Autotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides

Abstract The EstPS1 gene, which encodes a novel carboxylesterase of Pseudomonas synxantha PS1 isolated from oil well-produced water, was cloned and sequenced. EstPS1 has an open reading frame of 1923 bp and encodes the 640-amino acid carboxylesterase (EstPS1), which contains an autotransporter (AT)...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Xianghai Cai, Wei Wang, Lin Lin, Dannong He, Gang Huang, Yaling Shen, Wei Wei, Dongzhi Wei
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3c6c58f0d4f84faa9a484ec5f622adfa
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:3c6c58f0d4f84faa9a484ec5f622adfa
record_format	dspace
spelling	oai:doaj.org-article:3c6c58f0d4f84faa9a484ec5f622adfa2021-12-02T15:05:27ZAutotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides10.1038/s41598-017-03561-82045-2322https://doaj.org/article/3c6c58f0d4f84faa9a484ec5f622adfa2017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03561-8https://doaj.org/toc/2045-2322Abstract The EstPS1 gene, which encodes a novel carboxylesterase of Pseudomonas synxantha PS1 isolated from oil well-produced water, was cloned and sequenced. EstPS1 has an open reading frame of 1923 bp and encodes the 640-amino acid carboxylesterase (EstPS1), which contains an autotransporter (AT) domain (357–640 amino acids). Homology analysis revealed that EstPS1 shared the highest identity (88%) with EstA from Pseudomonas fluorescens A506 (NCBI database) and belonged to the carboxylesterase family (EC 3.1.1.1). The optimum pH and temperature of recombinant EstPS1 were found to be 8.0 and 60 °C, respectively. EstPS1 showed high thermostability, and the half-lives (T1/2 thermal inactivation) at 60, 70, 80, 90, and 100 °C were 14 h, 2 h, 31 min, 10 min, and 1 min, respectively. To understand the role of the AT domain in carboxylesterase, AT domain-truncated carboxylesterase (EstPS1ΔAT) was generated. EstPS1ΔAT showed a clearly decreased secretion rate, owing to the AT domain strongly improved secretory expression in the heterogeneous system. EstPS1 degraded various pyrethroid pesticides, and hydrolysis efficiencies were dependent on the pyrethroid molecular structure. EstPS1 degraded all the tested pyrethroid pesticides and hydrolysed the p-nitrophenyl esters of medium-short-chain fatty acids, indicating that EstPS1 is an esterase with broad specificity.Xianghai CaiWei WangLin LinDannong HeGang HuangYaling ShenWei WeiDongzhi WeiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Xianghai Cai Wei Wang Lin Lin Dannong He Gang Huang Yaling Shen Wei Wei Dongzhi Wei Autotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides
description	Abstract The EstPS1 gene, which encodes a novel carboxylesterase of Pseudomonas synxantha PS1 isolated from oil well-produced water, was cloned and sequenced. EstPS1 has an open reading frame of 1923 bp and encodes the 640-amino acid carboxylesterase (EstPS1), which contains an autotransporter (AT) domain (357–640 amino acids). Homology analysis revealed that EstPS1 shared the highest identity (88%) with EstA from Pseudomonas fluorescens A506 (NCBI database) and belonged to the carboxylesterase family (EC 3.1.1.1). The optimum pH and temperature of recombinant EstPS1 were found to be 8.0 and 60 °C, respectively. EstPS1 showed high thermostability, and the half-lives (T1/2 thermal inactivation) at 60, 70, 80, 90, and 100 °C were 14 h, 2 h, 31 min, 10 min, and 1 min, respectively. To understand the role of the AT domain in carboxylesterase, AT domain-truncated carboxylesterase (EstPS1ΔAT) was generated. EstPS1ΔAT showed a clearly decreased secretion rate, owing to the AT domain strongly improved secretory expression in the heterogeneous system. EstPS1 degraded various pyrethroid pesticides, and hydrolysis efficiencies were dependent on the pyrethroid molecular structure. EstPS1 degraded all the tested pyrethroid pesticides and hydrolysed the p-nitrophenyl esters of medium-short-chain fatty acids, indicating that EstPS1 is an esterase with broad specificity.
format	article
author	Xianghai Cai Wei Wang Lin Lin Dannong He Gang Huang Yaling Shen Wei Wei Dongzhi Wei
author_facet	Xianghai Cai Wei Wang Lin Lin Dannong He Gang Huang Yaling Shen Wei Wei Dongzhi Wei
author_sort	Xianghai Cai
title	Autotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides
title_short	Autotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides
title_full	Autotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides
title_fullStr	Autotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides
title_full_unstemmed	Autotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides
title_sort	autotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/3c6c58f0d4f84faa9a484ec5f622adfa
work_keys_str_mv	AT xianghaicai autotransporterdomaindependentenzymaticanalysisofanovelextremelythermostablecarboxylesterasewithhighbiodegradabilitytowardspyrethroidpesticides AT weiwang autotransporterdomaindependentenzymaticanalysisofanovelextremelythermostablecarboxylesterasewithhighbiodegradabilitytowardspyrethroidpesticides AT linlin autotransporterdomaindependentenzymaticanalysisofanovelextremelythermostablecarboxylesterasewithhighbiodegradabilitytowardspyrethroidpesticides AT dannonghe autotransporterdomaindependentenzymaticanalysisofanovelextremelythermostablecarboxylesterasewithhighbiodegradabilitytowardspyrethroidpesticides AT ganghuang autotransporterdomaindependentenzymaticanalysisofanovelextremelythermostablecarboxylesterasewithhighbiodegradabilitytowardspyrethroidpesticides AT yalingshen autotransporterdomaindependentenzymaticanalysisofanovelextremelythermostablecarboxylesterasewithhighbiodegradabilitytowardspyrethroidpesticides AT weiwei autotransporterdomaindependentenzymaticanalysisofanovelextremelythermostablecarboxylesterasewithhighbiodegradabilitytowardspyrethroidpesticides AT dongzhiwei autotransporterdomaindependentenzymaticanalysisofanovelextremelythermostablecarboxylesterasewithhighbiodegradabilitytowardspyrethroidpesticides
_version_	1718388822913318912

Autotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides

Ejemplares similares