Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Zong, Wei, Su, Wenfeng, Xie, Qingfen, Gu, Quliang, Deng, Xinyi, Ren, Yifei, Li, He
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
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
_version_ 1784863388535357440
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
work_keys_str_mv AT zongwei expressioncharacterizationandimmobilizationofanovelsgnhesteraseest882anditspotentialforpyrethroiddegradation
AT suwenfeng expressioncharacterizationandimmobilizationofanovelsgnhesteraseest882anditspotentialforpyrethroiddegradation
AT xieqingfen expressioncharacterizationandimmobilizationofanovelsgnhesteraseest882anditspotentialforpyrethroiddegradation
AT guquliang expressioncharacterizationandimmobilizationofanovelsgnhesteraseest882anditspotentialforpyrethroiddegradation
AT dengxinyi expressioncharacterizationandimmobilizationofanovelsgnhesteraseest882anditspotentialforpyrethroiddegradation
AT renyifei expressioncharacterizationandimmobilizationofanovelsgnhesteraseest882anditspotentialforpyrethroiddegradation
AT lihe expressioncharacterizationandimmobilizationofanovelsgnhesteraseest882anditspotentialforpyrethroiddegradation