncbi.nlm.nih.gov/pubmed/36620037 http://dx.doi.org/10.3389/fmicb.2022.1069754 |
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