ArticleExtremophiles : life under extreme conditions2012
A novel, extremely alkaliphilic and cold-active esterase from Antarctic desert soil.
Article in Extremophiles : life under extreme conditions, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 50 citations in OpenAlex.
- A CALB-like Cold-Active Lipolytic Enzyme fromMarine drugs · 2025Article
- Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues.International journal of molecular sciences · 2022Review
- Diversity of protease-producing bacteria in the soils of the South Shetland Islands, Antarctica.Antonie van Leeuwenhoek · 2021Article
- Recent Advances in Function-based Metagenomic Screening.Genomics, proteomics & bioinformatics · 2018Review
- Cloning, expression and characterization of a novel cold-active and organic solvent-tolerant esterase from Monascus ruber M7.Extremophiles : life under extreme conditions · 2016Article
- A novel cold-adapted and highly salt-tolerant esterase from Alkalibacterium sp. SL3 from the sediment of a soda lake.Scientific reports · 2016Article
- Characterization of a cold-active and salt tolerant esterase identified by functional screening of Arctic metagenomic libraries.BMC biochemistry · 2016Article
- Cloning, expression and characterization of a novel cold‑adapted GDSL family esterase from Photobacterium sp. strain J15.Extremophiles : life under extreme conditions · 2016Article
- Isolation and Characterization of a Novel Cold-Adapted Esterase, MtEst45, from Microbulbifer thermotolerans DAU221.Frontiers in microbiology · 2016Article
- Improved cultivation and metagenomics as new tools for bioprospecting in cold environments.Extremophiles : life under extreme conditions · 2015Review
- Synthetic biology approaches to improve biocatalyst identification in metagenomic library screening.Microbial biotechnology · 2015Review
- Characterization of a novel cold-active esterase isolated from swamp sediment metagenome.World journal of microbiology & biotechnology · 2014Article
- Characterization of EstB, a novel cold-active and organic solvent-tolerant esterase from marine microorganism Alcanivorax dieselolei B-5(T).Extremophiles : life under extreme conditions · 2014Article
- New extremophilic lipases and esterases from metagenomics.Current protein & peptide science · 2014Review
- Isolation and characterization of a metagenome-derived thermoalkaliphilic esterase with high stability over a broad pH range.Extremophiles : life under extreme conditions · 2013Article
- Cloning, overexpression in Escherichia coli, and characterization of a thermostable fungal acetylxylan esterase from Talaromyces emersonii.Applied and environmental microbiology · 2012Article
- Biocatalysts and small molecule products from metagenomic studies.Current opinion in chemical biology · 2012Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel, cold-active and highly alkaliphilic esterase was isolated from an Antarctic desert soil metagenomic library by functional screening. The 1,044 bp gene sequence contained several conserved regions common to lipases/esterases, but lacked clear classification based on sequence analysis alone. Moderate (<40%) amino acid sequence similarity to known esterases was apparent (the closest neighbour being a hypothetical protein from Chitinophaga pinensis), despite phylogenetic distance to many of the lipolytic "families". The enzyme functionally demonstrated activity towards shorter chain p-nitrophenyl esters with the optimal activity recorded towards p-nitrophenyl propionate (C3). The enzyme possessed an apparent T(opt) at 20°C and a pH optimum at pH 11. Esterases possessing such extreme alkaliphily are rare and so this enzyme represents an intriguing novel locus in protein sequence space. A metagenomic approach has been shown, in this case, to yield an enzyme with quite different sequential/structural properties to known lipases. It serves as an excellent candidate for analysis of the molecular mechanisms responsible for both cold and alkaline activity and novel structure-function relationships of esterase activity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.