ArticleBiology2013
Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome.
Article in Biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- Biodegradation and metabolic assimilation of poly (butylene adipate-co-terephthalate) (PBAT) by Gordonia sp. CN2K.Biodegradation · 2026Article
- Expression and characterization of Est2: a novel cold-adapted esterase from Antarctic bacterium defining the new esterase family XXII.Frontiers in microbiology · 2025Article
- Characterization of a Novel Esterase Est33 From an Antarctic Bacterium: A Representative of a New Esterase Family.Frontiers in microbiology · 2022Article
- Discovery of a Novel Gene Conferring Tellurite Tolerance Through Tellurite Reduction to Escherichia coli Transformant in Marine Sediment Metagenomic Library.Marine biotechnology (New York, N.Y.) · 2019Article
- GeneHunt for rapid domain-specific annotation of glycoside hydrolases.Scientific reports · 2019Article
- The future of genomics in polar and alpine cyanobacteria.FEMS microbiology ecology · 2018Article
- A novel cold-adapted esterase from Enterobacter cloacae: Characterization and improvement of its activity and thermostability via the site of Tyr193Cys.Microbial cell factories · 2018Article
- Amplicon-Metagenomic Analysis of Fungi from Antarctic Terrestrial Habitats.Frontiers in microbiology · 2017Article
- Characterization of a cold-active and salt tolerant esterase identified by functional screening of Arctic metagenomic libraries.BMC biochemistry · 2016Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An Antarctic soil metagenomic library was screened for lipolytic enzymes and allowed for the isolation of a new cytosolic esterase from the a/b hydrolase family 6, named MHlip. This enzyme is related to hypothetical genes coding esterases, aryl-esterases and peroxydases, among others. MHlip was produced, purified and its activity was determined. The substrate profile of MHlip reveals a high specificity for short p-nitrophenyl-esters. The apparent optimal activity of MHlip was measured for p-nitrophenyl-acetate, at 33 °C, in the pH range of 6-9. The MHlip thermal unfolding was investigated by spectrophotometric methods, highlighting a transition (Tm) at 50 °C. The biochemical characterization of this enzyme showed its adaptation to cold temperatures, even when it did not present evident signatures associated with cold-adapted proteins. Thus, MHlip adaptation to cold probably results from many discrete structural modifications, allowing the protein to remain active at low temperatures. Functional metagenomics is a powerful approach to isolate new enzymes with tailored biophysical properties (e.g., cold adaptation). In addition, beside the ever growing amount of sequenced DNA, the functional characterization of new catalysts derived from environment is still required, especially for poorly characterized protein families like α/b hydrolases.
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Registered trials
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