ReviewMicroorganisms2015
Thermus thermophilus as a Source of Thermostable Lipolytic Enzymes.
Review in Microorganisms, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Production of Novel Thermostable Esterases fromInternational journal of molecular sciences · 2026Article
- It Is Dangerous to Go Alone: Strategies to Optimize PET Biocatalysis and Upcycling through Enzymatic Synergism.ACS omega · 2025Review
- Precision Thermostability Predictions: Leveraging Machine Learning for Examining Laccases and Their Associated Genes.International journal of molecular sciences · 2024Article
- Longitudinal analysis of the Five Sisters hot springs in Yellowstone National Park reveals a dynamic thermoalkaline environment.Scientific reports · 2022Article
- Proteins from ThermophilicACS omega · 2022Article
- Reactivity of a Recombinant Esterase fromMicroorganisms · 2022Article
- Complete Genome Sequencing of Thermus thermophilus Strain HC11, Isolated from Mine Geyser in Japan.Microbiology resource announcements · 2019Article
- Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach.Extremophiles : life under extreme conditions · 2019Article
- Metagenomics of Thermophiles with a Focus on Discovery of Novel Thermozymes.Frontiers in microbiology · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipolytic enzymes, esterases (EC 3.1.1.1) and lipases (EC 3.1.1.3), catalyze the hydrolysis of ester bonds between alcohols and carboxylic acids, and its formation in organic media. At present, they represent about 20% of commercialized enzymes for industrial use. Lipolytic enzymes from thermophilic microorganisms are preferred for industrial use to their mesophilic counterparts, mainly due to higher thermostability and resistance to several denaturing agents. However, the production at an industrial scale from the native organisms is technically complicated and expensive. The thermophilic bacterium Thermus thermophilus (T. thermophilus) has high levels of lipolytic activity, and its whole genome has been sequenced. One esterase from the T. thermophilus strain HB27 has been widely characterized, both in its native form and in recombinant forms, being expressed in mesophilic microorganisms. Other putative lipases/esterases annotated in the T. thermophilus genome have been explored and will also be reviewed in this paper.
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What OpenQuestion holds
Registered trials
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.