ArticleBiomolecules2019
Thermal Inactivation of a Cold-Active Esterase PMGL3 Isolated from the Permafrost Metagenomic Library.
Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Identification of Cutinolytic Esterase from Microplastic-Associated Microbiota Using Functional Metagenomics and Its Plastic Degrading Potential.Molecular biotechnology · 2024Article
- Enzymatic Characterization of a Novel HSL Family IV Esterase EstD04 fromMolecules (Basel, Switzerland) · 2023Article
- Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst.International journal of molecular sciences · 2023Review
- Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic BacteriumBiomolecules · 2021Article
- Industrial applications of cold-adapted enzymes: challenges, innovations and future perspective.3 Biotech · 2021Review
- Microbial characterisation and Cold-Adapted Predicted Protein (CAPP) database construction from the active layer of Greenland's permafrost.FEMS microbiology ecology · 2021Article
- Structural and Biochemical Characterization of a Cold-Active PMGL3 Esterase with Unusual Oligomeric Structure.Biomolecules · 2021Article
- A Broad Temperature Active Lipase Purified From a Psychrotrophic Bacterium of Sikkim Himalaya With Potential Application in Detergent Formulation.Frontiers in bioengineering and biotechnology · 2020Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PMGL3 is a cold-adapted esterase which was recently isolated from the permafrost metagenomic library. It exhibits maximum activity at 30 °C and low stability at elevated temperatures (40 °C and higher). Sequence alignment has revealed that PMGL3 is a member of the hormone-sensitive lipase (HSL) family. In this work, we demonstrated that incubation at 40 °C led to the inactivation of the enzyme (
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