Biochemical characterization of a first fungal esterase from Rhizomucor miehei showing high efficiency of ester synthesis.

<h4>Background</h4>Esterases with excellent merits suitable for commercial use in ester production field are still insufficient. The aim of this research is to advance our understanding by seeking for more unusual esterases and revealing their characterizations for ester synthesis.<h4...

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Autores principales:	Yu Liu, Haibo Xu, Qiaojuan Yan, Shaoqing Yang, Xiaojie Duan, Zhengqiang Jiang
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/95664d38d6884da2ba21b357c9aa741f
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spelling	oai:doaj.org-article:95664d38d6884da2ba21b357c9aa741f2021-11-18T08:48:57ZBiochemical characterization of a first fungal esterase from Rhizomucor miehei showing high efficiency of ester synthesis.1932-620310.1371/journal.pone.0077856https://doaj.org/article/95664d38d6884da2ba21b357c9aa741f2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24204998/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Esterases with excellent merits suitable for commercial use in ester production field are still insufficient. The aim of this research is to advance our understanding by seeking for more unusual esterases and revealing their characterizations for ester synthesis.<h4>Methodology/principal findings</h4>A novel esterase-encoding gene from Rhizomucor miehei (RmEstA) was cloned and expressed in Escherichia coli. Sequence analysis revealed a 975-bp ORF encoding a 324-amino-acid polypeptide belonging to the hormone-sensitive lipase (HSL) family IV and showing highest similarity (44%) to the Paenibacillus mucilaginosus esterase/lipase. Recombinant RmEstA was purified to homogeneity: it was 34 kDa by SDS-PAGE and showed optimal pH and temperature of 6.5 and 45°C, respectively. The enzyme was stable to 50°C, under a broad pH range (5.0-10.6). RmEstA exhibited broad substrate specificity toward p-nitrophenol esters and short-acyl-chain triglycerols, with highest activities (1,480 U mg(-1) and 228 U mg(-1)) for p-nitrophenyl hexanoate and tributyrin, respectively. RmEstA efficiently synthesized butyl butyrate (92% conversion yield) when immobilized on AOT-based organogel.<h4>Conclusion</h4>RmEstA has great potential for industrial applications. RmEstA is the first reported esterase from Rhizomucor miehei.Yu LiuHaibo XuQiaojuan YanShaoqing YangXiaojie DuanZhengqiang JiangPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 10, p e77856 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yu Liu Haibo Xu Qiaojuan Yan Shaoqing Yang Xiaojie Duan Zhengqiang Jiang Biochemical characterization of a first fungal esterase from Rhizomucor miehei showing high efficiency of ester synthesis.
description	<h4>Background</h4>Esterases with excellent merits suitable for commercial use in ester production field are still insufficient. The aim of this research is to advance our understanding by seeking for more unusual esterases and revealing their characterizations for ester synthesis.<h4>Methodology/principal findings</h4>A novel esterase-encoding gene from Rhizomucor miehei (RmEstA) was cloned and expressed in Escherichia coli. Sequence analysis revealed a 975-bp ORF encoding a 324-amino-acid polypeptide belonging to the hormone-sensitive lipase (HSL) family IV and showing highest similarity (44%) to the Paenibacillus mucilaginosus esterase/lipase. Recombinant RmEstA was purified to homogeneity: it was 34 kDa by SDS-PAGE and showed optimal pH and temperature of 6.5 and 45°C, respectively. The enzyme was stable to 50°C, under a broad pH range (5.0-10.6). RmEstA exhibited broad substrate specificity toward p-nitrophenol esters and short-acyl-chain triglycerols, with highest activities (1,480 U mg(-1) and 228 U mg(-1)) for p-nitrophenyl hexanoate and tributyrin, respectively. RmEstA efficiently synthesized butyl butyrate (92% conversion yield) when immobilized on AOT-based organogel.<h4>Conclusion</h4>RmEstA has great potential for industrial applications. RmEstA is the first reported esterase from Rhizomucor miehei.
format	article
author	Yu Liu Haibo Xu Qiaojuan Yan Shaoqing Yang Xiaojie Duan Zhengqiang Jiang
author_facet	Yu Liu Haibo Xu Qiaojuan Yan Shaoqing Yang Xiaojie Duan Zhengqiang Jiang
author_sort	Yu Liu
title	Biochemical characterization of a first fungal esterase from Rhizomucor miehei showing high efficiency of ester synthesis.
title_short	Biochemical characterization of a first fungal esterase from Rhizomucor miehei showing high efficiency of ester synthesis.
title_full	Biochemical characterization of a first fungal esterase from Rhizomucor miehei showing high efficiency of ester synthesis.
title_fullStr	Biochemical characterization of a first fungal esterase from Rhizomucor miehei showing high efficiency of ester synthesis.
title_full_unstemmed	Biochemical characterization of a first fungal esterase from Rhizomucor miehei showing high efficiency of ester synthesis.
title_sort	biochemical characterization of a first fungal esterase from rhizomucor miehei showing high efficiency of ester synthesis.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/95664d38d6884da2ba21b357c9aa741f
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Biochemical characterization of a first fungal esterase from Rhizomucor miehei showing high efficiency of ester synthesis.

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