ArticleMicrobial cell factories2017
Thermus thermophilus as source of thermozymes for biotechnological applications: homologous expression and biochemical characterization of an α-galactosidase.
Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
23 citing papers in PubMed, 55 citations in OpenAlex.
- Draft genome sequences ofMicrobiology resource announcements · 2025Article
- Construction of primary chassis cells with efficient protein expression in Thermus thermophilus.Microbial cell factories · 2025Article
- Transcriptome Analysis of the Regulatory Mechanisms of Holly (Plants (Basel, Switzerland) · 2024Article
- Growth characteristics, redox potential changes and proton motive force generation inAIMS microbiology · 2024Article
- Genome-scale flux balance analysis reveals redox trade-offs in the metabolism of the thermoacidophileFrontiers in systems biology · 2024Article
- Article
- Article
- Molecular advances in microbial α-galactosidases: challenges and prospects.World journal of microbiology & biotechnology · 2022Review
- A Comparative Analysis ofInternational journal of molecular sciences · 2022Article
- A New Strategy for As(V) Biosensing Based on the Inhibition of the Phosphatase Activity of the Arsenate Reductase fromInternational journal of molecular sciences · 2022Article
- Article
- Article
- Extremophiles, a Nifty Tool to Face Environmental Pollution: From Exploitation of Metabolism to Genome Engineering.International journal of environmental research and public health · 2021Review
- Prebiotic properties of Bacillus coagulans MA-13: production of galactoside hydrolyzing enzymes and characterization of the transglycosylation properties of a GH42 β-galactosidase.Microbial cell factories · 2021Article
- Self-assembling thermostable chimeras as new platform for arsenic biosensing.Scientific reports · 2021Article
- Development of a new gene expression vector for Thermus thermophilus using a silica-inducible promoter.Microbial cell factories · 2020Article
- Characterization of a highly stable α-galactosidase from thermophilic Rasamsonia emersonii heterologously expressed in a modified Pichia pastoris expression system.Microbial cell factories · 2019Article
- Draft Genome Sequence of Bacillus coagulans MA-13, a Thermophilic Lactic Acid Producer from Lignocellulose.Microbiology resource announcements · 2019Article
- Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications.World journal of microbiology & biotechnology · 2019Review
- Seed culture pre-adaptation ofBiotechnology for biofuels · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe genus Thermus, which has been considered for a long time as a fruitful source of biotechnological relevant enzymes, has emerged more recently as suitable host to overproduce thermozymes. Among these, α-galactosidases are widely used in several industrial bioprocesses that require high working temperatures and for which thermostable variants offer considerable advantages over their thermolabile counterparts.
resultsThermus thermophilus HB27 strain was used for the homologous expression of the TTP0072 gene encoding for an α-galactosidase (TtGalA). Interestingly, a soluble and active histidine-tagged enzyme was produced in larger amounts (5 mg/L) in this thermophilic host than in Escherichia coli (0.5 mg/L). The purified recombinant enzyme showed an optimal activity at 90 °C and retained more than 40% of activity over a broad range of pH (from 5 to 8).
conclusionsTtGalA is among the most thermoactive and thermostable α-galactosidases discovered so far, thus pointing to T. thermophilus as cell factory for the recombinant production of biocatalysts active at temperature values over 90 °C.
Indexed as
Identifiers
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.