Screening and Identification of a Novel Esterase EstPE from a Metagenomic DNA Library

So-Youn Park; Hyun-Jae Shin; Geun-Joong Kim

doi:10.1007/s12275-011-0201-7

Articles

Page Path: HOME > J. Microbiol > Volume 49(1); 2011 > Article

Research Support, Non-U.S. Gov't
Screening and Identification of a Novel Esterase EstPE from a Metagenomic DNA Library: So-Youn Park ¹, Hyun-Jae Shin ², Geun-Joong Kim ¹; Journal of Microbiology 2011;49(1):7-14.
DOI: https://doi.org/10.1007/s12275-011-0201-7
Published online: March 3, 2011

¹Department of Biological Sciences, College of Natural Sciences, Chonnam National University, Gwangju 500-757, Republic of Korea, ²Department of Chemical Engineering, Chosun University, Gwangju 501-759, Republic of Korea

Corresponding author: Geun-Joong Kim , Tel: +82-62-530-3403,

Received: 31 May 2010 • Accepted: 1 September 2010

prev next

74 Views
0 Download
7 Crossref
10 Scopus

Full Article

Abstract

Esterases represent a large family of hydrolases with broad substrate specificity and functional sequence space. Although many attempts to screen new esterases have been conducted, there have been few reports conducted to discriminate unique enzymes from typical ones based on novel structure and function. In this study, we discovered an esterase and a novel family through a successive assay of whole cells and crude lysates (oxidative open condition). The screened putative esterases from the metagenomic DNA of salted shrimp consisted of 753 bp encoding 27 kDa of polypeptide, namely PE esterase. Sequence analyses revealed that an identical gene was reported from whole genome sequencing of Stenotrophomonas maltophilia K279a. However, its biochemical and phylogenetic characteristics have not yet been evaluated. PE esterase was overexpressed only by the MBP fusion state in E. coli and was easily purified using an affinity column. This enzyme showed a typical spectrum of substrate specificity and possessed the consensus motifs, Ser-Asp-His and GXSXG, which are essential for most esterase/lipase superfamilies. Interestingly, the entire organization of the ORF and consensus sequence around the active site were distinct from the related enzymes, and its structure could be affected by a reducing agent, DTT.

Keywords: esterase;oxidative modulation;novel family;metagenome

Figure & Data

References

Citations

Citations to this article as recorded by

Isolation, identification, and biochemical characterization of a novel bifunctional phosphomannomutase/phosphoglucomutase from the metagenome of the brown alga Laminaria digitata
Stephen A. Jackson, Maohang Duan, Pengyan Zhang, Maureen W. Ihua, Dagmar B. Stengel, Delin Duan, Alan D. W. Dobson
Frontiers in Microbiology.2022;[Epub] CrossRef
Recombinant expression and characterization of two glycoside hydrolases from extreme alklinphilic bacterium Cellulomonas bogoriensis 69B4T
Fan Li, Jiaying Dong, Xue Lv, Yanqiu Wen, Shan Chen
AMB Express.2020;[Epub] CrossRef
Recent Advances in Function-Based Metagenomic Screening
Tanyaradzwa Rodgers Ngara, Houjin Zhang
Genomics, Proteomics & Bioinformatics.2018; 16(6): 405. CrossRef
Molecular cloning and characterization of a thermostable esterase/lipase produced by a novel Anoxybacillus flavithermus strain
Laura Chiş, Monica Hriscu, Adriana Bica, Monica Toşa, Gergely Nagy, Gergely Róna, Beata G. Vértessy, Florin Dan Irimie
The Journal of General and Applied Microbiology.2013; 59(2): 119. CrossRef
Biochemical Diversity of Carboxyl Esterases and Lipases from Lake Arreo (Spain): a Metagenomic Approach
M�nica Mart�nez-Mart�nez, Mar�a Alcaide, Anatoli Tchigvintsev, Oleg Reva, Julio Polaina, Rafael Bargiela, Mar�a-Eugenia Guazzaroni, �lvaro Chicote, Albert Canet, Francisco Valero, Eugenio Rico Eguizabal, Mar�a del Carmen Guerrero, Alexander F. Yakunin, Ma
Applied and Environmental Microbiology.2013; 79(12): 3553. CrossRef
Isolation of a thioesterase gene from the metagenome of a mountain peak, Apharwat, in the northwestern Himalayas
Avneet Kour Sudan, Jyoti Vakhlu
3 Biotech.2013; 3(1): 19. CrossRef
Discovery and Protein Engineering of Biocatalysts for Organic Synthesis
Geoffrey A. Behrens, Anke Hummel, Santosh K. Padhi, Sebastian Schätzle, Uwe T. Bornscheuer
Advanced Synthesis & Catalysis.2011; 353(13): 2191. CrossRef

Cite this Article

Cite this Article: export Copy Download Format; Close

Download Citation

Download a citation file in RIS format that can be imported by all major citation management software, including EndNote, ProCite, RefWorks, and Reference Manager.

Format:

RIS — For EndNote, ProCite, RefWorks, and most other reference management software
BibTeX — For JabRef, BibDesk, and other BibTeX-specific software

Include:

Citation for the content below
Citation and abstract for the content below

Screening and Identification of a Novel Esterase EstPE from a Metagenomic DNA Library

J. Microbiol. 2011;49(1):7-14. Published online March 3, 2011

DOI: https://doi.org/10.1007/s12275-011-0201-7

Related articles